---
_id: '8094'
abstract:
- lang: eng
  text: 'With the accelerated development of robot technologies, optimal control becomes
    one of the central themes of research. In traditional approaches, the controller,
    by its internal functionality, finds appropriate actions on the basis of the history
    of sensor values, guided by the goals, intentions, objectives, learning schemes,
    and so forth. The idea is that the controller controls the world---the body plus
    its environment---as reliably as possible. This paper focuses on new lines of
    self-organization for developmental robotics. We apply the recently developed
    differential extrinsic synaptic plasticity to a muscle-tendon driven arm-shoulder
    system from the Myorobotics toolkit. In the experiments, we observe a vast variety
    of self-organized behavior patterns: when left alone, the arm realizes pseudo-random
    sequences of different poses. By applying physical forces, the system can be entrained
    into definite motion patterns like wiping a table. Most interestingly, after attaching
    an object, the controller gets in a functional resonance with the object''s internal
    dynamics, starting to shake spontaneously bottles half-filled with water or sensitively
    driving an attached pendulum into a circular mode. When attached to the crank
    of a wheel the neural system independently discovers how to rotate it. In this
    way, the robot discovers affordances of objects its body is interacting with.'
article_processing_charge: No
author:
- first_name: Georg S
  full_name: Martius, Georg S
  id: 3A276B68-F248-11E8-B48F-1D18A9856A87
  last_name: Martius
- first_name: Rafael
  full_name: Hostettler, Rafael
  last_name: Hostettler
- first_name: Alois
  full_name: Knoll, Alois
  last_name: Knoll
- first_name: Ralf
  full_name: Der, Ralf
  last_name: Der
citation:
  ama: 'Martius GS, Hostettler R, Knoll A, Der R. Self-organized control of an tendon
    driven arm by differential extrinsic plasticity. In: <i>15th International Conference
    on the Synthesis and Simulation of Living Systems</i>. Vol 28. MIT Press; 2016:142-143.
    doi:<a href="https://doi.org/10.7551/978-0-262-33936-0-ch029">10.7551/978-0-262-33936-0-ch029</a>'
  apa: 'Martius, G. S., Hostettler, R., Knoll, A., &#38; Der, R. (2016). Self-organized
    control of an tendon driven arm by differential extrinsic plasticity. In <i>15th
    International Conference on the Synthesis and Simulation of Living Systems</i>
    (Vol. 28, pp. 142–143). Cancun, Mexico: MIT Press. <a href="https://doi.org/10.7551/978-0-262-33936-0-ch029">https://doi.org/10.7551/978-0-262-33936-0-ch029</a>'
  chicago: Martius, Georg S, Rafael Hostettler, Alois Knoll, and Ralf Der. “Self-Organized
    Control of an Tendon Driven Arm by Differential Extrinsic Plasticity.” In <i>15th
    International Conference on the Synthesis and Simulation of Living Systems</i>,
    28:142–43. MIT Press, 2016. <a href="https://doi.org/10.7551/978-0-262-33936-0-ch029">https://doi.org/10.7551/978-0-262-33936-0-ch029</a>.
  ieee: G. S. Martius, R. Hostettler, A. Knoll, and R. Der, “Self-organized control
    of an tendon driven arm by differential extrinsic plasticity,” in <i>15th International
    Conference on the Synthesis and Simulation of Living Systems</i>, Cancun, Mexico,
    2016, vol. 28, pp. 142–143.
  ista: 'Martius GS, Hostettler R, Knoll A, Der R. 2016. Self-organized control of
    an tendon driven arm by differential extrinsic plasticity. 15th International
    Conference on the Synthesis and Simulation of Living Systems. ALIFE 2016: Conference
    on the Synthesis and Simulation of Living Systems vol. 28, 142–143.'
  mla: Martius, Georg S., et al. “Self-Organized Control of an Tendon Driven Arm by
    Differential Extrinsic Plasticity.” <i>15th International Conference on the Synthesis
    and Simulation of Living Systems</i>, vol. 28, MIT Press, 2016, pp. 142–43, doi:<a
    href="https://doi.org/10.7551/978-0-262-33936-0-ch029">10.7551/978-0-262-33936-0-ch029</a>.
  short: G.S. Martius, R. Hostettler, A. Knoll, R. Der, in:, 15th International Conference
    on the Synthesis and Simulation of Living Systems, MIT Press, 2016, pp. 142–143.
conference:
  end_date: 2016-07-08
  location: Cancun, Mexico
  name: 'ALIFE 2016: Conference on the Synthesis and Simulation of Living Systems'
  start_date: 2016-07-04
corr_author: '1'
date_created: 2020-07-05T22:00:47Z
date_published: 2016-09-01T00:00:00Z
date_updated: 2025-07-10T11:55:05Z
day: '01'
ddc:
- '610'
department:
- _id: ChLa
- _id: GaTk
doi: 10.7551/978-0-262-33936-0-ch029
ec_funded: 1
file:
- access_level: open_access
  checksum: cff63e7a4b8ac466ba51a9c84153a940
  content_type: application/pdf
  creator: cziletti
  date_created: 2020-07-06T12:59:09Z
  date_updated: 2020-07-14T12:48:09Z
  file_id: '8096'
  file_name: 2016_ProcALIFE_Martius.pdf
  file_size: 678670
  relation: main_file
file_date_updated: 2020-07-14T12:48:09Z
has_accepted_license: '1'
intvolume: '        28'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: 142-143
project:
- _id: 25681D80-B435-11E9-9278-68D0E5697425
  call_identifier: FP7
  grant_number: '291734'
  name: International IST Postdoc Fellowship Programme
publication: 15th International Conference on the Synthesis and Simulation of Living
  Systems
publication_identifier:
  isbn:
  - '9780262339360'
publication_status: published
publisher: MIT Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Self-organized control of an tendon driven arm by differential extrinsic plasticity
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 28
year: '2016'
...
---
_id: '8128'
abstract:
- lang: eng
  text: The stimulus selectivity of synaptic currents in cortical neurons often shows
    a co-tuning of excitation and inhibition, but the mechanisms that underlie the
    emergence and plasticity of this co-tuning are not fully understood. Using a computational
    model, we show that an interaction of excitatory and inhibitory synaptic plasticity
    reproduces both the developmental and – when combined with a disinhibitory gate
    – the adult plasticity of excitatory and inhibitory receptive fields in auditory
    cortex. The co-tuning arises from inhibitory plasticity that balances excitation
    and inhibition, while excitatory stimulus selectivity can result from two different
    mechanisms. Inhibitory inputs with a broad stimulus tuning introduce a sliding
    threshold as in Bienenstock-Cooper-Munro rules, introducing an excitatory stimulus
    selectivity at the cost of a broader inhibitory receptive field. Alternatively,
    input asymmetries can be amplified by synaptic competition. The latter leaves
    any receptive field plasticity transient, a prediction we verify in recordings
    in auditory cortex.
article_processing_charge: No
author:
- first_name: Claudia
  full_name: Clopath, Claudia
  last_name: Clopath
- first_name: Tim P
  full_name: Vogels, Tim P
  id: CB6FF8D2-008F-11EA-8E08-2637E6697425
  last_name: Vogels
  orcid: 0000-0003-3295-6181
- first_name: Robert C.
  full_name: Froemke, Robert C.
  last_name: Froemke
- first_name: Henning
  full_name: Sprekeler, Henning
  last_name: Sprekeler
citation:
  ama: Clopath C, Vogels TP, Froemke RC, Sprekeler H. Receptive field formation by
    interacting excitatory and inhibitory synaptic plasticity. <i>bioRxiv</i>. 2016.
  apa: Clopath, C., Vogels, T. P., Froemke, R. C., &#38; Sprekeler, H. (2016). Receptive
    field formation by interacting excitatory and inhibitory synaptic plasticity.
    <i>bioRxiv</i>. Cold Spring Harbor Laboratory.
  chicago: Clopath, Claudia, Tim P Vogels, Robert C. Froemke, and Henning Sprekeler.
    “Receptive Field Formation by Interacting Excitatory and Inhibitory Synaptic Plasticity.”
    <i>BioRxiv</i>. Cold Spring Harbor Laboratory, 2016.
  ieee: C. Clopath, T. P. Vogels, R. C. Froemke, and H. Sprekeler, “Receptive field
    formation by interacting excitatory and inhibitory synaptic plasticity,” <i>bioRxiv</i>.
    Cold Spring Harbor Laboratory, 2016.
  ista: Clopath C, Vogels TP, Froemke RC, Sprekeler H. 2016. Receptive field formation
    by interacting excitatory and inhibitory synaptic plasticity. bioRxiv, .
  mla: Clopath, Claudia, et al. “Receptive Field Formation by Interacting Excitatory
    and Inhibitory Synaptic Plasticity.” <i>BioRxiv</i>, Cold Spring Harbor Laboratory,
    2016.
  short: C. Clopath, T.P. Vogels, R.C. Froemke, H. Sprekeler, BioRxiv (2016).
date_created: 2020-07-16T12:26:55Z
date_published: 2016-07-29T00:00:00Z
date_updated: 2021-01-12T08:17:02Z
day: '29'
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: 'https://doi.org/10.1101/066589 '
month: '07'
oa: 1
oa_version: Preprint
page: '43'
publication: bioRxiv
publication_status: published
publisher: Cold Spring Harbor Laboratory
status: public
title: Receptive field formation by interacting excitatory and inhibitory synaptic
  plasticity
type: preprint
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
year: '2016'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '813'
abstract:
- lang: eng
  text: The Gag polyprotein of retroviruses drives immature virus assembly by forming
    hexameric protein lattices. The assembly is primarily mediated by protein-protein
    interactions between capsid (CA) domains and by interactions between nucleocapsid
    (NC) domains and RNA. Specific interactions between NC and the viral RNA are required
    for genome packaging. Previously reported cryoelectron microscopy analysis of
    immature Mason-Pfizer monkey virus (M-PMV) particles suggested that a basic region
    (residues RKK) in CA may serve as an additional binding site for nucleic acids.
    Here, we have introduced mutations into the RKK region in both bacterial and proviral
    M-PMV vectors and have assessed their impact on M-PMV assembly, structure, RNA
    binding, budding/release, nuclear trafficking, and infectivity using in vitro
    and in vivo systems. Our data indicate that the RKK region binds and structures
    nucleic acid that serves to promote virus particle assembly in the cytoplasm.
    Moreover, the RKK region appears to be important for recruitment of viral genomic
    RNA into Gag particles, and this function could be linked to changes in nuclear
    trafficking. Together these observations suggest that in M-PMV, direct interactions
    between CA and nucleic acid play important functions in the late stages of the
    viral life cycle.
acknowledgement: "Work in the laboratory of John A. G. Briggs was funded by Deutsche\r\nForschungsgemeinschaft
  (DFG) (BR 3635/2-1). This work, including the\r\nefforts of Tomas Ruml, was funded
  by the Grant Agency of the Czech\r\nRepublic (14-15326S) and the Czech Ministry
  of Education (NPU I sus-\r\ntainability projects LO1302 and LO1304)."
article_processing_charge: No
article_type: original
author:
- first_name: Tibor
  full_name: Füzik, Tibor
  last_name: Füzik
- first_name: Růžena
  full_name: Píchalová, Růžena
  last_name: Píchalová
- first_name: Florian
  full_name: Schur, Florian
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
- first_name: Karolína
  full_name: Strohalmová, Karolína
  last_name: Strohalmová
- first_name: Ivana
  full_name: Křížová, Ivana
  last_name: Křížová
- first_name: Romana
  full_name: Hadravová, Romana
  last_name: Hadravová
- first_name: Michaela
  full_name: Rumlová, Michaela
  last_name: Rumlová
- first_name: John
  full_name: Briggs, John
  last_name: Briggs
- first_name: Pavel
  full_name: Ulbrich, Pavel
  last_name: Ulbrich
- first_name: Tomáš
  full_name: Ruml, Tomáš
  last_name: Ruml
citation:
  ama: Füzik T, Píchalová R, Schur FK, et al. Nucleic acid binding by Mason-Pfizer
    monkey virus CA promotes virus assembly and genome packaging. <i>Journal of Virology</i>.
    2016;90(9):4593-4603. doi:<a href="https://doi.org/10.1128/JVI.03197-15">10.1128/JVI.03197-15</a>
  apa: Füzik, T., Píchalová, R., Schur, F. K., Strohalmová, K., Křížová, I., Hadravová,
    R., … Ruml, T. (2016). Nucleic acid binding by Mason-Pfizer monkey virus CA promotes
    virus assembly and genome packaging. <i>Journal of Virology</i>. American Society
    for Microbiology. <a href="https://doi.org/10.1128/JVI.03197-15">https://doi.org/10.1128/JVI.03197-15</a>
  chicago: Füzik, Tibor, Růžena Píchalová, Florian KM Schur, Karolína Strohalmová,
    Ivana Křížová, Romana Hadravová, Michaela Rumlová, John Briggs, Pavel Ulbrich,
    and Tomáš Ruml. “Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes
    Virus Assembly and Genome Packaging.” <i>Journal of Virology</i>. American Society
    for Microbiology, 2016. <a href="https://doi.org/10.1128/JVI.03197-15">https://doi.org/10.1128/JVI.03197-15</a>.
  ieee: T. Füzik <i>et al.</i>, “Nucleic acid binding by Mason-Pfizer monkey virus
    CA promotes virus assembly and genome packaging,” <i>Journal of Virology</i>,
    vol. 90, no. 9. American Society for Microbiology, pp. 4593–4603, 2016.
  ista: Füzik T, Píchalová R, Schur FK, Strohalmová K, Křížová I, Hadravová R, Rumlová
    M, Briggs J, Ulbrich P, Ruml T. 2016. Nucleic acid binding by Mason-Pfizer monkey
    virus CA promotes virus assembly and genome packaging. Journal of Virology. 90(9),
    4593–4603.
  mla: Füzik, Tibor, et al. “Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA
    Promotes Virus Assembly and Genome Packaging.” <i>Journal of Virology</i>, vol.
    90, no. 9, American Society for Microbiology, 2016, pp. 4593–603, doi:<a href="https://doi.org/10.1128/JVI.03197-15">10.1128/JVI.03197-15</a>.
  short: T. Füzik, R. Píchalová, F.K. Schur, K. Strohalmová, I. Křížová, R. Hadravová,
    M. Rumlová, J. Briggs, P. Ulbrich, T. Ruml, Journal of Virology 90 (2016) 4593–4603.
date_created: 2018-12-11T11:48:38Z
date_published: 2016-05-01T00:00:00Z
date_updated: 2026-05-20T07:34:00Z
day: '01'
doi: 10.1128/JVI.03197-15
extern: '1'
external_id:
  pmid:
  - '26912613'
intvolume: '        90'
issue: '9'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1128/jvi.03197-15
month: '05'
oa: 1
oa_version: Published Version
page: 4593 - 4603
pmid: 1
publication: Journal of Virology
publication_identifier:
  eissn:
  - 1098-5514
  issn:
  - 0022-538X
publication_status: published
publisher: American Society for Microbiology
publist_id: '6835'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly
  and genome packaging
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 90
year: '2016'
...
---
_id: '816'
abstract:
- lang: eng
  text: Immature HIV-1 assembles at and buds from the plasma membrane before proteolytic
    cleavage of the viral Gag polyprotein induces structural maturation. Maturation
    can be blocked by maturation inhibitors (MIs), thereby abolishing infectivity.
    The CA (capsid) and SP1 (spacer peptide 1) region of Gag is the key regulator
    of assembly and maturation and is the target of MIs.We applied optimized cryo-electron
    tomography and subtomogram averaging to resolve this region within assembled immature
    HIV-1 particles at 3.9 angstrom resolution and built an atomic model. The structure
    reveals a network of intra- And intermolecular interactions mediating immature
    HIV-1 assembly. The proteolytic cleavage site between CA and SP1 is inaccessible
    to protease.We suggest that MIs prevent CA-SP1 cleavage by stabilizing the structure,
    and MI resistance develops by destabilizing CA-SP1.
acknowledgement: The authors thank B. Glass for preparation of the immature HIV-1
  (D25A) sample; J. Plitzko and D. Tegunov for providing the K2Align software; and
  S. Mattei, N. Hoffman, F. Thommen, A. Sonnen, and S. Dodonova for technical assistance
  and/or discussion. This study was supported by Deutsche Forschungsgemeinschaft grants
  BR 3635/2-1 (to J.A.G.B.) and KR 906/7-1 (to H.-G.K.). The Briggs laboratory acknowledges
  financial support from the European Molecular Biology Laboratory (EMBL) and from
  the Chica und Heinz Schaller Stiftung. W.W. was supported by a European Molecular
  Biology Organization Long-Term Fellowship (ALTF 748-2014). A.J.J. acknowledges support
  by the EMBL Interdisciplinary Postdoc Program under the Marie Curie Action COFUND
  (PCOFUND-GA-2008-229597) and by the Joachim Herz Stiftung. This study was technically
  supported by the EMBL information technology services unit and the EMBL Proteomics
  Core Facility. F.K.M.S., M.O., H.-G.K., and J.A.G.B. designed the experiments, with
  J.M.K. assisting in the design of those involving mass spectrometry. F.K.M.S. and
  M.O. prepared samples. W.J.H.H. implemented tomography acquisition schemes. F.K.M.S.
  and W.J.H.H. acquired the data. F.K.M.S. and W.W. processed images. F.K.M.S., A.J.J.,
  and C.S. refined the model. F.K.M.S., M.O., and J.A.G.B. analyzed the data. F.K.M.S.
  and J.A.G.B. wrote the manuscript with support from all authors. Representative
  tomograms and the final electron microscopy structures have been deposited in the
  Electron Microscopy Data Bank with accession numbers EMD-4015, EMD-4016, EMD-4017,
  EMD-4018, EMD-4019, and EMD-4020. The refined HIV-1 CA-SP1 model has been deposited
  in the Protein Data Bank with accession number 5L93.
article_processing_charge: No
author:
- first_name: Florian
  full_name: Schur, Florian
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
- first_name: Martin
  full_name: Obr, Martin
  id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
  last_name: Obr
  orcid: 0000-0003-1756-6564
- first_name: Wim
  full_name: Hagen, Wim
  last_name: Hagen
- first_name: William
  full_name: Wan, William
  last_name: Wan
- first_name: Arjen
  full_name: Jakobi, Arjen
  last_name: Jakobi
- first_name: Joanna
  full_name: Kirkpatrick, Joanna
  last_name: Kirkpatrick
- first_name: Carsten
  full_name: Sachse, Carsten
  last_name: Sachse
- first_name: Hans
  full_name: Kraüsslich, Hans
  last_name: Kraüsslich
- first_name: John
  full_name: Briggs, John
  last_name: Briggs
citation:
  ama: Schur FK, Obr M, Hagen W, et al. <i>An Atomic Model of HIV-1 Capsid-SP1 Reveals
    Structures Regulating Assembly and Maturation</i>. Vol 353. American Association
    for the Advancement of Science; 2016:506-508. doi:<a href="https://doi.org/10.1126/science.aaf9620">10.1126/science.aaf9620</a>
  apa: Schur, F. K., Obr, M., Hagen, W., Wan, W., Jakobi, A., Kirkpatrick, J., … Briggs,
    J. (2016). <i>An atomic model of HIV-1 capsid-SP1 reveals structures regulating
    assembly and maturation</i> (Vol. 353, pp. 506–508). American Association for
    the Advancement of Science. <a href="https://doi.org/10.1126/science.aaf9620">https://doi.org/10.1126/science.aaf9620</a>
  chicago: Schur, Florian KM, Martin Obr, Wim Hagen, William Wan, Arjen Jakobi, Joanna
    Kirkpatrick, Carsten Sachse, Hans Kraüsslich, and John Briggs. <i>An Atomic Model
    of HIV-1 Capsid-SP1 Reveals Structures Regulating Assembly and Maturation</i>.
    Vol. 353. American Association for the Advancement of Science, 2016. <a href="https://doi.org/10.1126/science.aaf9620">https://doi.org/10.1126/science.aaf9620</a>.
  ieee: F. K. Schur <i>et al.</i>, <i>An atomic model of HIV-1 capsid-SP1 reveals
    structures regulating assembly and maturation</i>, vol. 353. American Association
    for the Advancement of Science, 2016, pp. 506–508.
  ista: Schur FK, Obr M, Hagen W, Wan W, Jakobi A, Kirkpatrick J, Sachse C, Kraüsslich
    H, Briggs J. 2016. An atomic model of HIV-1 capsid-SP1 reveals structures regulating
    assembly and maturation, American Association for the Advancement of Science,p.
  mla: Schur, Florian KM, et al. <i>An Atomic Model of HIV-1 Capsid-SP1 Reveals Structures
    Regulating Assembly and Maturation</i>. Vol. 353, American Association for the
    Advancement of Science, 2016, pp. 506–08, doi:<a href="https://doi.org/10.1126/science.aaf9620">10.1126/science.aaf9620</a>.
  short: F.K. Schur, M. Obr, W. Hagen, W. Wan, A. Jakobi, J. Kirkpatrick, C. Sachse,
    H. Kraüsslich, J. Briggs, An Atomic Model of HIV-1 Capsid-SP1 Reveals Structures
    Regulating Assembly and Maturation, American Association for the Advancement of
    Science, 2016.
date_created: 2018-12-11T11:48:39Z
date_published: 2016-07-29T00:00:00Z
date_updated: 2026-05-20T07:41:16Z
day: '29'
doi: 10.1126/science.aaf9620
extern: '1'
external_id:
  pmid:
  - '27417497'
intvolume: '       353'
language:
- iso: eng
month: '07'
oa_version: None
page: 506 - 508
pmid: 1
publication_identifier:
  eissn:
  - 1095-9203
  issn:
  - 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
publist_id: '6834'
scopus_import: '1'
status: public
title: An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly
  and maturation
type: report
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 353
year: '2016'
...
---
_id: '8241'
abstract:
- lang: eng
  text: 'Background: Anticancer vaccines could represent a valuable complementary
    strategy to established therapies, especially in settings of early stage and minimal
    residual disease. HER-2 is an important target for immunotherapy and addressed
    by the monoclonal antibody trastuzumab. We have previously generated HER-2 mimotope
    peptides from phage display libraries. The synthesized peptides were coupled to
    carriers and applied for epitope-specific induction of trastuzumab-like IgG. For
    simplification and to avoid methodological limitations of synthesis and coupling
    chemistry, we herewith present a novel and optimized approach by using adeno-associated
    viruses (AAV) as effective and high-density mimotope-display system, which can
    be directly used for vaccination. Methods: An AAV capsid display library was constructed
    by genetically incorporating random peptides in a plasmid encoding the wild-type
    AAV2 capsid protein. AAV clones, expressing peptides specifically reactive to
    trastuzumab, were employed to immunize BALB/c mice. Antibody titers against human
    HER-2 were determined, and the isotype composition and functional properties of
    these were tested. Finally, prophylactically immunized mice were challenged with
    human HER-2 transfected mouse D2F2/E2 cells. Results: HER-2 mimotope AAV-vaccines
    induced antibodies specific to human HER-2. Two clones were selected for immunization
    of mice, which were subsequently grafted D2F2/E2 cells. Both mimotope AAV clones
    delayed the growth of tumors significantly, as compared to controls. Conclusion:
    In this study, a novel mimotope AAV-based platform was created allowing the isolation
    of mimotopes, which can be directly used as anticancer vaccines. The example of
    trastuzumab AAV-mimotopes demonstrates that this vaccine strategy could help to
    establish active immunotherapy for breast-cancer patients.'
article_number: e1171446
article_processing_charge: No
article_type: original
author:
- first_name: Josef
  full_name: Singer, Josef
  last_name: Singer
- first_name: Krisztina
  full_name: Manzano-Szalai, Krisztina
  last_name: Manzano-Szalai
- first_name: Judit
  full_name: Fazekas, Judit
  id: 36432834-F248-11E8-B48F-1D18A9856A87
  last_name: Fazekas
  orcid: 0000-0002-8777-3502
- first_name: Kathrin
  full_name: Thell, Kathrin
  last_name: Thell
- first_name: Anna
  full_name: Bentley-Lukschal, Anna
  last_name: Bentley-Lukschal
- first_name: Caroline
  full_name: Stremnitzer, Caroline
  last_name: Stremnitzer
- first_name: Franziska
  full_name: Roth-Walter, Franziska
  last_name: Roth-Walter
- first_name: Margit
  full_name: Weghofer, Margit
  last_name: Weghofer
- first_name: Mirko
  full_name: Ritter, Mirko
  last_name: Ritter
- first_name: Kerstin
  full_name: Pino Tossi, Kerstin
  last_name: Pino Tossi
- first_name: Markus
  full_name: Hörer, Markus
  last_name: Hörer
- first_name: Uwe
  full_name: Michaelis, Uwe
  last_name: Michaelis
- first_name: Erika
  full_name: Jensen-Jarolim, Erika
  last_name: Jensen-Jarolim
citation:
  ama: Singer J, Manzano-Szalai K, Singer J, et al. Proof of concept study with an
    HER-2 mimotope anticancer vaccine deduced from a novel AAV-mimotope library platform.
    <i>OncoImmunology</i>. 2016;5(7). doi:<a href="https://doi.org/10.1080/2162402x.2016.1171446">10.1080/2162402x.2016.1171446</a>
  apa: Singer, J., Manzano-Szalai, K., Singer, J., Thell, K., Bentley-Lukschal, A.,
    Stremnitzer, C., … Jensen-Jarolim, E. (2016). Proof of concept study with an HER-2
    mimotope anticancer vaccine deduced from a novel AAV-mimotope library platform.
    <i>OncoImmunology</i>. Taylor &#38; Francis. <a href="https://doi.org/10.1080/2162402x.2016.1171446">https://doi.org/10.1080/2162402x.2016.1171446</a>
  chicago: Singer, Josef, Krisztina Manzano-Szalai, Judit Singer, Kathrin Thell, Anna
    Bentley-Lukschal, Caroline Stremnitzer, Franziska Roth-Walter, et al. “Proof of
    Concept Study with an HER-2 Mimotope Anticancer Vaccine Deduced from a Novel AAV-Mimotope
    Library Platform.” <i>OncoImmunology</i>. Taylor &#38; Francis, 2016. <a href="https://doi.org/10.1080/2162402x.2016.1171446">https://doi.org/10.1080/2162402x.2016.1171446</a>.
  ieee: J. Singer <i>et al.</i>, “Proof of concept study with an HER-2 mimotope anticancer
    vaccine deduced from a novel AAV-mimotope library platform,” <i>OncoImmunology</i>,
    vol. 5, no. 7. Taylor &#38; Francis, 2016.
  ista: Singer J, Manzano-Szalai K, Singer J, Thell K, Bentley-Lukschal A, Stremnitzer
    C, Roth-Walter F, Weghofer M, Ritter M, Pino Tossi K, Hörer M, Michaelis U, Jensen-Jarolim
    E. 2016. Proof of concept study with an HER-2 mimotope anticancer vaccine deduced
    from a novel AAV-mimotope library platform. OncoImmunology. 5(7), e1171446.
  mla: Singer, Josef, et al. “Proof of Concept Study with an HER-2 Mimotope Anticancer
    Vaccine Deduced from a Novel AAV-Mimotope Library Platform.” <i>OncoImmunology</i>,
    vol. 5, no. 7, e1171446, Taylor &#38; Francis, 2016, doi:<a href="https://doi.org/10.1080/2162402x.2016.1171446">10.1080/2162402x.2016.1171446</a>.
  short: J. Singer, K. Manzano-Szalai, J. Singer, K. Thell, A. Bentley-Lukschal, C.
    Stremnitzer, F. Roth-Walter, M. Weghofer, M. Ritter, K. Pino Tossi, M. Hörer,
    U. Michaelis, E. Jensen-Jarolim, OncoImmunology 5 (2016).
date_created: 2020-08-10T11:54:03Z
date_published: 2016-06-30T00:00:00Z
date_updated: 2021-01-12T08:17:41Z
day: '30'
doi: 10.1080/2162402x.2016.1171446
extern: '1'
intvolume: '         5'
issue: '7'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1080/2162402X.2016.1171446
month: '06'
oa: 1
oa_version: Published Version
publication: OncoImmunology
publication_identifier:
  issn:
  - 2162-402X
publication_status: published
publisher: Taylor & Francis
quality_controlled: '1'
status: public
title: Proof of concept study with an HER-2 mimotope anticancer vaccine deduced from
  a novel AAV-mimotope library platform
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2016'
...
---
_id: '8300'
abstract:
- lang: eng
  text: The integration of social networking concepts into Internet of Things systems
    is a burgeoning topic of research that promises to support novel and more powerful
    applications. In this paper we focus on the design and implementation of a highly
    scalable Trust and Reputation Model for the Internet of Things based on the social
    approach that the COSMOS project introduces, as part of its final results. We
    create our model by combining popular solutions proposed for Peer-to-Peer and
    mobile ad-hoc networks and adapting them on the Internet of Things concept. Each
    Thing can compute the Trust index of another Thing based on its own experiences,
    while it has the capability of determining its Reputation Index either by consulting
    its other “friends” (Followees) or referring to the Platform, a management system
    used in COSMOS. The model is tested through simulations of the proposed social
    system, demonstrating the ability of TRM-SIoT to achieve the Social Exclusion
    of malicious nodes and collectives from the network, with low computational overhead
    and high scalability. Furthermore, due to the adaptive nature of the system, Social
    Reintegration of these nodes is also possible.
article_number: '7733612'
article_processing_charge: No
author:
- first_name: Eleftherios
  full_name: Kokoris Kogias, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: Kokoris Kogias
- first_name: Orfefs
  full_name: Voutyras, Orfefs
  last_name: Voutyras
- first_name: Theodora
  full_name: Varvarigou, Theodora
  last_name: Varvarigou
citation:
  ama: 'Kokoris Kogias E, Voutyras O, Varvarigou T. TRM-SIoT: A scalable hybrid trust
    &#38; reputation model for the social Internet of Things. In: <i>2016 IEEE 21st
    International Conference on Emerging Technologies and Factory Automation</i>.
    IEEE; 2016. doi:<a href="https://doi.org/10.1109/etfa.2016.7733612">10.1109/etfa.2016.7733612</a>'
  apa: 'Kokoris Kogias, E., Voutyras, O., &#38; Varvarigou, T. (2016). TRM-SIoT: A
    scalable hybrid trust &#38; reputation model for the social Internet of Things.
    In <i>2016 IEEE 21st International Conference on Emerging Technologies and Factory
    Automation</i>. Berlin, Germany: IEEE. <a href="https://doi.org/10.1109/etfa.2016.7733612">https://doi.org/10.1109/etfa.2016.7733612</a>'
  chicago: 'Kokoris Kogias, Eleftherios, Orfefs Voutyras, and Theodora Varvarigou.
    “TRM-SIoT: A Scalable Hybrid Trust &#38; Reputation Model for the Social Internet
    of Things.” In <i>2016 IEEE 21st International Conference on Emerging Technologies
    and Factory Automation</i>. IEEE, 2016. <a href="https://doi.org/10.1109/etfa.2016.7733612">https://doi.org/10.1109/etfa.2016.7733612</a>.'
  ieee: 'E. Kokoris Kogias, O. Voutyras, and T. Varvarigou, “TRM-SIoT: A scalable
    hybrid trust &#38; reputation model for the social Internet of Things,” in <i>2016
    IEEE 21st International Conference on Emerging Technologies and Factory Automation</i>,
    Berlin, Germany, 2016.'
  ista: 'Kokoris Kogias E, Voutyras O, Varvarigou T. 2016. TRM-SIoT: A scalable hybrid
    trust &#38; reputation model for the social Internet of Things. 2016 IEEE 21st
    International Conference on Emerging Technologies and Factory Automation. ETFA:
    Conference on Emerging Technologies and Factory Automation, 7733612.'
  mla: 'Kokoris Kogias, Eleftherios, et al. “TRM-SIoT: A Scalable Hybrid Trust &#38;
    Reputation Model for the Social Internet of Things.” <i>2016 IEEE 21st International
    Conference on Emerging Technologies and Factory Automation</i>, 7733612, IEEE,
    2016, doi:<a href="https://doi.org/10.1109/etfa.2016.7733612">10.1109/etfa.2016.7733612</a>.'
  short: E. Kokoris Kogias, O. Voutyras, T. Varvarigou, in:, 2016 IEEE 21st International
    Conference on Emerging Technologies and Factory Automation, IEEE, 2016.
conference:
  end_date: 2016-09-09
  location: Berlin, Germany
  name: 'ETFA: Conference on Emerging Technologies and Factory Automation'
  start_date: 2016-09-06
date_created: 2020-08-26T11:48:54Z
date_published: 2016-09-09T00:00:00Z
date_updated: 2021-01-12T08:17:59Z
day: '09'
doi: 10.1109/etfa.2016.7733612
extern: '1'
language:
- iso: eng
month: '09'
oa_version: None
publication: 2016 IEEE 21st International Conference on Emerging Technologies and
  Factory Automation
publication_identifier:
  isbn:
  - '9781509013142'
publication_status: published
publisher: IEEE
quality_controlled: '1'
status: public
title: 'TRM-SIoT: A scalable hybrid trust & reputation model for the social Internet
  of Things'
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2016'
...
---
_id: '8302'
abstract:
- lang: eng
  text: While showing great promise, Bitcoin requires users to wait tens of minutes
    for transactions to commit, and even then, offering only probabilistic guarantees.
    This paper introduces ByzCoin, a novel Byzantine consensus protocol that leverages
    scalable collective signing to commit Bitcoin transactions irreversibly within
    seconds. ByzCoin achieves Byzantine consensus while preserving Bitcoin’s open
    membership by dynamically forming hash power-proportionate consensus groups that
    represent recently-successful block miners. ByzCoin employs communication trees
    to optimize transaction commitment and verification under normal operation while
    guaranteeing safety and liveness under Byzantine faults, up to a near-optimal
    tolerance of f faulty group members among 3f + 2 total. ByzCoin mitigates double
    spending and selfish mining attacks by producing collectively signed transaction
    blocks within one minute of transaction submission. Tree-structured communication
    further reduces this latency to less than 30 seconds. Due to these optimizations,
    ByzCoin achieves a throughput higher than Paypal currently handles, with a confirmation
    latency of 15-20 seconds.
article_processing_charge: No
arxiv: 1
author:
- first_name: Eleftherios
  full_name: Kokoris Kogias, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: Kokoris Kogias
- first_name: Philipp
  full_name: Jovanovic, Philipp
  last_name: Jovanovic
- first_name: Nicolas
  full_name: Gailly, Nicolas
  last_name: Gailly
- first_name: Ismail
  full_name: Khoffi, Ismail
  last_name: Khoffi
- first_name: Linus
  full_name: Gasser, Linus
  last_name: Gasser
- first_name: Bryan
  full_name: Ford, Bryan
  last_name: Ford
citation:
  ama: 'Kokoris Kogias E, Jovanovic P, Gailly N, Khoffi I, Gasser L, Ford B. Enhancing
    bitcoin security and performance with strong consistency via collective signing.
    In: <i>Proceedings of the 25th USENIX Conference on Security Symposium</i>. USENIX
    Association; 2016:279–296.'
  apa: 'Kokoris Kogias, E., Jovanovic, P., Gailly, N., Khoffi, I., Gasser, L., &#38;
    Ford, B. (2016). Enhancing bitcoin security and performance with strong consistency
    via collective signing. In <i>Proceedings of the 25th USENIX Conference on Security
    Symposium</i> (pp. 279–296). Austin, TX, United States: USENIX Association.'
  chicago: Kokoris Kogias, Eleftherios, Philipp Jovanovic, Nicolas Gailly, Ismail
    Khoffi, Linus Gasser, and Bryan Ford. “Enhancing Bitcoin Security and Performance
    with Strong Consistency via Collective Signing.” In <i>Proceedings of the 25th
    USENIX Conference on Security Symposium</i>, 279–296. USENIX Association, 2016.
  ieee: E. Kokoris Kogias, P. Jovanovic, N. Gailly, I. Khoffi, L. Gasser, and B. Ford,
    “Enhancing bitcoin security and performance with strong consistency via collective
    signing,” in <i>Proceedings of the 25th USENIX Conference on Security Symposium</i>,
    Austin, TX, United States, 2016, pp. 279–296.
  ista: 'Kokoris Kogias E, Jovanovic P, Gailly N, Khoffi I, Gasser L, Ford B. 2016.
    Enhancing bitcoin security and performance with strong consistency via collective
    signing. Proceedings of the 25th USENIX Conference on Security Symposium. SEC:
    Security Symposium, 279–296.'
  mla: Kokoris Kogias, Eleftherios, et al. “Enhancing Bitcoin Security and Performance
    with Strong Consistency via Collective Signing.” <i>Proceedings of the 25th USENIX
    Conference on Security Symposium</i>, USENIX Association, 2016, pp. 279–296.
  short: E. Kokoris Kogias, P. Jovanovic, N. Gailly, I. Khoffi, L. Gasser, B. Ford,
    in:, Proceedings of the 25th USENIX Conference on Security Symposium, USENIX Association,
    2016, pp. 279–296.
conference:
  end_date: 2016-08-12
  location: Austin, TX, United States
  name: 'SEC: Security Symposium'
  start_date: 2016-08-10
date_created: 2020-08-26T12:08:35Z
date_published: 2016-09-01T00:00:00Z
date_updated: 2021-01-12T08:18:00Z
day: '01'
extern: '1'
external_id:
  arxiv:
  - '1602.06997'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1602.06997
month: '09'
oa: 1
oa_version: Published Version
page: 279–296
publication: Proceedings of the 25th USENIX Conference on Security Symposium
publication_identifier:
  isbn:
  - '9781931971324'
publication_status: published
publisher: USENIX Association
quality_controlled: '1'
status: public
title: Enhancing bitcoin security and performance with strong consistency via collective
  signing
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2016'
...
---
_id: '8452'
abstract:
- lang: eng
  text: During spore formation in Bacillus subtilis a transenvelope complex is assembled
    across the double membrane that separates the mother cell and forespore. This
    complex (called the “A–Q complex”) is required to maintain forespore development
    and is composed of proteins with remote homology to components of type II, III,
    and IV secretion systems found in Gram-negative bacteria. Here, we show that one
    of these proteins, SpoIIIAG, which has remote homology to ring-forming proteins
    found in type III secretion systems, assembles into an oligomeric ring in the
    periplasmic-like space between the two membranes. Three-dimensional reconstruction
    of images generated by cryo-electron microscopy indicates that the SpoIIIAG ring
    has a cup-and-saucer architecture with a 6-nm central pore. Structural modeling
    of SpoIIIAG generated a 24-member ring with dimensions similar to those of the
    EM-derived saucer. Point mutations in the predicted oligomeric interface disrupted
    ring formation in vitro and impaired forespore gene expression and efficient spore
    formation in vivo. Taken together, our data provide strong support for the model
    in which the A–Q transenvelope complex contains a conduit that connects the mother
    cell and forespore. We propose that a set of stacked rings spans the intermembrane
    space, as has been found for type III secretion systems.
article_processing_charge: No
article_type: original
author:
- first_name: Christopher D. A.
  full_name: Rodrigues, Christopher D. A.
  last_name: Rodrigues
- first_name: Xavier
  full_name: Henry, Xavier
  last_name: Henry
- first_name: Emmanuelle
  full_name: Neumann, Emmanuelle
  last_name: Neumann
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Laure
  full_name: Bellard, Laure
  last_name: Bellard
- first_name: Yann
  full_name: Fichou, Yann
  last_name: Fichou
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Guy
  full_name: Schoehn, Guy
  last_name: Schoehn
- first_name: David Z.
  full_name: Rudner, David Z.
  last_name: Rudner
- first_name: Cecile
  full_name: Morlot, Cecile
  last_name: Morlot
citation:
  ama: Rodrigues CDA, Henry X, Neumann E, et al. A ring-shaped conduit connects the
    mother cell and forespore during sporulation in Bacillus subtilis. <i>Proceedings
    of the National Academy of Sciences</i>. 2016;113(41):11585-11590. doi:<a href="https://doi.org/10.1073/pnas.1609604113">10.1073/pnas.1609604113</a>
  apa: Rodrigues, C. D. A., Henry, X., Neumann, E., Kurauskas, V., Bellard, L., Fichou,
    Y., … Morlot, C. (2016). A ring-shaped conduit connects the mother cell and forespore
    during sporulation in Bacillus subtilis. <i>Proceedings of the National Academy
    of Sciences</i>. National Academy of Sciences. <a href="https://doi.org/10.1073/pnas.1609604113">https://doi.org/10.1073/pnas.1609604113</a>
  chicago: Rodrigues, Christopher D. A., Xavier Henry, Emmanuelle Neumann, Vilius
    Kurauskas, Laure Bellard, Yann Fichou, Paul Schanda, Guy Schoehn, David Z. Rudner,
    and Cecile Morlot. “A Ring-Shaped Conduit Connects the Mother Cell and Forespore
    during Sporulation in Bacillus Subtilis.” <i>Proceedings of the National Academy
    of Sciences</i>. National Academy of Sciences, 2016. <a href="https://doi.org/10.1073/pnas.1609604113">https://doi.org/10.1073/pnas.1609604113</a>.
  ieee: C. D. A. Rodrigues <i>et al.</i>, “A ring-shaped conduit connects the mother
    cell and forespore during sporulation in Bacillus subtilis,” <i>Proceedings of
    the National Academy of Sciences</i>, vol. 113, no. 41. National Academy of Sciences,
    pp. 11585–11590, 2016.
  ista: Rodrigues CDA, Henry X, Neumann E, Kurauskas V, Bellard L, Fichou Y, Schanda
    P, Schoehn G, Rudner DZ, Morlot C. 2016. A ring-shaped conduit connects the mother
    cell and forespore during sporulation in Bacillus subtilis. Proceedings of the
    National Academy of Sciences. 113(41), 11585–11590.
  mla: Rodrigues, Christopher D. A., et al. “A Ring-Shaped Conduit Connects the Mother
    Cell and Forespore during Sporulation in Bacillus Subtilis.” <i>Proceedings of
    the National Academy of Sciences</i>, vol. 113, no. 41, National Academy of Sciences,
    2016, pp. 11585–90, doi:<a href="https://doi.org/10.1073/pnas.1609604113">10.1073/pnas.1609604113</a>.
  short: C.D.A. Rodrigues, X. Henry, E. Neumann, V. Kurauskas, L. Bellard, Y. Fichou,
    P. Schanda, G. Schoehn, D.Z. Rudner, C. Morlot, Proceedings of the National Academy
    of Sciences 113 (2016) 11585–11590.
date_created: 2020-09-18T10:06:58Z
date_published: 2016-09-28T00:00:00Z
date_updated: 2021-01-12T08:19:22Z
day: '28'
doi: 10.1073/pnas.1609604113
extern: '1'
intvolume: '       113'
issue: '41'
language:
- iso: eng
month: '09'
oa_version: None
page: 11585-11590
publication: Proceedings of the National Academy of Sciences
publication_identifier:
  issn:
  - 0027-8424
  - 1091-6490
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
status: public
title: A ring-shaped conduit connects the mother cell and forespore during sporulation
  in Bacillus subtilis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 113
year: '2016'
...
---
_id: '8453'
abstract:
- lang: eng
  text: Transverse relaxation rate measurements in magic-angle spinning solid-state
    nuclear magnetic resonance provide information about molecular motions occurring
    on nanosecond-to-millisecond (ns–ms) time scales. The measurement of heteronuclear
    (13C, 15N) relaxation rate constants in the presence of a spin-lock radiofrequency
    field (R1ρ relaxation) provides access to such motions, and an increasing number
    of studies involving R1ρ relaxation in proteins have been reported. However, two
    factors that influence the observed relaxation rate constants have so far been
    neglected, namely, (1) the role of CSA/dipolar cross-correlated relaxation (CCR)
    and (2) the impact of fast proton spin flips (i.e., proton spin diffusion and
    relaxation). We show that CSA/D CCR in R1ρ experiments is measurable and that
    the CCR rate constant depends on ns–ms motions; it can thus provide insight into
    dynamics. We find that proton spin diffusion attenuates this CCR due to its decoupling
    effect on the doublet components. For measurements of dynamics, the use of R1ρ
    rate constants has practical advantages over the use of CCR rates, and this article
    reveals factors that have so far been disregarded and which are important for
    accurate measurements and interpretation.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Emmanuelle
  full_name: Weber, Emmanuelle
  last_name: Weber
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Isabel
  full_name: Ayala, Isabel
  last_name: Ayala
- first_name: Dominique
  full_name: Marion, Dominique
  last_name: Marion
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. Cross-correlated
    relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning
    R1ρ NMR measurements: Application to protein backbone dynamics measurements. <i>The
    Journal of Physical Chemistry B</i>. 2016;120(34):8905-8913. doi:<a href="https://doi.org/10.1021/acs.jpcb.6b06129">10.1021/acs.jpcb.6b06129</a>'
  apa: 'Kurauskas, V., Weber, E., Hessel, A., Ayala, I., Marion, D., &#38; Schanda,
    P. (2016). Cross-correlated relaxation of dipolar coupling and chemical-shift
    anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein
    backbone dynamics measurements. <i>The Journal of Physical Chemistry B</i>. American
    Chemical Society. <a href="https://doi.org/10.1021/acs.jpcb.6b06129">https://doi.org/10.1021/acs.jpcb.6b06129</a>'
  chicago: 'Kurauskas, Vilius, Emmanuelle Weber, Audrey Hessel, Isabel Ayala, Dominique
    Marion, and Paul Schanda. “Cross-Correlated Relaxation of Dipolar Coupling and
    Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application
    to Protein Backbone Dynamics Measurements.” <i>The Journal of Physical Chemistry
    B</i>. American Chemical Society, 2016. <a href="https://doi.org/10.1021/acs.jpcb.6b06129">https://doi.org/10.1021/acs.jpcb.6b06129</a>.'
  ieee: 'V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, and P. Schanda, “Cross-correlated
    relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning
    R1ρ NMR measurements: Application to protein backbone dynamics measurements,”
    <i>The Journal of Physical Chemistry B</i>, vol. 120, no. 34. American Chemical
    Society, pp. 8905–8913, 2016.'
  ista: 'Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. 2016. Cross-correlated
    relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning
    R1ρ NMR measurements: Application to protein backbone dynamics measurements. The
    Journal of Physical Chemistry B. 120(34), 8905–8913.'
  mla: 'Kurauskas, Vilius, et al. “Cross-Correlated Relaxation of Dipolar Coupling
    and Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application
    to Protein Backbone Dynamics Measurements.” <i>The Journal of Physical Chemistry
    B</i>, vol. 120, no. 34, American Chemical Society, 2016, pp. 8905–13, doi:<a
    href="https://doi.org/10.1021/acs.jpcb.6b06129">10.1021/acs.jpcb.6b06129</a>.'
  short: V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, P. Schanda, The Journal
    of Physical Chemistry B 120 (2016) 8905–8913.
date_created: 2020-09-18T10:07:07Z
date_published: 2016-08-08T00:00:00Z
date_updated: 2021-01-12T08:19:22Z
day: '08'
doi: 10.1021/acs.jpcb.6b06129
extern: '1'
intvolume: '       120'
issue: '34'
keyword:
- Physical and Theoretical Chemistry
- Materials Chemistry
- Surfaces
- Coatings and Films
language:
- iso: eng
month: '08'
oa_version: None
page: 8905-8913
publication: The Journal of Physical Chemistry B
publication_identifier:
  issn:
  - 1520-6106
  - 1520-5207
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy
  in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics
  measurements'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2016'
...
---
_id: '8454'
abstract:
- lang: eng
  text: Magic-angle spinning solid-state NMR spectroscopy is an important technique
    to study molecular structure, dynamics and interactions, and is rapidly gaining
    importance in biomolecular sciences. Here we provide an overview of experimental
    approaches to study molecular dynamics by MAS solid-state NMR, with an emphasis
    on the underlying theoretical concepts and differences of MAS solid-state NMR
    compared to solution-state NMR. The theoretical foundations of nuclear spin relaxation
    are revisited, focusing on the particularities of spin relaxation in solid samples
    under magic-angle spinning. We discuss the range of validity of Redfield theory,
    as well as the inherent multi-exponential behavior of relaxation in solids. Experimental
    challenges for measuring relaxation parameters in MAS solid-state NMR and a few
    recently proposed relaxation approaches are discussed, which provide information
    about time scales and amplitudes of motions ranging from picoseconds to milliseconds.
    We also discuss the theoretical basis and experimental measurements of anisotropic
    interactions (chemical-shift anisotropies, dipolar and quadrupolar couplings),
    which give direct information about the amplitude of motions. The potential of
    combining relaxation data with such measurements of dynamically-averaged anisotropic
    interactions is discussed. Although the focus of this review is on the theoretical
    foundations of dynamics studies rather than their application, we close by discussing
    a small number of recent dynamics studies, where the dynamic properties of proteins
    in crystals are compared to those in solution.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Matthias
  full_name: Ernst, Matthias
  last_name: Ernst
citation:
  ama: 'Schanda P, Ernst M. Studying dynamics by magic-angle spinning solid-state
    NMR spectroscopy: Principles and applications to biomolecules. <i>Progress in
    Nuclear Magnetic Resonance Spectroscopy</i>. 2016;96(8):1-46. doi:<a href="https://doi.org/10.1016/j.pnmrs.2016.02.001">10.1016/j.pnmrs.2016.02.001</a>'
  apa: 'Schanda, P., &#38; Ernst, M. (2016). Studying dynamics by magic-angle spinning
    solid-state NMR spectroscopy: Principles and applications to biomolecules. <i>Progress
    in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier. <a href="https://doi.org/10.1016/j.pnmrs.2016.02.001">https://doi.org/10.1016/j.pnmrs.2016.02.001</a>'
  chicago: 'Schanda, Paul, and Matthias Ernst. “Studying Dynamics by Magic-Angle Spinning
    Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.” <i>Progress
    in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier, 2016. <a href="https://doi.org/10.1016/j.pnmrs.2016.02.001">https://doi.org/10.1016/j.pnmrs.2016.02.001</a>.'
  ieee: 'P. Schanda and M. Ernst, “Studying dynamics by magic-angle spinning solid-state
    NMR spectroscopy: Principles and applications to biomolecules,” <i>Progress in
    Nuclear Magnetic Resonance Spectroscopy</i>, vol. 96, no. 8. Elsevier, pp. 1–46,
    2016.'
  ista: 'Schanda P, Ernst M. 2016. Studying dynamics by magic-angle spinning solid-state
    NMR spectroscopy: Principles and applications to biomolecules. Progress in Nuclear
    Magnetic Resonance Spectroscopy. 96(8), 1–46.'
  mla: 'Schanda, Paul, and Matthias Ernst. “Studying Dynamics by Magic-Angle Spinning
    Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.” <i>Progress
    in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 96, no. 8, Elsevier, 2016,
    pp. 1–46, doi:<a href="https://doi.org/10.1016/j.pnmrs.2016.02.001">10.1016/j.pnmrs.2016.02.001</a>.'
  short: P. Schanda, M. Ernst, Progress in Nuclear Magnetic Resonance Spectroscopy
    96 (2016) 1–46.
date_created: 2020-09-18T10:07:17Z
date_published: 2016-08-01T00:00:00Z
date_updated: 2021-01-12T08:19:23Z
day: '01'
doi: 10.1016/j.pnmrs.2016.02.001
extern: '1'
intvolume: '        96'
issue: '8'
language:
- iso: eng
month: '08'
oa_version: None
page: 1-46
publication: Progress in Nuclear Magnetic Resonance Spectroscopy
publication_identifier:
  issn:
  - 0079-6565
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles
  and applications to biomolecules'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 96
year: '2016'
...
---
_id: '8455'
abstract:
- lang: eng
  text: Solid-state NMR spectroscopy allows the characterization of the structure,
    interactions and dynamics of insoluble and/or very large proteins. Sensitivity
    and resolution are often major challenges for obtaining atomic-resolution information,
    in particular for very large protein complexes. Here we show that the use of deuterated,
    specifically CH3-labelled proteins result in significant sensitivity gains compared
    to previously employed CHD2 labelling, while line widths increase only marginally.
    We apply this labelling strategy to a 468 kDa-large dodecameric aminopeptidase,
    TET2, and the 1.6 MDa-large 50S ribosome subunit of Thermus thermophilus.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Elodie
  full_name: Crublet, Elodie
  last_name: Crublet
- first_name: Pavel
  full_name: Macek, Pavel
  last_name: Macek
- first_name: Rime
  full_name: Kerfah, Rime
  last_name: Kerfah
- first_name: Diego F.
  full_name: Gauto, Diego F.
  last_name: Gauto
- first_name: Jérôme
  full_name: Boisbouvier, Jérôme
  last_name: Boisbouvier
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Kurauskas V, Crublet E, Macek P, et al. Sensitive proton-detected solid-state
    NMR spectroscopy of large proteins with selective CH3labelling: Application to
    the 50S ribosome subunit. <i>Chemical Communications</i>. 2016;52(61):9558-9561.
    doi:<a href="https://doi.org/10.1039/c6cc04484k">10.1039/c6cc04484k</a>'
  apa: 'Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier,
    J., &#38; Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy
    of large proteins with selective CH3labelling: Application to the 50S ribosome
    subunit. <i>Chemical Communications</i>. Royal Society of Chemistry. <a href="https://doi.org/10.1039/c6cc04484k">https://doi.org/10.1039/c6cc04484k</a>'
  chicago: 'Kurauskas, Vilius, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F.
    Gauto, Jérôme Boisbouvier, and Paul Schanda. “Sensitive Proton-Detected Solid-State
    NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to
    the 50S Ribosome Subunit.” <i>Chemical Communications</i>. Royal Society of Chemistry,
    2016. <a href="https://doi.org/10.1039/c6cc04484k">https://doi.org/10.1039/c6cc04484k</a>.'
  ieee: 'V. Kurauskas <i>et al.</i>, “Sensitive proton-detected solid-state NMR spectroscopy
    of large proteins with selective CH3labelling: Application to the 50S ribosome
    subunit,” <i>Chemical Communications</i>, vol. 52, no. 61. Royal Society of Chemistry,
    pp. 9558–9561, 2016.'
  ista: 'Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda
    P. 2016. Sensitive proton-detected solid-state NMR spectroscopy of large proteins
    with selective CH3labelling: Application to the 50S ribosome subunit. Chemical
    Communications. 52(61), 9558–9561.'
  mla: 'Kurauskas, Vilius, et al. “Sensitive Proton-Detected Solid-State NMR Spectroscopy
    of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome
    Subunit.” <i>Chemical Communications</i>, vol. 52, no. 61, Royal Society of Chemistry,
    2016, pp. 9558–61, doi:<a href="https://doi.org/10.1039/c6cc04484k">10.1039/c6cc04484k</a>.'
  short: V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier,
    P. Schanda, Chemical Communications 52 (2016) 9558–9561.
date_created: 2020-09-18T10:07:29Z
date_published: 2016-07-04T00:00:00Z
date_updated: 2021-01-12T08:19:23Z
day: '04'
doi: 10.1039/c6cc04484k
extern: '1'
intvolume: '        52'
issue: '61'
keyword:
- Materials Chemistry
- Electronic
- Optical and Magnetic Materials
- General Chemistry
- Surfaces
- Coatings and Films
- Metals and Alloys
- Ceramics and Composites
- Catalysis
language:
- iso: eng
month: '07'
oa_version: None
page: 9558-9561
publication: Chemical Communications
publication_identifier:
  issn:
  - 1359-7345
  - 1364-548X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: 'Sensitive proton-detected solid-state NMR spectroscopy of large proteins with
  selective CH3labelling: Application to the 50S ribosome subunit'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 52
year: '2016'
...
---
OA_place: publisher
OA_type: gold
_id: '849'
abstract:
- lang: eng
  text: Understanding the principles that led to the current complexity of the genetic
    code is a central question in evolution. Expansion of the genetic code required
    the selection of new transfer RNAs (tRNAs) with specific recognition signals that
    allowed them to be matured, modified, aminoacylated, and processed by the ribosome
    without compromising the fidelity or efficiency of protein synthesis. We show
    that saturation of recognition signals blocks the emergence of new tRNA identities
    and that the rate of nucleotide substitutions in tRNAs is higher in species with
    fewer tRNA genes. We propose that the growth of the genetic code stalled because
    a limit was reached in the number of identity elements that can be effectively
    used in the tRNA structure.
acknowledgement: "We thank D. Söll, H. Grosjean, and L. Filonava for comments and
  suggestions.\r\nM.O. and P.D.D. thank the Barcelona Supercomputing Center for CPU/GPU
  time on MareNostrum/\r\nMinoTauro. P.D.D. is a PEDECIBA (Programa de Desarrollo
  de las Ciencias Básicas) and an SNI\r\n(Sistema Nacional de Investigadores) (ANII,
  Uruguay) researcher. Funding: This work was\r\nsupported in part by the Spanish
  Ministry of Economy and Competitiveness (grants\r\nBIO2012-32200, Sev-2012-0208,
  and BIO2012-32868 to L.R.d.P., F.A.K., and M.O., respectively)\r\nand by the Catalan
  Government (grants 2014-SGR-0771, 2014-SGR-0974, and 2014-SGR-0134 to\r\nL.R.d.P.,
  F.A.K., and M.O., respectively). This work was also supported by the Howard Hughes\r\nMedical
  Institute International Early Career Scientist Program (55007424), by a European
  Research\r\nCouncil (ERC) Starting Grant (335980_EinME to F.K.), and by a grant
  from the ERC (ERC_SimDNA to\r\nM.O). A.G.T. and C.B. are funded by the Spanish Ministry
  of Economy and Competitiveness\r\n(FPDI-2013-17742 and BES-2013-064004, respectively)."
article_number: e1501860
article_processing_charge: No
article_type: original
author:
- first_name: Adélaïde
  full_name: Saint Léger, Adélaïde
  last_name: Saint Léger
- first_name: Carla
  full_name: Bello, Carla
  last_name: Bello
- first_name: Pablo
  full_name: Dans, Pablo
  last_name: Dans
- first_name: Adrian
  full_name: Torres, Adrian
  last_name: Torres
- first_name: Eva
  full_name: Novoa, Eva
  last_name: Novoa
- first_name: Noelia
  full_name: Camacho, Noelia
  last_name: Camacho
- first_name: Modesto
  full_name: Orozco, Modesto
  last_name: Orozco
- first_name: Fyodor
  full_name: Kondrashov, Fyodor
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
- first_name: Lluís
  full_name: Ribas De Pouplana, Lluís
  last_name: Ribas De Pouplana
citation:
  ama: Saint Léger A, Bello C, Dans P, et al. Saturation of recognition elements blocks
    evolution of new tRNA identities. <i>Science advances</i>. 2016;2(4). doi:<a href="https://doi.org/10.1126/sciadv.1501860">10.1126/sciadv.1501860</a>
  apa: Saint Léger, A., Bello, C., Dans, P., Torres, A., Novoa, E., Camacho, N., …
    Ribas De Pouplana, L. (2016). Saturation of recognition elements blocks evolution
    of new tRNA identities. <i>Science Advances</i>. American Association for the
    Advancement of Science. <a href="https://doi.org/10.1126/sciadv.1501860">https://doi.org/10.1126/sciadv.1501860</a>
  chicago: Saint Léger, Adélaïde, Carla Bello, Pablo Dans, Adrian Torres, Eva Novoa,
    Noelia Camacho, Modesto Orozco, Fyodor Kondrashov, and Lluís Ribas De Pouplana.
    “Saturation of Recognition Elements Blocks Evolution of New TRNA Identities.”
    <i>Science Advances</i>. American Association for the Advancement of Science,
    2016. <a href="https://doi.org/10.1126/sciadv.1501860">https://doi.org/10.1126/sciadv.1501860</a>.
  ieee: A. Saint Léger <i>et al.</i>, “Saturation of recognition elements blocks evolution
    of new tRNA identities,” <i>Science advances</i>, vol. 2, no. 4. American Association
    for the Advancement of Science, 2016.
  ista: Saint Léger A, Bello C, Dans P, Torres A, Novoa E, Camacho N, Orozco M, Kondrashov
    F, Ribas De Pouplana L. 2016. Saturation of recognition elements blocks evolution
    of new tRNA identities. Science advances. 2(4), e1501860.
  mla: Saint Léger, Adélaïde, et al. “Saturation of Recognition Elements Blocks Evolution
    of New TRNA Identities.” <i>Science Advances</i>, vol. 2, no. 4, e1501860, American
    Association for the Advancement of Science, 2016, doi:<a href="https://doi.org/10.1126/sciadv.1501860">10.1126/sciadv.1501860</a>.
  short: A. Saint Léger, C. Bello, P. Dans, A. Torres, E. Novoa, N. Camacho, M. Orozco,
    F. Kondrashov, L. Ribas De Pouplana, Science Advances 2 (2016).
date_created: 2018-12-11T11:48:50Z
date_published: 2016-04-29T00:00:00Z
date_updated: 2026-05-20T08:27:46Z
day: '29'
doi: 10.1126/sciadv.1501860
extern: '1'
external_id:
  pmid:
  - '27386510'
intvolume: '         2'
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1126/sciadv.1501860
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Science advances
publication_identifier:
  eissn:
  - 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
publist_id: '6798'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Saturation of recognition elements blocks evolution of new tRNA identities
tmp:
  image: /images/cc_by_nc.png
  legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
  short: CC BY-NC (4.0)
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 2
year: '2016'
...
---
_id: '8493'
abstract:
- lang: eng
  text: In this paper we study a so-called separatrix map introduced by Zaslavskii–Filonenko
    (Sov Phys JETP 27:851–857, 1968) and studied by Treschev (Physica D 116(1–2):21–43,
    1998; J Nonlinear Sci 12(1):27–58, 2002), Piftankin (Nonlinearity (19):2617–2644,
    2006) Piftankin and Treshchëv (Uspekhi Mat Nauk 62(2(374)):3–108, 2007). We derive
    a second order expansion of this map for trigonometric perturbations. In Castejon
    et al. (Random iteration of maps of a cylinder and diffusive behavior. Preprint
    available at arXiv:1501.03319, 2015), Guardia and Kaloshin (Stochastic diffusive
    behavior through big gaps in a priori unstable systems (in preparation), 2015),
    and Kaloshin et al. (Normally Hyperbolic Invariant Laminations and diffusive behavior
    for the generalized Arnold example away from resonances. Preprint available at
    http://www.terpconnect.umd.edu/vkaloshi/, 2015), applying the results of the present
    paper, we describe a class of nearly integrable deterministic systems with stochastic
    diffusive behavior.
article_processing_charge: No
article_type: original
author:
- first_name: M.
  full_name: Guardia, M.
  last_name: Guardia
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: J.
  full_name: Zhang, J.
  last_name: Zhang
citation:
  ama: Guardia M, Kaloshin V, Zhang J. A second order expansion of the separatrix
    map for trigonometric perturbations of a priori unstable systems. <i>Communications
    in Mathematical Physics</i>. 2016;348:321-361. doi:<a href="https://doi.org/10.1007/s00220-016-2705-9">10.1007/s00220-016-2705-9</a>
  apa: Guardia, M., Kaloshin, V., &#38; Zhang, J. (2016). A second order expansion
    of the separatrix map for trigonometric perturbations of a priori unstable systems.
    <i>Communications in Mathematical Physics</i>. Springer Nature. <a href="https://doi.org/10.1007/s00220-016-2705-9">https://doi.org/10.1007/s00220-016-2705-9</a>
  chicago: Guardia, M., Vadim Kaloshin, and J. Zhang. “A Second Order Expansion of
    the Separatrix Map for Trigonometric Perturbations of a Priori Unstable Systems.”
    <i>Communications in Mathematical Physics</i>. Springer Nature, 2016. <a href="https://doi.org/10.1007/s00220-016-2705-9">https://doi.org/10.1007/s00220-016-2705-9</a>.
  ieee: M. Guardia, V. Kaloshin, and J. Zhang, “A second order expansion of the separatrix
    map for trigonometric perturbations of a priori unstable systems,” <i>Communications
    in Mathematical Physics</i>, vol. 348. Springer Nature, pp. 321–361, 2016.
  ista: Guardia M, Kaloshin V, Zhang J. 2016. A second order expansion of the separatrix
    map for trigonometric perturbations of a priori unstable systems. Communications
    in Mathematical Physics. 348, 321–361.
  mla: Guardia, M., et al. “A Second Order Expansion of the Separatrix Map for Trigonometric
    Perturbations of a Priori Unstable Systems.” <i>Communications in Mathematical
    Physics</i>, vol. 348, Springer Nature, 2016, pp. 321–61, doi:<a href="https://doi.org/10.1007/s00220-016-2705-9">10.1007/s00220-016-2705-9</a>.
  short: M. Guardia, V. Kaloshin, J. Zhang, Communications in Mathematical Physics
    348 (2016) 321–361.
date_created: 2020-09-18T10:45:50Z
date_published: 2016-11-01T00:00:00Z
date_updated: 2021-01-12T08:19:39Z
day: '01'
doi: 10.1007/s00220-016-2705-9
extern: '1'
intvolume: '       348'
language:
- iso: eng
month: '11'
oa_version: None
page: 321-361
publication: Communications in Mathematical Physics
publication_identifier:
  issn:
  - 0010-3616
  - 1432-0916
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: A second order expansion of the separatrix map for trigonometric perturbations
  of a priori unstable systems
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 348
year: '2016'
...
---
_id: '8494'
abstract:
- lang: eng
  text: "We prove a form of Arnold diffusion in the a-priori stable case. Let\r\nH0(p)+ϵH1(θ,p,t),θ∈Tn,p∈Bn,t∈T=R/T,\r\nbe
    a nearly integrable system of arbitrary degrees of freedom n⩾2 with a strictly
    convex H0. We show that for a “generic” ϵH1, there exists an orbit (θ,p) satisfying\r\n∥p(t)−p(0)∥>l(H1)>0,\r\nwhere
    l(H1) is independent of ϵ. The diffusion orbit travels along a codimension-1 resonance,
    and the only obstruction to our construction is a finite set of additional resonances.\r\n\r\nFor
    the proof we use a combination of geometric and variational methods, and manage
    to adapt tools which have recently been developed in the a-priori unstable case."
article_processing_charge: No
article_type: original
author:
- first_name: Patrick
  full_name: Bernard, Patrick
  last_name: Bernard
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: Ke
  full_name: Zhang, Ke
  last_name: Zhang
citation:
  ama: Bernard P, Kaloshin V, Zhang K. Arnold diffusion in arbitrary degrees of freedom
    and normally hyperbolic invariant cylinders. <i>Acta Mathematica</i>. 2016;217(1):1-79.
    doi:<a href="https://doi.org/10.1007/s11511-016-0141-5">10.1007/s11511-016-0141-5</a>
  apa: Bernard, P., Kaloshin, V., &#38; Zhang, K. (2016). Arnold diffusion in arbitrary
    degrees of freedom and normally hyperbolic invariant cylinders. <i>Acta Mathematica</i>.
    Institut Mittag-Leffler. <a href="https://doi.org/10.1007/s11511-016-0141-5">https://doi.org/10.1007/s11511-016-0141-5</a>
  chicago: Bernard, Patrick, Vadim Kaloshin, and Ke Zhang. “Arnold Diffusion in Arbitrary
    Degrees of Freedom and Normally Hyperbolic Invariant Cylinders.” <i>Acta Mathematica</i>.
    Institut Mittag-Leffler, 2016. <a href="https://doi.org/10.1007/s11511-016-0141-5">https://doi.org/10.1007/s11511-016-0141-5</a>.
  ieee: P. Bernard, V. Kaloshin, and K. Zhang, “Arnold diffusion in arbitrary degrees
    of freedom and normally hyperbolic invariant cylinders,” <i>Acta Mathematica</i>,
    vol. 217, no. 1. Institut Mittag-Leffler, pp. 1–79, 2016.
  ista: Bernard P, Kaloshin V, Zhang K. 2016. Arnold diffusion in arbitrary degrees
    of freedom and normally hyperbolic invariant cylinders. Acta Mathematica. 217(1),
    1–79.
  mla: Bernard, Patrick, et al. “Arnold Diffusion in Arbitrary Degrees of Freedom
    and Normally Hyperbolic Invariant Cylinders.” <i>Acta Mathematica</i>, vol. 217,
    no. 1, Institut Mittag-Leffler, 2016, pp. 1–79, doi:<a href="https://doi.org/10.1007/s11511-016-0141-5">10.1007/s11511-016-0141-5</a>.
  short: P. Bernard, V. Kaloshin, K. Zhang, Acta Mathematica 217 (2016) 1–79.
date_created: 2020-09-18T10:46:07Z
date_published: 2016-09-28T00:00:00Z
date_updated: 2021-01-12T08:19:39Z
day: '28'
doi: 10.1007/s11511-016-0141-5
extern: '1'
intvolume: '       217'
issue: '1'
language:
- iso: eng
month: '09'
oa_version: None
page: 1-79
publication: Acta Mathematica
publication_identifier:
  issn:
  - 0001-5962
publication_status: published
publisher: Institut Mittag-Leffler
quality_controlled: '1'
status: public
title: Arnold diffusion in arbitrary degrees of freedom and normally hyperbolic invariant
  cylinders
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 217
year: '2016'
...
---
_id: '8496'
article_processing_charge: No
article_type: original
author:
- first_name: Artur
  full_name: Avila, Artur
  last_name: Avila
- first_name: Jacopo
  full_name: De Simoi, Jacopo
  last_name: De Simoi
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
citation:
  ama: Avila A, De Simoi J, Kaloshin V. An integrable deformation of an ellipse of
    small eccentricity is an ellipse. <i>Annals of Mathematics</i>. 2016;184(2):527-558.
    doi:<a href="https://doi.org/10.4007/annals.2016.184.2.5">10.4007/annals.2016.184.2.5</a>
  apa: Avila, A., De Simoi, J., &#38; Kaloshin, V. (2016). An integrable deformation
    of an ellipse of small eccentricity is an ellipse. <i>Annals of Mathematics</i>.
    Princeton University Press. <a href="https://doi.org/10.4007/annals.2016.184.2.5">https://doi.org/10.4007/annals.2016.184.2.5</a>
  chicago: Avila, Artur, Jacopo De Simoi, and Vadim Kaloshin. “An Integrable Deformation
    of an Ellipse of Small Eccentricity Is an Ellipse.” <i>Annals of Mathematics</i>.
    Princeton University Press, 2016. <a href="https://doi.org/10.4007/annals.2016.184.2.5">https://doi.org/10.4007/annals.2016.184.2.5</a>.
  ieee: A. Avila, J. De Simoi, and V. Kaloshin, “An integrable deformation of an ellipse
    of small eccentricity is an ellipse,” <i>Annals of Mathematics</i>, vol. 184,
    no. 2. Princeton University Press, pp. 527–558, 2016.
  ista: Avila A, De Simoi J, Kaloshin V. 2016. An integrable deformation of an ellipse
    of small eccentricity is an ellipse. Annals of Mathematics. 184(2), 527–558.
  mla: Avila, Artur, et al. “An Integrable Deformation of an Ellipse of Small Eccentricity
    Is an Ellipse.” <i>Annals of Mathematics</i>, vol. 184, no. 2, Princeton University
    Press, 2016, pp. 527–58, doi:<a href="https://doi.org/10.4007/annals.2016.184.2.5">10.4007/annals.2016.184.2.5</a>.
  short: A. Avila, J. De Simoi, V. Kaloshin, Annals of Mathematics 184 (2016) 527–558.
date_created: 2020-09-18T10:46:22Z
date_published: 2016-09-01T00:00:00Z
date_updated: 2021-01-12T08:19:40Z
day: '01'
doi: 10.4007/annals.2016.184.2.5
extern: '1'
intvolume: '       184'
issue: '2'
language:
- iso: eng
month: '09'
oa_version: None
page: 527-558
publication: Annals of Mathematics
publication_identifier:
  issn:
  - 0003-486X
publication_status: published
publisher: Princeton University Press
quality_controlled: '1'
status: public
title: An integrable deformation of an ellipse of small eccentricity is an ellipse
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 184
year: '2016'
...
---
_id: '8497'
abstract:
- lang: eng
  text: "We study the dynamics of the restricted planar three-body problem near mean
    motion resonances, i.e. a resonance involving the Keplerian periods of the two
    lighter bodies revolving around the most massive one. This problem is often used
    to model Sun–Jupiter–asteroid systems. For the primaries (Sun and Jupiter), we
    pick a realistic mass ratio μ=10−3 and a small eccentricity e0>0. The main result
    is a construction of a variety of non local diffusing orbits which show a drastic
    change of the osculating (instant) eccentricity of the asteroid, while the osculating
    semi major axis is kept almost constant. The proof relies on the careful analysis
    of the circular problem, which has a hyperbolic structure, but for which diffusion
    is prevented by KAM tori. In the proof we verify certain non-degeneracy conditions
    numerically.\r\n\r\nBased on the work of Treschev, it is natural to conjecture
    that the time of diffusion for this problem is ∼−ln(μe0)μ3/2e0. We expect our
    instability mechanism to apply to realistic values of e0 and we give heuristic
    arguments in its favor. If so, the applicability of Nekhoroshev theory to the
    three-body problem as well as the long time stability become questionable.\r\n\r\nIt
    is well known that, in the Asteroid Belt, located between the orbits of Mars and
    Jupiter, the distribution of asteroids has the so-called Kirkwood gaps exactly
    at mean motion resonances of low order. Our mechanism gives a possible explanation
    of their existence. To relate the existence of Kirkwood gaps with Arnol'd diffusion,
    we also state a conjecture on its existence for a typical ϵ-perturbation of the
    product of the pendulum and the rotator. Namely, we predict that a positive conditional
    measure of initial conditions concentrated in the main resonance exhibits Arnol’d
    diffusion on time scales −lnϵϵ2."
article_processing_charge: No
article_type: original
author:
- first_name: Jacques
  full_name: Féjoz, Jacques
  last_name: Féjoz
- first_name: Marcel
  full_name: Guàrdia, Marcel
  last_name: Guàrdia
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: Pablo
  full_name: Roldán, Pablo
  last_name: Roldán
citation:
  ama: Féjoz J, Guàrdia M, Kaloshin V, Roldán P. Kirkwood gaps and diffusion along
    mean motion resonances in the restricted planar three-body problem. <i>Journal
    of the European Mathematical Society</i>. 2016;18(10):2315-2403. doi:<a href="https://doi.org/10.4171/jems/642">10.4171/jems/642</a>
  apa: Féjoz, J., Guàrdia, M., Kaloshin, V., &#38; Roldán, P. (2016). Kirkwood gaps
    and diffusion along mean motion resonances in the restricted planar three-body
    problem. <i>Journal of the European Mathematical Society</i>. European Mathematical
    Society Publishing House. <a href="https://doi.org/10.4171/jems/642">https://doi.org/10.4171/jems/642</a>
  chicago: Féjoz, Jacques, Marcel Guàrdia, Vadim Kaloshin, and Pablo Roldán. “Kirkwood
    Gaps and Diffusion along Mean Motion Resonances in the Restricted Planar Three-Body
    Problem.” <i>Journal of the European Mathematical Society</i>. European Mathematical
    Society Publishing House, 2016. <a href="https://doi.org/10.4171/jems/642">https://doi.org/10.4171/jems/642</a>.
  ieee: J. Féjoz, M. Guàrdia, V. Kaloshin, and P. Roldán, “Kirkwood gaps and diffusion
    along mean motion resonances in the restricted planar three-body problem,” <i>Journal
    of the European Mathematical Society</i>, vol. 18, no. 10. European Mathematical
    Society Publishing House, pp. 2315–2403, 2016.
  ista: Féjoz J, Guàrdia M, Kaloshin V, Roldán P. 2016. Kirkwood gaps and diffusion
    along mean motion resonances in the restricted planar three-body problem. Journal
    of the European Mathematical Society. 18(10), 2315–2403.
  mla: Féjoz, Jacques, et al. “Kirkwood Gaps and Diffusion along Mean Motion Resonances
    in the Restricted Planar Three-Body Problem.” <i>Journal of the European Mathematical
    Society</i>, vol. 18, no. 10, European Mathematical Society Publishing House,
    2016, pp. 2315–403, doi:<a href="https://doi.org/10.4171/jems/642">10.4171/jems/642</a>.
  short: J. Féjoz, M. Guàrdia, V. Kaloshin, P. Roldán, Journal of the European Mathematical
    Society 18 (2016) 2315–2403.
date_created: 2020-09-18T10:46:31Z
date_published: 2016-09-19T00:00:00Z
date_updated: 2021-01-12T08:19:41Z
day: '19'
doi: 10.4171/jems/642
extern: '1'
intvolume: '        18'
issue: '10'
language:
- iso: eng
month: '09'
oa_version: None
page: 2315-2403
publication: Journal of the European Mathematical Society
publication_identifier:
  issn:
  - 1435-9855
publication_status: published
publisher: European Mathematical Society Publishing House
quality_controlled: '1'
status: public
title: Kirkwood gaps and diffusion along mean motion resonances in the restricted
  planar three-body problem
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 18
year: '2016'
...
---
OA_type: closed access
_id: '850'
abstract:
- lang: eng
  text: Fitness landscapes depict how genotypes manifest at the phenotypic level and
    form the basis of our understanding of many areas of biology, yet their properties
    remain elusive. Previous studies have analysed specific genes, often using their
    function as a proxy for fitness, experimentally assessing the effect on function
    of single mutations and their combinations in a specific sequence or in different
    sequences. However, systematic high-throughput studies of the local fitness landscape
    of an entire protein have not yet been reported. Here we visualize an extensive
    region of the local fitness landscape of the green fluorescent protein from Aequorea
    Victoria (avGFP) by measuring the native function (fluorescence) of tens of thousands
    of derivative genotypes of avGFP. We show that the fitness landscape of avGFP
    is narrow, with 3/4 of the derivatives with a single mutation showing reduced
    fluorescence and half of the derivatives with four mutations being completely
    non-fluorescent. The narrowness is enhanced by epistasis, which was detected in
    up to 30% of genotypes with multiple mutations and mostly occurred through the
    cumulative effect of slightly deleterious mutations causing a threshold-like decrease
    in protein stability and a concomitant loss of fluorescence. A model of orthologous
    sequence divergence spanning hundreds of millions of years predicted the extent
    of epistasis in our data, indicating congruence between the fitness landscape
    properties at the local and global scales. The characterization of the local fitness
    landscape of avGFP has important implications for several fields including molecular
    evolution, population genetics and protein design.
acknowledgement: We thank Y. Kulikova and G. Filion for discussion on statistical
  analysis and I. Osterman, R. Moretti and J. Meiler for technical assistance and
  M. Friesen for a critical reading of the manuscript. We thank H. Himmelbauer, CRG
  Genomic Unit and the Russian Science Foundation project (14-50-00150) for sequencing.
  Experiments were partially carried out using the equipment provided by the IBCH
  core facility (CKP IBCH). The work was supported by HHMI International Early Career
  Scientist Program (55007424), the EMBO Young Investigator Programme, MINECO (BFU2012-31329),
  Spanish Ministry of Economy and Competitiveness Centro de Excelencia Severo Ochoa
  2013-2017 grant (SEV-2012-0208), Secretaria d'Universitats i Recerca del Departament
  d'Economia i Coneixement de la Generalitat's AGAUR program (2014 SGR 0974), Russian
  Science Foundation (14-25-00129) and the European Research Council under the European
  Union's Seventh Framework Programme (FP7/2007-2013, ERC grant agreement, 335980-EinME).
article_processing_charge: No
article_type: original
author:
- first_name: Karen
  full_name: Sarkisyan, Karen
  id: 39A7BF80-F248-11E8-B48F-1D18A9856A87
  last_name: Sarkisyan
  orcid: 0000-0002-5375-6341
- first_name: Dmitry
  full_name: Bolotin, Dmitry
  last_name: Bolotin
- first_name: Margarita
  full_name: Meer, Margarita
  last_name: Meer
- first_name: Dinara
  full_name: Usmanova, Dinara
  last_name: Usmanova
- first_name: Alexander
  full_name: Mishin, Alexander
  last_name: Mishin
- first_name: George
  full_name: Sharonov, George
  last_name: Sharonov
- first_name: Dmitry
  full_name: Ivankov, Dmitry
  last_name: Ivankov
- first_name: Nina
  full_name: Bozhanova, Nina
  last_name: Bozhanova
- first_name: Mikhail
  full_name: Baranov, Mikhail
  last_name: Baranov
- first_name: Onuralp
  full_name: Soylemez, Onuralp
  last_name: Soylemez
- first_name: Natalya
  full_name: Bogatyreva, Natalya
  last_name: Bogatyreva
- first_name: Peter
  full_name: Vlasov, Peter
  last_name: Vlasov
- first_name: Evgeny
  full_name: Egorov, Evgeny
  last_name: Egorov
- first_name: Maria
  full_name: Logacheva, Maria
  last_name: Logacheva
- first_name: Alexey
  full_name: Kondrashov, Alexey
  last_name: Kondrashov
- first_name: Dmitriy
  full_name: Chudakov, Dmitriy
  last_name: Chudakov
- first_name: Ekaterina
  full_name: Putintseva, Ekaterina
  last_name: Putintseva
- first_name: Ilgar
  full_name: Mamedov, Ilgar
  last_name: Mamedov
- first_name: Dan
  full_name: Tawfik, Dan
  last_name: Tawfik
- first_name: Konstantin
  full_name: Lukyanov, Konstantin
  last_name: Lukyanov
- first_name: Fyodor
  full_name: Kondrashov, Fyodor
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
citation:
  ama: Sarkisyan K, Bolotin D, Meer M, et al. Local fitness landscape of the green
    fluorescent protein. <i>Nature</i>. 2016;533:397-401. doi:<a href="https://doi.org/10.1038/nature17995">10.1038/nature17995</a>
  apa: Sarkisyan, K., Bolotin, D., Meer, M., Usmanova, D., Mishin, A., Sharonov, G.,
    … Kondrashov, F. (2016). Local fitness landscape of the green fluorescent protein.
    <i>Nature</i>. Springer Nature. <a href="https://doi.org/10.1038/nature17995">https://doi.org/10.1038/nature17995</a>
  chicago: Sarkisyan, Karen, Dmitry Bolotin, Margarita Meer, Dinara Usmanova, Alexander
    Mishin, George Sharonov, Dmitry Ivankov, et al. “Local Fitness Landscape of the
    Green Fluorescent Protein.” <i>Nature</i>. Springer Nature, 2016. <a href="https://doi.org/10.1038/nature17995">https://doi.org/10.1038/nature17995</a>.
  ieee: K. Sarkisyan <i>et al.</i>, “Local fitness landscape of the green fluorescent
    protein,” <i>Nature</i>, vol. 533. Springer Nature, pp. 397–401, 2016.
  ista: Sarkisyan K, Bolotin D, Meer M, Usmanova D, Mishin A, Sharonov G, Ivankov
    D, Bozhanova N, Baranov M, Soylemez O, Bogatyreva N, Vlasov P, Egorov E, Logacheva
    M, Kondrashov A, Chudakov D, Putintseva E, Mamedov I, Tawfik D, Lukyanov K, Kondrashov
    F. 2016. Local fitness landscape of the green fluorescent protein. Nature. 533,
    397–401.
  mla: Sarkisyan, Karen, et al. “Local Fitness Landscape of the Green Fluorescent
    Protein.” <i>Nature</i>, vol. 533, Springer Nature, 2016, pp. 397–401, doi:<a
    href="https://doi.org/10.1038/nature17995">10.1038/nature17995</a>.
  short: K. Sarkisyan, D. Bolotin, M. Meer, D. Usmanova, A. Mishin, G. Sharonov, D.
    Ivankov, N. Bozhanova, M. Baranov, O. Soylemez, N. Bogatyreva, P. Vlasov, E. Egorov,
    M. Logacheva, A. Kondrashov, D. Chudakov, E. Putintseva, I. Mamedov, D. Tawfik,
    K. Lukyanov, F. Kondrashov, Nature 533 (2016) 397–401.
date_created: 2018-12-11T11:48:50Z
date_published: 2016-05-19T00:00:00Z
date_updated: 2026-05-20T08:10:59Z
day: '19'
doi: 10.1038/nature17995
extern: '1'
external_id:
  pmid:
  - '27193686'
intvolume: '       533'
language:
- iso: eng
month: '05'
oa_version: None
page: 397 - 401
pmid: 1
publication: Nature
publication_identifier:
  eissn:
  - 1476-4687
  issn:
  - 0028-0836
publication_status: published
publisher: Springer Nature
publist_id: '6799'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Local fitness landscape of the green fluorescent protein
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 533
year: '2016'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '853'
abstract:
- lang: eng
  text: A comparative analysis of the metagenomes from two 30 000-year-old permafrost
    samples, one of lake-alluvial origin and the other from late Pleistocene Ice Complex
    sediments, revealed significant differences within microbial communities. The
    late Pleistocene Ice Complex sediments (which have been characterized by the absence
    of methane with lower values of redox potential and Fe2+ content) showed a low
    abundance of methanogenic archaea and enzymes from both the carbon and nitrogen
    cycles, but a higher abundance of enzymes associated with the sulfur cycle. The
    metagenomic and geochemical analyses described in the paper provide evidence that
    the formation of the sampled late Pleistocene Ice Complex sediments likely took
    place under much more aerobic conditions than lake-alluvial sediments.
acknowledgement: This work was supported by grants from the Russian Scientific Fund
  (14-14-01115) to Elizaveta Rivkina; from the National Science Foundation (DEB-1442262)
  to Tatiana Vish- nivetskaya; and from the HHMI International Early Career Scientist
  Program (55007424), the EMBO Young Investigator Programme, MINECO (BFU2012-31329
  and Sev-2012-0208), and the AGAUR program (2014 SGR 0974) to Fyodor Kondrashov.
  Support from the Russian Scientific Fund (14-14-01115) was allocated for sample
  collection, gDNA isolation, and analysis of metagenomic data.
article_processing_charge: No
article_type: original
author:
- first_name: Elizaveta
  full_name: Rivkina, Elizaveta
  last_name: Rivkina
- first_name: Lada
  full_name: Petrovskaya, Lada
  last_name: Petrovskaya
- first_name: Tatiana
  full_name: Vishnivetskaya, Tatiana
  last_name: Vishnivetskaya
- first_name: Kirill
  full_name: Krivushin, Kirill
  last_name: Krivushin
- first_name: Lyubov
  full_name: Shmakova, Lyubov
  last_name: Shmakova
- first_name: Maria
  full_name: Tutukina, Maria
  last_name: Tutukina
- first_name: Arthur
  full_name: Meyers, Arthur
  last_name: Meyers
- first_name: Fyodor
  full_name: Kondrashov, Fyodor
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
citation:
  ama: Rivkina E, Petrovskaya L, Vishnivetskaya T, et al. Metagenomic analyses of
    the late Pleistocene permafrost - Additional tools for reconstruction of environmental
    conditions. <i>Biogeosciences</i>. 2016;13(7):2207-2219. doi:<a href="https://doi.org/10.5194/bg-13-2207-2016">10.5194/bg-13-2207-2016</a>
  apa: Rivkina, E., Petrovskaya, L., Vishnivetskaya, T., Krivushin, K., Shmakova,
    L., Tutukina, M., … Kondrashov, F. (2016). Metagenomic analyses of the late Pleistocene
    permafrost - Additional tools for reconstruction of environmental conditions.
    <i>Biogeosciences</i>. European Geosciences Union. <a href="https://doi.org/10.5194/bg-13-2207-2016">https://doi.org/10.5194/bg-13-2207-2016</a>
  chicago: Rivkina, Elizaveta, Lada Petrovskaya, Tatiana Vishnivetskaya, Kirill Krivushin,
    Lyubov Shmakova, Maria Tutukina, Arthur Meyers, and Fyodor Kondrashov. “Metagenomic
    Analyses of the Late Pleistocene Permafrost - Additional Tools for Reconstruction
    of Environmental Conditions.” <i>Biogeosciences</i>. European Geosciences Union,
    2016. <a href="https://doi.org/10.5194/bg-13-2207-2016">https://doi.org/10.5194/bg-13-2207-2016</a>.
  ieee: E. Rivkina <i>et al.</i>, “Metagenomic analyses of the late Pleistocene permafrost
    - Additional tools for reconstruction of environmental conditions,” <i>Biogeosciences</i>,
    vol. 13, no. 7. European Geosciences Union, pp. 2207–2219, 2016.
  ista: Rivkina E, Petrovskaya L, Vishnivetskaya T, Krivushin K, Shmakova L, Tutukina
    M, Meyers A, Kondrashov F. 2016. Metagenomic analyses of the late Pleistocene
    permafrost - Additional tools for reconstruction of environmental conditions.
    Biogeosciences. 13(7), 2207–2219.
  mla: Rivkina, Elizaveta, et al. “Metagenomic Analyses of the Late Pleistocene Permafrost
    - Additional Tools for Reconstruction of Environmental Conditions.” <i>Biogeosciences</i>,
    vol. 13, no. 7, European Geosciences Union, 2016, pp. 2207–19, doi:<a href="https://doi.org/10.5194/bg-13-2207-2016">10.5194/bg-13-2207-2016</a>.
  short: E. Rivkina, L. Petrovskaya, T. Vishnivetskaya, K. Krivushin, L. Shmakova,
    M. Tutukina, A. Meyers, F. Kondrashov, Biogeosciences 13 (2016) 2207–2219.
date_created: 2018-12-11T11:48:51Z
date_published: 2016-04-15T00:00:00Z
date_updated: 2026-05-20T08:59:47Z
day: '15'
doi: 10.5194/bg-13-2207-2016
extern: '1'
intvolume: '        13'
issue: '7'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.5194/bg-13-2207-2016
month: '04'
oa: 1
oa_version: Published Version
page: 2207 - 2219
publication: Biogeosciences
publication_identifier:
  eissn:
  - 1726-4189
  issn:
  - 1726-4170
publication_status: published
publisher: European Geosciences Union
publist_id: '6793'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Metagenomic analyses of the late Pleistocene permafrost - Additional tools
  for reconstruction of environmental conditions
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 13
year: '2016'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '896'
abstract:
- lang: eng
  text: Multicellular eukaryotes have evolved a range of mechanisms for immune recognition.
    A widespread family involved in innate immunity are the NACHT-domain and leucine-rich-repeat-containing
    (NLR) proteins.Mammals have small numbers of NLR proteins, whereas in some species,
    mostly those without adaptive immune systems, NLRs have expanded into very large
    families.We describe a family of nearly 400NLR proteins encoded in the zebrafish
    genome. The proteins share a defining overall structure, which arose in fishes
    after a fusion of the core NLR domains with a B30.2 domain, but can be subdivided
    into four groups based on their NACHT domains. Gene conversion acting differentially
    on the NACHT and B30.2 domains has shaped the family and created the groups. Evidence
    of positive selection in the B30.2 domain indicates that this domain rather than
    the leucine-rich repeats acts as the pathogen recognition module. In an unusual
    chromosomal organization, the majority of the genes are located on one chromosome
    arm, interspersed with other large multigene families, including a new family
    encoding zinc-finger proteins. The NLR-B30.2 proteins represent a new family with
    diversity in the specific recognition module that is present in fishes in spite
    of the parallel existence of an adaptive immune system.
acknowledgement: Financial support was provided by EMBO and the DFG SFB 670 'Zellautonome
  Immunität' to M.L., DFG SFB 680 'Molecular basis of evolutionary innovation' to
  T.W., DFG SPP1819 to M.L. and T.W., the HHMI International Early Career Scientist
  Programme (55007424), MINECO (Sev-2012-0208), AGAUR programme (2014 SGR 0974), and
  an ERC Starting Grant (335980-EinME) to F.K., the European Molecular Biology Laboratory
  to J.M., the Wellcome Trust to K.H. (zebrafish genome sequencing project) and the
  National Human Genome Research Institute (NHGRI) grant HG002659 to G.K.L. (gene
  annotation), and a grant from the Volkswagen Foundation to P.H.S. We thank the CHEOPS
  support team and the Bundesland Nordrhein Westfalen for making HPC applications
  freely available at the University of Cologne.
article_number: ' 160009'
article_processing_charge: No
article_type: original
author:
- first_name: Kerstin
  full_name: Howe, Kerstin
  last_name: Howe
- first_name: Philipp
  full_name: Schiffer, Philipp
  last_name: Schiffer
- first_name: Julia
  full_name: Zielinski, Julia
  last_name: Zielinski
- first_name: Thomas
  full_name: Wiehe, Thomas
  last_name: Wiehe
- first_name: Gavin
  full_name: Laird, Gavin
  last_name: Laird
- first_name: John
  full_name: Marioni, John
  last_name: Marioni
- first_name: Onuralp
  full_name: Soylemez, Onuralp
  last_name: Soylemez
- first_name: Fyodor
  full_name: Kondrashov, Fyodor
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
- first_name: Maria
  full_name: Leptin, Maria
  last_name: Leptin
citation:
  ama: Howe K, Schiffer P, Zielinski J, et al. Structure and evolutionary history
    of a large family of NLR proteins in the zebrafish. <i>Open Biology</i>. 2016;6(4).
    doi:<a href="https://doi.org/10.1098/rsob.160009">10.1098/rsob.160009</a>
  apa: Howe, K., Schiffer, P., Zielinski, J., Wiehe, T., Laird, G., Marioni, J., …
    Leptin, M. (2016). Structure and evolutionary history of a large family of NLR
    proteins in the zebrafish. <i>Open Biology</i>. Royal Society, The. <a href="https://doi.org/10.1098/rsob.160009">https://doi.org/10.1098/rsob.160009</a>
  chicago: Howe, Kerstin, Philipp Schiffer, Julia Zielinski, Thomas Wiehe, Gavin Laird,
    John Marioni, Onuralp Soylemez, Fyodor Kondrashov, and Maria Leptin. “Structure
    and Evolutionary History of a Large Family of NLR Proteins in the Zebrafish.”
    <i>Open Biology</i>. Royal Society, The, 2016. <a href="https://doi.org/10.1098/rsob.160009">https://doi.org/10.1098/rsob.160009</a>.
  ieee: K. Howe <i>et al.</i>, “Structure and evolutionary history of a large family
    of NLR proteins in the zebrafish,” <i>Open Biology</i>, vol. 6, no. 4. Royal Society,
    The, 2016.
  ista: Howe K, Schiffer P, Zielinski J, Wiehe T, Laird G, Marioni J, Soylemez O,
    Kondrashov F, Leptin M. 2016. Structure and evolutionary history of a large family
    of NLR proteins in the zebrafish. Open Biology. 6(4), 160009.
  mla: Howe, Kerstin, et al. “Structure and Evolutionary History of a Large Family
    of NLR Proteins in the Zebrafish.” <i>Open Biology</i>, vol. 6, no. 4, 160009,
    Royal Society, The, 2016, doi:<a href="https://doi.org/10.1098/rsob.160009">10.1098/rsob.160009</a>.
  short: K. Howe, P. Schiffer, J. Zielinski, T. Wiehe, G. Laird, J. Marioni, O. Soylemez,
    F. Kondrashov, M. Leptin, Open Biology 6 (2016).
date_created: 2018-12-11T11:49:04Z
date_published: 2016-04-01T00:00:00Z
date_updated: 2026-05-20T09:09:18Z
day: '01'
doi: 10.1098/rsob.160009
extern: '1'
external_id:
  pmid:
  - '27248802'
intvolume: '         6'
issue: '4'
keyword:
- NACHT
- B30
- SPRY
- Gene conversion
- Innate immune system
- Genome evolution
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1098/rsob.160009
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Open Biology
publication_identifier:
  eissn:
  - 2046-2441
publication_status: published
publisher: Royal Society, The
publist_id: '6754'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure and evolutionary history of a large family of NLR proteins in the
  zebrafish
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 6
year: '2016'
...
---
_id: '9019'
abstract:
- lang: eng
  text: Targeting protein–protein interactions has long been considered as a very
    difficult if impossible task, but over the past decade, front lines have moved.
    The number of successful examples is exponentially growing. This review presents
    a rapid overview of recent advances in this field considering the strengths and
    weaknesses of the small molecule approaches and alternative strategies such as
    the selection or design of artificial antibodies, peptides or peptidomimetics.
- lang: fre
  text: Cibler les interactions protéine–protéine a longtemps été considéré comme
    une tâche très difficile, voire impossible, mais, depuis les dix dernières années,
    les lignes ont bougé. Le nombre d’exemples de réussites s’accroît exponentiellement.
    Cette revue présente un rapide panorama des avancées récentes dans ce domaine,
    considérant les forces et les faiblesses de l’approche « petite molécule » ainsi
    que des stratégies alternatives comme la sélection ou le design d’anticorps artificiels,
    de peptides ou de peptidomimétiques.
article_processing_charge: No
article_type: original
author:
- first_name: May M
  full_name: Bakail, May M
  id: FB3C3F8E-522F-11EA-B186-22963DDC885E
  last_name: Bakail
  orcid: 0000-0002-9592-1587
- first_name: Francoise
  full_name: Ochsenbein, Francoise
  last_name: Ochsenbein
citation:
  ama: Bakail MM, Ochsenbein F. Targeting protein–protein interactions, a wide open
    field for drug design. <i>Comptes Rendus Chimie</i>. 2016;19(1-2):19-27. doi:<a
    href="https://doi.org/10.1016/j.crci.2015.12.004">10.1016/j.crci.2015.12.004</a>
  apa: Bakail, M. M., &#38; Ochsenbein, F. (2016). Targeting protein–protein interactions,
    a wide open field for drug design. <i>Comptes Rendus Chimie</i>. Elsevier. <a
    href="https://doi.org/10.1016/j.crci.2015.12.004">https://doi.org/10.1016/j.crci.2015.12.004</a>
  chicago: Bakail, May M, and Francoise Ochsenbein. “Targeting Protein–Protein Interactions,
    a Wide Open Field for Drug Design.” <i>Comptes Rendus Chimie</i>. Elsevier, 2016.
    <a href="https://doi.org/10.1016/j.crci.2015.12.004">https://doi.org/10.1016/j.crci.2015.12.004</a>.
  ieee: M. M. Bakail and F. Ochsenbein, “Targeting protein–protein interactions, a
    wide open field for drug design,” <i>Comptes Rendus Chimie</i>, vol. 19, no. 1–2.
    Elsevier, pp. 19–27, 2016.
  ista: Bakail MM, Ochsenbein F. 2016. Targeting protein–protein interactions, a wide
    open field for drug design. Comptes Rendus Chimie. 19(1–2), 19–27.
  mla: Bakail, May M., and Francoise Ochsenbein. “Targeting Protein–Protein Interactions,
    a Wide Open Field for Drug Design.” <i>Comptes Rendus Chimie</i>, vol. 19, no.
    1–2, Elsevier, 2016, pp. 19–27, doi:<a href="https://doi.org/10.1016/j.crci.2015.12.004">10.1016/j.crci.2015.12.004</a>.
  short: M.M. Bakail, F. Ochsenbein, Comptes Rendus Chimie 19 (2016) 19–27.
date_created: 2021-01-19T11:11:54Z
date_published: 2016-02-06T00:00:00Z
date_updated: 2023-02-23T13:46:55Z
day: '06'
ddc:
- '570'
doi: 10.1016/j.crci.2015.12.004
extern: '1'
file:
- access_level: open_access
  checksum: c262814ffdbfe95900256ab9ff42cdf5
  content_type: application/pdf
  creator: dernst
  date_created: 2021-01-22T12:36:52Z
  date_updated: 2021-01-22T12:36:52Z
  file_id: '9035'
  file_name: 2016_ComptesRendueChimie_Bakail.pdf
  file_size: 2045260
  relation: main_file
  success: 1
file_date_updated: 2021-01-22T12:36:52Z
has_accepted_license: '1'
intvolume: '        19'
issue: 1-2
keyword:
- General Chemistry
- General Chemical Engineering
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 19-27
publication: Comptes Rendus Chimie
publication_identifier:
  issn:
  - 1631-0748
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Targeting protein–protein interactions, a wide open field for drug design
tmp:
  image: /images/cc_by_nc_nd.png
  legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
    (CC BY-NC-ND 4.0)
  short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2016'
...
