---
_id: '8306'
abstract:
- lang: eng
text: Bias-resistant public randomness is a critical component in many (distributed)
protocols. Generating public randomness is hard, however, because active adversaries
may behave dishonestly to bias public random choices toward their advantage. Existing
solutions do not scale to hundreds or thousands of participants, as is needed
in many decentralized systems. We propose two large-scale distributed protocols,
RandHound and RandHerd, which provide publicly-verifiable, unpredictable, and
unbiasable randomness against Byzantine adversaries. RandHound relies on an untrusted
client to divide a set of randomness servers into groups for scalability, and
it depends on the pigeonhole principle to ensure output integrity, even for non-random,
adversarial group choices. RandHerd implements an efficient, decentralized randomness
beacon. RandHerd is structurally similar to a BFT protocol, but uses RandHound
in a one-time setup to arrange participants into verifiably unbiased random secret-sharing
groups, which then repeatedly produce random output at predefined intervals. Our
prototype demonstrates that RandHound and RandHerd achieve good performance across
hundreds of participants while retaining a low failure probability by properly
selecting protocol parameters, such as a group size and secret-sharing threshold.
For example, when sharding 512 nodes into groups of 32, our experiments show that
RandHound can produce fresh random output after 240 seconds. RandHerd, after a
setup phase of 260 seconds, is able to generate fresh random output in intervals
of approximately 6 seconds. For this configuration, both protocols operate at
a failure probability of at most 0.08% against a Byzantine adversary.
article_processing_charge: No
author:
- first_name: E.
full_name: Syta, E.
last_name: Syta
- first_name: P.
full_name: Jovanovic, P.
last_name: Jovanovic
- first_name: Eleftherios
full_name: Kokoris Kogias, Eleftherios
id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
last_name: Kokoris Kogias
- first_name: N.
full_name: Gailly, N.
last_name: Gailly
- first_name: L.
full_name: Gasser, L.
last_name: Gasser
- first_name: I.
full_name: Khoffi, I.
last_name: Khoffi
- first_name: M. J.
full_name: Fischer, M. J.
last_name: Fischer
- first_name: B.
full_name: Ford, B.
last_name: Ford
citation:
ama: 'Syta E, Jovanovic P, Kokoris Kogias E, et al. Scalable bias-resistant distributed
randomness. In: 2017 IEEE Symposium on Security and Privacy. IEEE; 2017:444-460.
doi:10.1109/SP.2017.45'
apa: 'Syta, E., Jovanovic, P., Kokoris Kogias, E., Gailly, N., Gasser, L., Khoffi,
I., … Ford, B. (2017). Scalable bias-resistant distributed randomness. In 2017
IEEE Symposium on Security and Privacy (pp. 444–460). San Jose, CA, United
States: IEEE. https://doi.org/10.1109/SP.2017.45'
chicago: Syta, E., P. Jovanovic, Eleftherios Kokoris Kogias, N. Gailly, L. Gasser,
I. Khoffi, M. J. Fischer, and B. Ford. “Scalable Bias-Resistant Distributed Randomness.”
In 2017 IEEE Symposium on Security and Privacy, 444–60. IEEE, 2017. https://doi.org/10.1109/SP.2017.45.
ieee: E. Syta et al., “Scalable bias-resistant distributed randomness,” in
2017 IEEE Symposium on Security and Privacy, San Jose, CA, United States,
2017, pp. 444–460.
ista: 'Syta E, Jovanovic P, Kokoris Kogias E, Gailly N, Gasser L, Khoffi I, Fischer
MJ, Ford B. 2017. Scalable bias-resistant distributed randomness. 2017 IEEE Symposium
on Security and Privacy. SP: Symposium on Security and Privacy, 444–460.'
mla: Syta, E., et al. “Scalable Bias-Resistant Distributed Randomness.” 2017
IEEE Symposium on Security and Privacy, IEEE, 2017, pp. 444–60, doi:10.1109/SP.2017.45.
short: E. Syta, P. Jovanovic, E. Kokoris Kogias, N. Gailly, L. Gasser, I. Khoffi,
M.J. Fischer, B. Ford, in:, 2017 IEEE Symposium on Security and Privacy, IEEE,
2017, pp. 444–460.
conference:
end_date: 2017-05-26
location: San Jose, CA, United States
name: 'SP: Symposium on Security and Privacy'
start_date: 2017-05-22
date_created: 2020-08-26T12:26:08Z
date_published: 2017-06-01T00:00:00Z
date_updated: 2021-01-12T08:18:02Z
day: '01'
doi: 10.1109/SP.2017.45
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://eprint.iacr.org/2016/1067
month: '06'
oa: 1
oa_version: Preprint
page: 444-460
publication: 2017 IEEE Symposium on Security and Privacy
publication_identifier:
isbn:
- '9781509055340'
issn:
- 2375-1207
publication_status: published
publisher: IEEE
quality_controlled: '1'
status: public
title: Scalable bias-resistant distributed randomness
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2017'
...
---
_id: '833'
abstract:
- lang: eng
text: We present an efficient algorithm to compute Euler characteristic curves of
gray scale images of arbitrary dimension. In various applications the Euler characteristic
curve is used as a descriptor of an image. Our algorithm is the first streaming
algorithm for Euler characteristic curves. The usage of streaming removes the
necessity to store the entire image in RAM. Experiments show that our implementation
handles terabyte scale images on commodity hardware. Due to lock-free parallelism,
it scales well with the number of processor cores. Additionally, we put the concept
of the Euler characteristic curve in the wider context of computational topology.
In particular, we explain the connection with persistence diagrams.
alternative_title:
- LNCS
article_processing_charge: No
arxiv: 1
author:
- first_name: Teresa
full_name: Heiss, Teresa
id: 4879BB4E-F248-11E8-B48F-1D18A9856A87
last_name: Heiss
orcid: 0000-0002-1780-2689
- first_name: Hubert
full_name: Wagner, Hubert
id: 379CA8B8-F248-11E8-B48F-1D18A9856A87
last_name: Wagner
citation:
ama: 'Heiss T, Wagner H. Streaming algorithm for Euler characteristic curves of
multidimensional images. In: Felsberg M, Heyden A, Krüger N, eds. Vol 10424. Springer;
2017:397-409. doi:10.1007/978-3-319-64689-3_32'
apa: 'Heiss, T., & Wagner, H. (2017). Streaming algorithm for Euler characteristic
curves of multidimensional images. In M. Felsberg, A. Heyden, & N. Krüger
(Eds.) (Vol. 10424, pp. 397–409). Presented at the CAIP: Computer Analysis of
Images and Patterns, Ystad, Sweden: Springer. https://doi.org/10.1007/978-3-319-64689-3_32'
chicago: Heiss, Teresa, and Hubert Wagner. “Streaming Algorithm for Euler Characteristic
Curves of Multidimensional Images.” edited by Michael Felsberg, Anders Heyden,
and Norbert Krüger, 10424:397–409. Springer, 2017. https://doi.org/10.1007/978-3-319-64689-3_32.
ieee: 'T. Heiss and H. Wagner, “Streaming algorithm for Euler characteristic curves
of multidimensional images,” presented at the CAIP: Computer Analysis of Images
and Patterns, Ystad, Sweden, 2017, vol. 10424, pp. 397–409.'
ista: 'Heiss T, Wagner H. 2017. Streaming algorithm for Euler characteristic curves
of multidimensional images. CAIP: Computer Analysis of Images and Patterns, LNCS,
vol. 10424, 397–409.'
mla: Heiss, Teresa, and Hubert Wagner. Streaming Algorithm for Euler Characteristic
Curves of Multidimensional Images. Edited by Michael Felsberg et al., vol.
10424, Springer, 2017, pp. 397–409, doi:10.1007/978-3-319-64689-3_32.
short: T. Heiss, H. Wagner, in:, M. Felsberg, A. Heyden, N. Krüger (Eds.), Springer,
2017, pp. 397–409.
conference:
end_date: 2017-08-24
location: Ystad, Sweden
name: 'CAIP: Computer Analysis of Images and Patterns'
start_date: 2017-08-22
corr_author: '1'
date_created: 2018-12-11T11:48:45Z
date_published: 2017-07-28T00:00:00Z
date_updated: 2025-06-04T09:54:22Z
day: '28'
department:
- _id: HeEd
doi: 10.1007/978-3-319-64689-3_32
editor:
- first_name: Michael
full_name: Felsberg, Michael
last_name: Felsberg
- first_name: Anders
full_name: Heyden, Anders
last_name: Heyden
- first_name: Norbert
full_name: Krüger, Norbert
last_name: Krüger
external_id:
arxiv:
- '1705.02045'
isi:
- '000432085900032'
intvolume: ' 10424'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1705.02045
month: '07'
oa: 1
oa_version: Submitted Version
page: 397 - 409
publication_identifier:
issn:
- 0302-9743
publication_status: published
publisher: Springer
publist_id: '6815'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Streaming algorithm for Euler characteristic curves of multidimensional images
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10424
year: '2017'
...
---
_id: '834'
abstract:
- lang: eng
text: 'Thermal and many-body localized phases are separated by a dynamical phase
transition of a new kind. We analyze the distribution of off-diagonal matrix elements
of local operators across this transition in two different models of disordered
spin chains. We show that the behavior of matrix elements can be used to characterize
the breakdown of thermalization and to extract the many-body Thouless energy.
We find that upon increasing the disorder strength the system enters a critical
region around the many-body localization transition. The properties of the system
in this region are: (i) the Thouless energy becomes smaller than the level spacing,
(ii) the matrix elements show critical dependence on the energy difference, and
(iii) the matrix elements, viewed as amplitudes of a fictitious wave function,
exhibit strong multifractality. This critical region decreases with the system
size, which we interpret as evidence for a diverging correlation length at the
many-body localization transition. Our findings show that the correlation length
becomes larger than the accessible system sizes in a broad range of disorder strength
values and shed light on the critical behavior near the many-body localization
transition.'
acknowledgement: We acknowledge useful discussions with V. Kravtsov, T. Grover,
and R. Vasseur. M.S. was supported by Gordon and Betty Moore Foundation’s EPiQS
Initiative through Grant GBMF4307. M.S. and D.A. acknowledge hospitality of KITP, where parts of
this work were completed (supported in part by the National Science Foundation under
Grant No. NSF PHY11-25915)
article_number: '104201'
article_processing_charge: No
arxiv: 1
author:
- first_name: Maksym
full_name: Serbyn, Maksym
id: 47809E7E-F248-11E8-B48F-1D18A9856A87
last_name: Serbyn
orcid: 0000-0002-2399-5827
- first_name: Papic
full_name: Zlatko, Papic
last_name: Zlatko
- first_name: Dmitry
full_name: Abanin, Dmitry
last_name: Abanin
citation:
ama: Serbyn M, Zlatko P, Abanin D. Thouless energy and multifractality across the
many-body localization transition. Physical Review B - Condensed Matter and
Materials Physics. 2017;96(10). doi:10.1103/PhysRevB.96.104201
apa: Serbyn, M., Zlatko, P., & Abanin, D. (2017). Thouless energy and multifractality
across the many-body localization transition. Physical Review B - Condensed
Matter and Materials Physics. American Physical Society. https://doi.org/10.1103/PhysRevB.96.104201
chicago: Serbyn, Maksym, Papic Zlatko, and Dmitry Abanin. “Thouless Energy and Multifractality
across the Many-Body Localization Transition.” Physical Review B - Condensed
Matter and Materials Physics. American Physical Society, 2017. https://doi.org/10.1103/PhysRevB.96.104201.
ieee: M. Serbyn, P. Zlatko, and D. Abanin, “Thouless energy and multifractality
across the many-body localization transition,” Physical Review B - Condensed
Matter and Materials Physics, vol. 96, no. 10. American Physical Society,
2017.
ista: Serbyn M, Zlatko P, Abanin D. 2017. Thouless energy and multifractality across
the many-body localization transition. Physical Review B - Condensed Matter and
Materials Physics. 96(10), 104201.
mla: Serbyn, Maksym, et al. “Thouless Energy and Multifractality across the Many-Body
Localization Transition.” Physical Review B - Condensed Matter and Materials
Physics, vol. 96, no. 10, 104201, American Physical Society, 2017, doi:10.1103/PhysRevB.96.104201.
short: M. Serbyn, P. Zlatko, D. Abanin, Physical Review B - Condensed Matter and
Materials Physics 96 (2017).
date_created: 2018-12-11T11:48:45Z
date_published: 2017-09-06T00:00:00Z
date_updated: 2025-06-04T09:55:57Z
day: '06'
department:
- _id: MaSe
doi: 10.1103/PhysRevB.96.104201
external_id:
arxiv:
- '1610.02389'
isi:
- '000409429300004'
intvolume: ' 96'
isi: 1
issue: '10'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1610.02389
month: '09'
oa: 1
oa_version: Submitted Version
publication: Physical Review B - Condensed Matter and Materials Physics
publication_identifier:
issn:
- 2469-9950
publication_status: published
publisher: American Physical Society
publist_id: '6814'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Thouless energy and multifractality across the many-body localization transition
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 96
year: '2017'
...
---
_id: '835'
abstract:
- lang: eng
text: An outstanding question in animal development, tissue homeostasis and disease
is how cell populations adapt to sensory inputs. During Drosophila larval development,
hematopoietic sites are in direct contact with sensory neuron clusters of the
peripheral nervous system (PNS), and blood cells (hemocytes) require the PNS for
their survival and recruitment to these microenvironments, known as Hematopoietic
Pockets. Here we report that Activin-β, a TGF-β family ligand, is expressed by
sensory neurons of the PNS and regulates the proliferation and adhesion of hemocytes.
These hemocyte responses depend on PNS activity, as shown by agonist treatment
and transient silencing of sensory neurons. Activin-β has a key role in this regulation,
which is apparent from reporter expression and mutant analyses. This mechanism
of local sensory neurons controlling blood cell adaptation invites evolutionary
parallels with vertebrate hematopoietic progenitors and the independent myeloid
system of tissue macrophages, whose regulation by local microenvironments remain
undefined.
article_number: '15990'
article_processing_charge: No
author:
- first_name: Kalpana
full_name: Makhijani, Kalpana
last_name: Makhijani
- first_name: Brandy
full_name: Alexander, Brandy
last_name: Alexander
- first_name: Deepti
full_name: Rao, Deepti
last_name: Rao
- first_name: Sophia
full_name: Petraki, Sophia
last_name: Petraki
- first_name: Leire
full_name: Herboso, Leire
last_name: Herboso
- first_name: Katelyn
full_name: Kukar, Katelyn
last_name: Kukar
- first_name: Itrat
full_name: Batool, Itrat
last_name: Batool
- first_name: Stephanie
full_name: Wachner, Stephanie
id: 2A95E7B0-F248-11E8-B48F-1D18A9856A87
last_name: Wachner
- first_name: Katrina
full_name: Gold, Katrina
last_name: Gold
- first_name: Corinna
full_name: Wong, Corinna
last_name: Wong
- first_name: Michael
full_name: O'Connor, Michael
last_name: O'Connor
- first_name: Katja
full_name: Brückner, Katja
last_name: Brückner
citation:
ama: Makhijani K, Alexander B, Rao D, et al. Regulation of Drosophila hematopoietic
sites by Activin-β from active sensory neurons. Nature Communications.
2017;8. doi:10.1038/ncomms15990
apa: Makhijani, K., Alexander, B., Rao, D., Petraki, S., Herboso, L., Kukar, K.,
… Brückner, K. (2017). Regulation of Drosophila hematopoietic sites by Activin-β
from active sensory neurons. Nature Communications. Nature Publishing Group.
https://doi.org/10.1038/ncomms15990
chicago: Makhijani, Kalpana, Brandy Alexander, Deepti Rao, Sophia Petraki, Leire
Herboso, Katelyn Kukar, Itrat Batool, et al. “Regulation of Drosophila Hematopoietic
Sites by Activin-β from Active Sensory Neurons.” Nature Communications.
Nature Publishing Group, 2017. https://doi.org/10.1038/ncomms15990.
ieee: K. Makhijani et al., “Regulation of Drosophila hematopoietic sites
by Activin-β from active sensory neurons,” Nature Communications, vol.
8. Nature Publishing Group, 2017.
ista: Makhijani K, Alexander B, Rao D, Petraki S, Herboso L, Kukar K, Batool I,
Wachner S, Gold K, Wong C, O’Connor M, Brückner K. 2017. Regulation of Drosophila
hematopoietic sites by Activin-β from active sensory neurons. Nature Communications.
8, 15990.
mla: Makhijani, Kalpana, et al. “Regulation of Drosophila Hematopoietic Sites by
Activin-β from Active Sensory Neurons.” Nature Communications, vol. 8,
15990, Nature Publishing Group, 2017, doi:10.1038/ncomms15990.
short: K. Makhijani, B. Alexander, D. Rao, S. Petraki, L. Herboso, K. Kukar, I.
Batool, S. Wachner, K. Gold, C. Wong, M. O’Connor, K. Brückner, Nature Communications
8 (2017).
date_created: 2018-12-11T11:48:45Z
date_published: 2017-07-27T00:00:00Z
date_updated: 2023-09-26T15:51:28Z
day: '27'
ddc:
- '570'
- '576'
- '616'
doi: 10.1038/ncomms15990
extern: '1'
external_id:
isi:
- '000406360100001'
file:
- access_level: open_access
checksum: 99a3d63308d4250eda0a35341171f80e
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:15:32Z
date_updated: 2020-07-14T12:48:12Z
file_id: '5153'
file_name: IST-2017-859-v1+1_ncomms15990.pdf
file_size: 3027104
relation: main_file
file_date_updated: 2020-07-14T12:48:12Z
has_accepted_license: '1'
intvolume: ' 8'
isi: 1
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
issn:
- '20411723'
publication_status: published
publisher: Nature Publishing Group
publist_id: '6813'
pubrep_id: '859'
quality_controlled: '1'
status: public
title: Regulation of Drosophila hematopoietic sites by Activin-β from active sensory
neurons
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: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 8
year: '2017'
...
---
_id: '836'
abstract:
- lang: eng
text: Recent research has examined how to study the topological features of a continuous
self-map by means of the persistence of the eigenspaces, for given eigenvalues,
of the endomorphism induced in homology over a field. This raised the question
of how to select dynamically significant eigenvalues. The present paper aims to
answer this question, giving an algorithm that computes the persistence of eigenspaces
for every eigenvalue simultaneously, also expressing said eigenspaces as direct
sums of “finite” and “singular” subspaces.
alternative_title:
- PROMS
article_processing_charge: No
author:
- first_name: Marc
full_name: Ethier, Marc
last_name: Ethier
- first_name: Grzegorz
full_name: Jablonski, Grzegorz
id: 4483EF78-F248-11E8-B48F-1D18A9856A87
last_name: Jablonski
orcid: 0000-0002-3536-9866
- first_name: Marian
full_name: Mrozek, Marian
last_name: Mrozek
citation:
ama: 'Ethier M, Jablonski G, Mrozek M. Finding eigenvalues of self-maps with the
Kronecker canonical form. In: Special Sessions in Applications of Computer
Algebra. Vol 198. Springer; 2017:119-136. doi:10.1007/978-3-319-56932-1_8'
apa: 'Ethier, M., Jablonski, G., & Mrozek, M. (2017). Finding eigenvalues of
self-maps with the Kronecker canonical form. In Special Sessions in Applications
of Computer Algebra (Vol. 198, pp. 119–136). Kalamata, Greece: Springer. https://doi.org/10.1007/978-3-319-56932-1_8'
chicago: Ethier, Marc, Grzegorz Jablonski, and Marian Mrozek. “Finding Eigenvalues
of Self-Maps with the Kronecker Canonical Form.” In Special Sessions in Applications
of Computer Algebra, 198:119–36. Springer, 2017. https://doi.org/10.1007/978-3-319-56932-1_8.
ieee: M. Ethier, G. Jablonski, and M. Mrozek, “Finding eigenvalues of self-maps
with the Kronecker canonical form,” in Special Sessions in Applications of
Computer Algebra, Kalamata, Greece, 2017, vol. 198, pp. 119–136.
ista: 'Ethier M, Jablonski G, Mrozek M. 2017. Finding eigenvalues of self-maps with
the Kronecker canonical form. Special Sessions in Applications of Computer Algebra.
ACA: Applications of Computer Algebra, PROMS, vol. 198, 119–136.'
mla: Ethier, Marc, et al. “Finding Eigenvalues of Self-Maps with the Kronecker Canonical
Form.” Special Sessions in Applications of Computer Algebra, vol. 198,
Springer, 2017, pp. 119–36, doi:10.1007/978-3-319-56932-1_8.
short: M. Ethier, G. Jablonski, M. Mrozek, in:, Special Sessions in Applications
of Computer Algebra, Springer, 2017, pp. 119–136.
conference:
end_date: 2015-07-23
location: Kalamata, Greece
name: 'ACA: Applications of Computer Algebra'
start_date: 2015-07-20
date_created: 2018-12-11T11:48:46Z
date_published: 2017-07-27T00:00:00Z
date_updated: 2025-04-15T08:37:55Z
day: '27'
department:
- _id: HeEd
doi: 10.1007/978-3-319-56932-1_8
ec_funded: 1
external_id:
isi:
- '000434088200008'
intvolume: ' 198'
isi: 1
language:
- iso: eng
month: '07'
oa_version: None
page: 119 - 136
project:
- _id: 255D761E-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '318493'
name: Topological Complex Systems
publication: Special Sessions in Applications of Computer Algebra
publication_identifier:
isbn:
- 978-331956930-7
publication_status: published
publisher: Springer
publist_id: '6812'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Finding eigenvalues of self-maps with the Kronecker canonical form
type: conference
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 198
year: '2017'
...
---
_id: '84'
abstract:
- lang: eng
text: The advent of high-throughput technologies and the concurrent advances in
information sciences have led to a data revolution in biology. This revolution
is most significant in molecular biology, with an increase in the number and scale
of the “omics” projects over the last decade. Genomics projects, for example,
have produced impressive advances in our knowledge of the information concealed
into genomes, from the many genes that encode for the proteins that are responsible
for most if not all cellular functions, to the noncoding regions that are now
known to provide regulatory functions. Proteomics initiatives help to decipher
the role of post-translation modifications on the protein structures and provide
maps of protein-protein interactions, while functional genomics is the field that
attempts to make use of the data produced by these projects to understand protein
functions. The biggest challenge today is to assimilate the wealth of information
provided by these initiatives into a conceptual framework that will help us decipher
life. For example, the current views of the relationship between protein structure
and function remain fragmented. We know of their sequences, more and more about
their structures, we have information on their biological activities, but we have
difficulties connecting this dotted line into an informed whole. We lack the experimental
and computational tools for directly studying protein structure, function, and
dynamics at the molecular and supra-molecular levels. In this chapter, we review
some of the current developments in building the computational tools that are
needed, focusing on the role that geometry and topology play in these efforts.
One of our goals is to raise the general awareness about the importance of geometric
methods in elucidating the mysterious foundations of our very existence. Another
goal is the broadening of what we consider a geometric algorithm. There is plenty
of valuable no-man’s-land between combinatorial and numerical algorithms, and
it seems opportune to explore this land with a computational-geometric frame of
mind.
article_processing_charge: No
author:
- first_name: Herbert
full_name: Edelsbrunner, Herbert
id: 3FB178DA-F248-11E8-B48F-1D18A9856A87
last_name: Edelsbrunner
orcid: 0000-0002-9823-6833
- first_name: Patrice
full_name: Koehl, Patrice
last_name: Koehl
citation:
ama: 'Edelsbrunner H, Koehl P. Computational topology for structural molecular biology.
In: Toth C, O’Rourke J, Goodman J, eds. Handbook of Discrete and Computational
Geometry, Third Edition. Handbook of Discrete and Computational Geometry.
Taylor & Francis; 2017:1709-1735. doi:10.1201/9781315119601'
apa: Edelsbrunner, H., & Koehl, P. (2017). Computational topology for structural
molecular biology. In C. Toth, J. O’Rourke, & J. Goodman (Eds.), Handbook
of Discrete and Computational Geometry, Third Edition (pp. 1709–1735). Taylor
& Francis. https://doi.org/10.1201/9781315119601
chicago: Edelsbrunner, Herbert, and Patrice Koehl. “Computational Topology for Structural
Molecular Biology.” In Handbook of Discrete and Computational Geometry, Third
Edition, edited by Csaba Toth, Joseph O’Rourke, and Jacob Goodman, 1709–35.
Handbook of Discrete and Computational Geometry. Taylor & Francis, 2017. https://doi.org/10.1201/9781315119601.
ieee: H. Edelsbrunner and P. Koehl, “Computational topology for structural molecular
biology,” in Handbook of Discrete and Computational Geometry, Third Edition,
C. Toth, J. O’Rourke, and J. Goodman, Eds. Taylor & Francis, 2017, pp. 1709–1735.
ista: 'Edelsbrunner H, Koehl P. 2017.Computational topology for structural molecular
biology. In: Handbook of Discrete and Computational Geometry, Third Edition. ,
1709–1735.'
mla: Edelsbrunner, Herbert, and Patrice Koehl. “Computational Topology for Structural
Molecular Biology.” Handbook of Discrete and Computational Geometry, Third
Edition, edited by Csaba Toth et al., Taylor & Francis, 2017, pp. 1709–35,
doi:10.1201/9781315119601.
short: H. Edelsbrunner, P. Koehl, in:, C. Toth, J. O’Rourke, J. Goodman (Eds.),
Handbook of Discrete and Computational Geometry, Third Edition, Taylor & Francis,
2017, pp. 1709–1735.
date_created: 2018-12-11T11:44:32Z
date_published: 2017-11-09T00:00:00Z
date_updated: 2023-10-16T11:15:22Z
day: '09'
department:
- _id: HeEd
doi: 10.1201/9781315119601
editor:
- first_name: Csaba
full_name: Toth, Csaba
last_name: Toth
- first_name: Joseph
full_name: O'Rourke, Joseph
last_name: O'Rourke
- first_name: Jacob
full_name: Goodman, Jacob
last_name: Goodman
language:
- iso: eng
month: '11'
oa_version: None
page: 1709 - 1735
publication: Handbook of Discrete and Computational Geometry, Third Edition
publication_identifier:
eisbn:
- '9781498711425'
publication_status: published
publisher: Taylor & Francis
publist_id: '7970'
quality_controlled: '1'
scopus_import: '1'
series_title: Handbook of Discrete and Computational Geometry
status: public
title: Computational topology for structural molecular biology
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2017'
...
---
_id: '8423'
abstract:
- lang: eng
text: In this paper we show that for a generic strictly convex domain, one can recover
the eigendata corresponding to Aubry–Mather periodic orbits of the induced billiard
map from the (maximal) marked length spectrum of the domain.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Guan
full_name: Huang, Guan
last_name: Huang
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Alfonso
full_name: Sorrentino, Alfonso
last_name: Sorrentino
citation:
ama: Huang G, Kaloshin V, Sorrentino A. On the marked length spectrum of generic
strictly convex billiard tables. Duke Mathematical Journal. 2017;167(1):175-209.
doi:10.1215/00127094-2017-0038
apa: Huang, G., Kaloshin, V., & Sorrentino, A. (2017). On the marked length
spectrum of generic strictly convex billiard tables. Duke Mathematical Journal.
Duke University Press. https://doi.org/10.1215/00127094-2017-0038
chicago: Huang, Guan, Vadim Kaloshin, and Alfonso Sorrentino. “On the Marked Length
Spectrum of Generic Strictly Convex Billiard Tables.” Duke Mathematical Journal.
Duke University Press, 2017. https://doi.org/10.1215/00127094-2017-0038.
ieee: G. Huang, V. Kaloshin, and A. Sorrentino, “On the marked length spectrum of
generic strictly convex billiard tables,” Duke Mathematical Journal, vol.
167, no. 1. Duke University Press, pp. 175–209, 2017.
ista: Huang G, Kaloshin V, Sorrentino A. 2017. On the marked length spectrum of
generic strictly convex billiard tables. Duke Mathematical Journal. 167(1), 175–209.
mla: Huang, Guan, et al. “On the Marked Length Spectrum of Generic Strictly Convex
Billiard Tables.” Duke Mathematical Journal, vol. 167, no. 1, Duke University
Press, 2017, pp. 175–209, doi:10.1215/00127094-2017-0038.
short: G. Huang, V. Kaloshin, A. Sorrentino, Duke Mathematical Journal 167 (2017)
175–209.
date_created: 2020-09-17T10:42:42Z
date_published: 2017-12-08T00:00:00Z
date_updated: 2021-01-12T08:19:11Z
day: '08'
doi: 10.1215/00127094-2017-0038
extern: '1'
external_id:
arxiv:
- '1603.08838'
intvolume: ' 167'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1603.08838
month: '12'
oa: 1
oa_version: Preprint
page: 175-209
publication: Duke Mathematical Journal
publication_identifier:
issn:
- 0012-7094
publication_status: published
publisher: Duke University Press
quality_controlled: '1'
status: public
title: On the marked length spectrum of generic strictly convex billiard tables
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 167
year: '2017'
...
---
_id: '8427'
abstract:
- lang: eng
text: We show that any sufficiently (finitely) smooth ℤ₂-symmetric strictly convex
domain sufficiently close to a circle is dynamically spectrally rigid; i.e., all
deformations among domains in the same class that preserve the length of all periodic
orbits of the associated billiard flow must necessarily be isometric deformations.
This gives a partial answer to a question of P. Sarnak.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- 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
- first_name: Qiaoling
full_name: Wei, Qiaoling
last_name: Wei
citation:
ama: De Simoi J, Kaloshin V, Wei Q. Dynamical spectral rigidity among Z2-symmetric
strictly convex domains close to a circle. Annals of Mathematics. 2017;186(1):277-314.
doi:10.4007/annals.2017.186.1.7
apa: De Simoi, J., Kaloshin, V., & Wei, Q. (2017). Dynamical spectral rigidity
among Z2-symmetric strictly convex domains close to a circle. Annals of Mathematics.
Annals of Mathematics. https://doi.org/10.4007/annals.2017.186.1.7
chicago: De Simoi, Jacopo, Vadim Kaloshin, and Qiaoling Wei. “Dynamical Spectral
Rigidity among Z2-Symmetric Strictly Convex Domains Close to a Circle.” Annals
of Mathematics. Annals of Mathematics, 2017. https://doi.org/10.4007/annals.2017.186.1.7.
ieee: J. De Simoi, V. Kaloshin, and Q. Wei, “Dynamical spectral rigidity among Z2-symmetric
strictly convex domains close to a circle,” Annals of Mathematics, vol.
186, no. 1. Annals of Mathematics, pp. 277–314, 2017.
ista: De Simoi J, Kaloshin V, Wei Q. 2017. Dynamical spectral rigidity among Z2-symmetric
strictly convex domains close to a circle. Annals of Mathematics. 186(1), 277–314.
mla: De Simoi, Jacopo, et al. “Dynamical Spectral Rigidity among Z2-Symmetric Strictly
Convex Domains Close to a Circle.” Annals of Mathematics, vol. 186, no.
1, Annals of Mathematics, 2017, pp. 277–314, doi:10.4007/annals.2017.186.1.7.
short: J. De Simoi, V. Kaloshin, Q. Wei, Annals of Mathematics 186 (2017) 277–314.
date_created: 2020-09-17T10:46:42Z
date_published: 2017-07-01T00:00:00Z
date_updated: 2021-01-12T08:19:12Z
day: '01'
doi: 10.4007/annals.2017.186.1.7
extern: '1'
external_id:
arxiv:
- '1606.00230'
intvolume: ' 186'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1606.00230
month: '07'
oa: 1
oa_version: Preprint
page: 277-314
publication: Annals of Mathematics
publication_identifier:
issn:
- 0003-486X
publication_status: published
publisher: Annals of Mathematics
quality_controlled: '1'
status: public
title: Dynamical spectral rigidity among Z2-symmetric strictly convex domains close
to a circle
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 186
year: '2017'
...
---
_id: '8444'
abstract:
- lang: eng
text: Biophysical investigation of membrane proteins generally requires their extraction
from native sources using detergents, a step that can lead, possibly irreversibly,
to protein denaturation. The propensity of dodecylphosphocholine (DPC), a detergent
widely utilized in NMR studies of membrane proteins, to distort their structure
has been the subject of much controversy. It has been recently proposed that the
binding specificity of the yeast mitochondrial ADP/ATP carrier (yAAC3) toward
cardiolipins is preserved in DPC, thereby suggesting that DPC is a suitable environment
in which to study membrane proteins. In this communication, we used all-atom molecular
dynamics simulations to investigate the specific binding of cardiolipins to yAAC3.
Our data demonstrate that the interaction interface observed in a native-like
environment differs markedly from that inferred from an NMR investigation in DPC,
implying that in this detergent, the protein structure is distorted. We further
investigated yAAC3 solubilized in DPC and in the milder dodecylmaltoside with
thermal-shift assays. The loss of thermal transition observed in DPC confirms
that the protein is no longer properly folded in this environment.
article_processing_charge: No
article_type: original
author:
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Martin S.
full_name: King, Martin S.
last_name: King
- first_name: Edmund R.S.
full_name: Kunji, Edmund R.S.
last_name: Kunji
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
citation:
ama: Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. Mitochondrial ADP/ATP carrier
in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical
Journal. 2017;113(11):2311-2315. doi:10.1016/j.bpj.2017.09.019
apa: Dehez, F., Schanda, P., King, M. S., Kunji, E. R. S., & Chipot, C. (2017).
Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with
non-native affinity. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2017.09.019
chicago: Dehez, François, Paul Schanda, Martin S. King, Edmund R.S. Kunji, and Christophe
Chipot. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins
with Non-Native Affinity.” Biophysical Journal. Elsevier, 2017. https://doi.org/10.1016/j.bpj.2017.09.019.
ieee: F. Dehez, P. Schanda, M. S. King, E. R. S. Kunji, and C. Chipot, “Mitochondrial
ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity,”
Biophysical Journal, vol. 113, no. 11. Elsevier, pp. 2311–2315, 2017.
ista: Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. 2017. Mitochondrial ADP/ATP
carrier in dodecylphosphocholine binds cardiolipins with non-native affinity.
Biophysical Journal. 113(11), 2311–2315.
mla: Dehez, François, et al. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine
Binds Cardiolipins with Non-Native Affinity.” Biophysical Journal, vol.
113, no. 11, Elsevier, 2017, pp. 2311–15, doi:10.1016/j.bpj.2017.09.019.
short: F. Dehez, P. Schanda, M.S. King, E.R.S. Kunji, C. Chipot, Biophysical Journal
113 (2017) 2311–2315.
date_created: 2020-09-18T10:05:54Z
date_published: 2017-12-05T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '05'
doi: 10.1016/j.bpj.2017.09.019
extern: '1'
intvolume: ' 113'
issue: '11'
keyword:
- Biophysics
language:
- iso: eng
month: '12'
oa_version: None
page: 2311-2315
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with
non-native affinity
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 113
year: '2017'
...
---
OA_place: publisher
OA_type: gold
_id: '8445'
abstract:
- lang: eng
text: Proteins perform their functions in solution but their structures are most
frequently studied inside crystals. Here we probe how the crystal packing alters
microsecond dynamics, using solid-state NMR measurements and multi-microsecond
MD simulations of different crystal forms of ubiquitin. In particular, near-rotary-resonance
relaxation dispersion (NERRD) experiments probe angular backbone motion, while
Bloch–McConnell relaxation dispersion data report on fluctuations of the local
electronic environment. These experiments and simulations reveal that the packing
of the protein can significantly alter the thermodynamics and kinetics of local
conformational exchange. Moreover, we report small-amplitude reorientational motion
of protein molecules in the crystal lattice with an ~3–5° amplitude on a tens-of-microseconds
time scale in one of the crystals, but not in others. An intriguing possibility
arises that overall motion is to some extent coupled to local dynamics. Our study
highlights the importance of considering the packing when analyzing dynamics of
crystalline proteins.
article_number: '145'
article_processing_charge: Yes
article_type: original
author:
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Sergei A.
full_name: Izmailov, Sergei A.
last_name: Izmailov
- first_name: Olga N.
full_name: Rogacheva, Olga N.
last_name: Rogacheva
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Joyce
full_name: Woodhouse, Joyce
last_name: Woodhouse
- first_name: Anastasya
full_name: Shilova, Anastasya
last_name: Shilova
- first_name: Yi
full_name: Xue, Yi
last_name: Xue
- first_name: Tairan
full_name: Yuwen, Tairan
last_name: Yuwen
- first_name: Nicolas
full_name: Coquelle, Nicolas
last_name: Coquelle
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Nikolai R.
full_name: Skrynnikov, Nikolai R.
last_name: Skrynnikov
- 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, Izmailov SA, Rogacheva ON, et al. Slow conformational exchange
and overall rocking motion in ubiquitin protein crystals. Nature Communications.
2017;8. doi:10.1038/s41467-017-00165-8
apa: Kurauskas, V., Izmailov, S. A., Rogacheva, O. N., Hessel, A., Ayala, I., Woodhouse,
J., … Schanda, P. (2017). Slow conformational exchange and overall rocking motion
in ubiquitin protein crystals. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-017-00165-8
chicago: Kurauskas, Vilius, Sergei A. Izmailov, Olga N. Rogacheva, Audrey Hessel,
Isabel Ayala, Joyce Woodhouse, Anastasya Shilova, et al. “Slow Conformational
Exchange and Overall Rocking Motion in Ubiquitin Protein Crystals.” Nature
Communications. Springer Nature, 2017. https://doi.org/10.1038/s41467-017-00165-8.
ieee: V. Kurauskas et al., “Slow conformational exchange and overall rocking
motion in ubiquitin protein crystals,” Nature Communications, vol. 8. Springer
Nature, 2017.
ista: Kurauskas V, Izmailov SA, Rogacheva ON, Hessel A, Ayala I, Woodhouse J, Shilova
A, Xue Y, Yuwen T, Coquelle N, Colletier J-P, Skrynnikov NR, Schanda P. 2017.
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals.
Nature Communications. 8, 145.
mla: Kurauskas, Vilius, et al. “Slow Conformational Exchange and Overall Rocking
Motion in Ubiquitin Protein Crystals.” Nature Communications, vol. 8, 145,
Springer Nature, 2017, doi:10.1038/s41467-017-00165-8.
short: V. Kurauskas, S.A. Izmailov, O.N. Rogacheva, A. Hessel, I. Ayala, J. Woodhouse,
A. Shilova, Y. Xue, T. Yuwen, N. Coquelle, J.-P. Colletier, N.R. Skrynnikov, P.
Schanda, Nature Communications 8 (2017).
date_created: 2020-09-18T10:06:01Z
date_published: 2017-07-27T00:00:00Z
date_updated: 2025-01-22T14:32:38Z
day: '27'
doi: 10.1038/s41467-017-00165-8
extern: '1'
intvolume: ' 8'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-017-00165-8
month: '07'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Slow conformational exchange and overall rocking motion in ubiquitin protein
crystals
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2017'
...
---
_id: '8446'
abstract:
- lang: eng
text: Solid‐state NMR spectroscopy can provide insight into protein structure and
dynamics at the atomic level without inherent protein size limitations. However,
a major hurdle to studying large proteins by solid‐state NMR spectroscopy is related
to spectral complexity and resonance overlap, which increase with molecular weight
and severely hamper the assignment process. Here the use of two sets of experiments
is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate
a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH),
or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be
extended to 5D). The experiments are based on efficient coherence transfers between
backbone atoms using INEPT transfers between carbons and cross‐polarization for
heteronuclear transfers. The utility of these experiments is exemplified with
application to assemblies of deuterated, fully amide‐protonated proteins from
approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies
from approximately 40 to 55 kHz. These experiments will also be applicable to
protonated proteins at higher MAS frequencies. The resonance assignment of a domain
within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is
compared to NMR assignments of the isolated domain in solution. This comparison
reveals contacts of this domain to the core of the polymeric tail tube assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Charles‐Adrien
full_name: Arnaud, Charles‐Adrien
last_name: Arnaud
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Maxime
full_name: Audin, Maxime
last_name: Audin
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Carsten
full_name: Krichel, Carsten
last_name: Krichel
- first_name: Jia‐Ying
full_name: Guan, Jia‐Ying
last_name: Guan
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Remco
full_name: Sprangers, Remco
last_name: Sprangers
- first_name: Cécile
full_name: Breyton, Cécile
last_name: Breyton
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D
correlation experiments for resonance assignment of large proteins. ChemPhysChem.
2017;18(19):2697-2703. doi:10.1002/cphc.201700572
apa: Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., …
Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments
for resonance assignment of large proteins. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201700572
chicago: Fraga, Hugo, Charles‐Adrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius
Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solid‐state NMR H–N–(C)–H and
H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.”
ChemPhysChem. Wiley, 2017. https://doi.org/10.1002/cphc.201700572.
ieee: H. Fraga et al., “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation
experiments for resonance assignment of large proteins,” ChemPhysChem,
vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.
ista: Fraga H, Arnaud C, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan
J, Boisbouvier J, Sprangers R, Breyton C, Schanda P. 2017. Solid‐state NMR H–N–(C)–H
and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins.
ChemPhysChem. 18(19), 2697–2703.
mla: Fraga, Hugo, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation
Experiments for Resonance Assignment of Large Proteins.” ChemPhysChem,
vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:10.1002/cphc.201700572.
short: H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel,
J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18
(2017) 2697–2703.
date_created: 2020-09-18T10:06:09Z
date_published: 2017-08-09T00:00:00Z
date_updated: 2021-01-12T08:19:19Z
day: '09'
doi: 10.1002/cphc.201700572
extern: '1'
intvolume: ' 18'
issue: '19'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '08'
oa_version: None
page: 2697-2703
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
- 1439-7641
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance
assignment of large proteins
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 18
year: '2017'
...
---
_id: '8447'
abstract:
- lang: eng
text: 'Solid-state NMR spectroscopy can provide site-resolved information about
protein dynamics over many time scales. Here we combine protein deuteration, fast
magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin
in microcrystals, and in particular a mutant in a region that undergoes microsecond
motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation
measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation
dispersion, to probe how the G53A mutation alters these dynamics. We report a
population-inversion of conformational states: the conformation that in the wild-type
protein is populated only sparsely becomes the predominant state. We furthermore
explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics.
We show that while quantitative interpretation of 1H relaxation remains beyond
reach under the experimental conditions, due to coherent contributions to decay,
one may extract qualitative information about flexibility.'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Petra
full_name: Rovó, Petra
last_name: Rovó
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Rasmus
full_name: Linser, Rasmus
last_name: Linser
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational
dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type
and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 2017;87(10):86-95.
doi:10.1016/j.ssnmr.2017.04.002'
apa: 'Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., & Schanda,
P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation
dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State
Nuclear Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.ssnmr.2017.04.002'
chicago: 'Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser,
and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation
Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” Solid State
Nuclear Magnetic Resonance. Elsevier, 2017. https://doi.org/10.1016/j.ssnmr.2017.04.002.'
ieee: 'D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda,
“Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
Application to wild-type and G53A ubiquitin crystals,” Solid State Nuclear
Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.'
ista: 'Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein
conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application
to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance.
87(10), 86–95.'
mla: 'Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and
1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.”
Solid State Nuclear Magnetic Resonance, vol. 87, no. 10, Elsevier, 2017,
pp. 86–95, doi:10.1016/j.ssnmr.2017.04.002.'
short: D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid
State Nuclear Magnetic Resonance 87 (2017) 86–95.
date_created: 2020-09-18T10:06:18Z
date_published: 2017-10-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.ssnmr.2017.04.002
extern: '1'
intvolume: ' 87'
issue: '10'
keyword:
- Nuclear and High Energy Physics
- Instrumentation
- General Chemistry
- Radiation
language:
- iso: eng
month: '10'
oa_version: None
page: 86-95
publication: Solid State Nuclear Magnetic Resonance
publication_identifier:
issn:
- 0926-2040
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
Application to wild-type and G53A ubiquitin crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 87
year: '2017'
...
---
_id: '8448'
abstract:
- lang: eng
text: We present an improved fast mixing device based on the rapid mixing of two
solutions inside the NMR probe, as originally proposed by Hore and coworkers (J.
Am. Chem. Soc. 125 (2003) 12484–12492). Such a device is important for off-equilibrium
studies of molecular kinetics by multidimensional real-time NMR spectrsocopy.
The novelty of this device is that it allows removing the injector from the NMR
detection volume after mixing, and thus provides good magnetic field homogeneity
independently of the initial sample volume placed in the NMR probe. The apparatus
is simple to build, inexpensive, and can be used without any hardware modification
on any type of liquid-state NMR spectrometer. We demonstrate the performance of
our fast mixing device in terms of improved magnetic field homogeneity, and show
an application to the study of protein folding and the structural characterization
of transiently populated folding intermediates.
article_processing_charge: No
article_type: original
author:
- first_name: Rémi
full_name: Franco, Rémi
last_name: Franco
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for
real-time NMR applications. Journal of Magnetic Resonance. 2017;281(8):125-129.
doi:10.1016/j.jmr.2017.05.016
apa: Franco, R., Favier, A., Schanda, P., & Brutscher, B. (2017). Optimized
fast mixing device for real-time NMR applications. Journal of Magnetic Resonance.
Elsevier. https://doi.org/10.1016/j.jmr.2017.05.016
chicago: Franco, Rémi, Adrien Favier, Paul Schanda, and Bernhard Brutscher. “Optimized
Fast Mixing Device for Real-Time NMR Applications.” Journal of Magnetic Resonance.
Elsevier, 2017. https://doi.org/10.1016/j.jmr.2017.05.016.
ieee: R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing
device for real-time NMR applications,” Journal of Magnetic Resonance,
vol. 281, no. 8. Elsevier, pp. 125–129, 2017.
ista: Franco R, Favier A, Schanda P, Brutscher B. 2017. Optimized fast mixing device
for real-time NMR applications. Journal of Magnetic Resonance. 281(8), 125–129.
mla: Franco, Rémi, et al. “Optimized Fast Mixing Device for Real-Time NMR Applications.”
Journal of Magnetic Resonance, vol. 281, no. 8, Elsevier, 2017, pp. 125–29,
doi:10.1016/j.jmr.2017.05.016.
short: R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance
281 (2017) 125–129.
date_created: 2020-09-18T10:06:27Z
date_published: 2017-08-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.jmr.2017.05.016
extern: '1'
intvolume: ' 281'
issue: '8'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '08'
oa_version: None
page: 125-129
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Optimized fast mixing device for real-time NMR applications
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 281
year: '2017'
...
---
_id: '8449'
abstract:
- lang: eng
text: Ensuring the correct folding of RNA molecules in the cell is of major importance
for a large variety of biological functions. Therefore, chaperone proteins that
assist RNA in adopting their functionally active states are abundant in all living
organisms. An important feature of RNA chaperone proteins is that they do not
require an external energy source to perform their activity, and that they interact
transiently and non-specifically with their RNA targets. So far, little is known
about the mechanistic details of the RNA chaperone activity of these proteins.
Prominent examples of RNA chaperones are bacterial cold shock proteins (Csp) that
have been reported to bind single-stranded RNA and DNA. Here, we have used advanced
NMR spectroscopy techniques to investigate at atomic resolution the RNA-melting
activity of CspA, the major cold shock protein of Escherichia coli, upon binding
to different RNA hairpins. Real-time NMR provides detailed information on the
folding kinetics and folding pathways. Finally, comparison of wild-type CspA with
single-point mutants and small peptides yields insights into the complementary
roles of aromatic and positively charged amino-acid side chains for the RNA chaperone
activity of the protein.
article_processing_charge: No
article_type: original
author:
- first_name: Enrico
full_name: Rennella, Enrico
last_name: Rennella
- first_name: Tomáš
full_name: Sára, Tomáš
last_name: Sára
- first_name: Michael
full_name: Juen, Michael
last_name: Juen
- first_name: Christoph
full_name: Wunderlich, Christoph
last_name: Wunderlich
- first_name: Lionel
full_name: Imbert, Lionel
last_name: Imbert
- first_name: Zsofia
full_name: Solyom, Zsofia
last_name: Solyom
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
- first_name: Christoph
full_name: Kreutz, Christoph
last_name: Kreutz
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Rennella E, Sára T, Juen M, et al. RNA binding and chaperone activity of the
E.coli cold-shock protein CspA. Nucleic Acids Research. 2017;45(7):4255-4268.
doi:10.1093/nar/gkx044
apa: Rennella, E., Sára, T., Juen, M., Wunderlich, C., Imbert, L., Solyom, Z., …
Brutscher, B. (2017). RNA binding and chaperone activity of the E.coli cold-shock
protein CspA. Nucleic Acids Research. Oxford University Press. https://doi.org/10.1093/nar/gkx044
chicago: Rennella, Enrico, Tomáš Sára, Michael Juen, Christoph Wunderlich, Lionel
Imbert, Zsofia Solyom, Adrien Favier, et al. “RNA Binding and Chaperone Activity
of the E.Coli Cold-Shock Protein CspA.” Nucleic Acids Research. Oxford
University Press, 2017. https://doi.org/10.1093/nar/gkx044.
ieee: E. Rennella et al., “RNA binding and chaperone activity of the E.coli
cold-shock protein CspA,” Nucleic Acids Research, vol. 45, no. 7. Oxford
University Press, pp. 4255–4268, 2017.
ista: Rennella E, Sára T, Juen M, Wunderlich C, Imbert L, Solyom Z, Favier A, Ayala
I, Weinhäupl K, Schanda P, Konrat R, Kreutz C, Brutscher B. 2017. RNA binding
and chaperone activity of the E.coli cold-shock protein CspA. Nucleic Acids Research.
45(7), 4255–4268.
mla: Rennella, Enrico, et al. “RNA Binding and Chaperone Activity of the E.Coli
Cold-Shock Protein CspA.” Nucleic Acids Research, vol. 45, no. 7, Oxford
University Press, 2017, pp. 4255–68, doi:10.1093/nar/gkx044.
short: E. Rennella, T. Sára, M. Juen, C. Wunderlich, L. Imbert, Z. Solyom, A. Favier,
I. Ayala, K. Weinhäupl, P. Schanda, R. Konrat, C. Kreutz, B. Brutscher, Nucleic
Acids Research 45 (2017) 4255–4268.
date_created: 2020-09-18T10:06:34Z
date_published: 2017-04-20T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '20'
doi: 10.1093/nar/gkx044
extern: '1'
intvolume: ' 45'
issue: '7'
language:
- iso: eng
month: '04'
oa_version: None
page: 4255-4268
publication: Nucleic Acids Research
publication_identifier:
issn:
- 0305-1048
- 1362-4962
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
status: public
title: RNA binding and chaperone activity of the E.coli cold-shock protein CspA
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 45
year: '2017'
...
---
_id: '8450'
abstract:
- lang: eng
text: Methyl groups are very useful probes of structure, dynamics, and interactions
in protein NMR spectroscopy. In particular, methyl-directed experiments provide
high sensitivity even in very large proteins, such as membrane proteins in a membrane-mimicking
environment. In this chapter, we discuss the approach for labeling methyl groups
in E. coli-based protein expression, as exemplified with the mitochondrial carrier
GGC.
alternative_title:
- Methods in Molecular Biology
article_processing_charge: No
author:
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Remy
full_name: Sounier, Remy
last_name: Sounier
citation:
ama: 'Kurauskas V, Schanda P, Sounier R. Methyl-specific isotope labeling strategies
for NMR studies of membrane proteins. In: Membrane Protein Structure and Function
Characterization. Vol 1635. Springer Nature; 2017:109-123. doi:10.1007/978-1-4939-7151-0_6'
apa: Kurauskas, V., Schanda, P., & Sounier, R. (2017). Methyl-specific isotope
labeling strategies for NMR studies of membrane proteins. In Membrane protein
structure and function characterization (Vol. 1635, pp. 109–123). Springer
Nature. https://doi.org/10.1007/978-1-4939-7151-0_6
chicago: Kurauskas, Vilius, Paul Schanda, and Remy Sounier. “Methyl-Specific Isotope
Labeling Strategies for NMR Studies of Membrane Proteins.” In Membrane Protein
Structure and Function Characterization, 1635:109–23. Springer Nature, 2017.
https://doi.org/10.1007/978-1-4939-7151-0_6.
ieee: V. Kurauskas, P. Schanda, and R. Sounier, “Methyl-specific isotope labeling
strategies for NMR studies of membrane proteins,” in Membrane protein structure
and function characterization, vol. 1635, Springer Nature, 2017, pp. 109–123.
ista: 'Kurauskas V, Schanda P, Sounier R. 2017.Methyl-specific isotope labeling
strategies for NMR studies of membrane proteins. In: Membrane protein structure
and function characterization. Methods in Molecular Biology, vol. 1635, 109–123.'
mla: Kurauskas, Vilius, et al. “Methyl-Specific Isotope Labeling Strategies for
NMR Studies of Membrane Proteins.” Membrane Protein Structure and Function
Characterization, vol. 1635, Springer Nature, 2017, pp. 109–23, doi:10.1007/978-1-4939-7151-0_6.
short: V. Kurauskas, P. Schanda, R. Sounier, in:, Membrane Protein Structure and
Function Characterization, Springer Nature, 2017, pp. 109–123.
date_created: 2020-09-18T10:06:44Z
date_published: 2017-07-29T00:00:00Z
date_updated: 2022-08-26T09:14:20Z
day: '29'
doi: 10.1007/978-1-4939-7151-0_6
extern: '1'
intvolume: ' 1635'
language:
- iso: eng
month: '07'
oa_version: None
page: 109-123
publication: Membrane protein structure and function characterization
publication_identifier:
isbn:
- '9781493971497'
- '9781493971510'
issn:
- 1064-3745
- 1940-6029
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Methyl-specific isotope labeling strategies for NMR studies of membrane proteins
type: book_chapter
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 1635
year: '2017'
...
---
_id: '8451'
abstract:
- lang: eng
text: The structure, dynamics, and function of membrane proteins are intimately
linked to the properties of the membrane environment in which the proteins are
embedded. For structural and biophysical characterization, membrane proteins generally
need to be extracted from the membrane and reconstituted in a suitable membrane‐mimicking
environment. Ensuring functional and structural integrity in these environments
is often a major concern. The styrene/maleic acid co‐polymer has recently been
shown to be able to extract lipid/membrane protein patches directly from native
membranes to form nanosize discoidal proteolipid particles, also referred to as
native nanodiscs. In this work, we show that high‐resolution solid‐state NMR spectra
can be obtained from an integral membrane protein in native nanodiscs, as exemplified
by the 2×34 kDa bacterial cation diffusion facilitator CzcD.
article_processing_charge: No
article_type: original
author:
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Jonas M.
full_name: Dörr, Jonas M.
last_name: Dörr
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: J. Antoinette
full_name: Killian, J. Antoinette
last_name: Killian
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. Proton-detected solid-state
NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs.
Angewandte Chemie International Edition. 2017;56(9):2508-2512. doi:10.1002/anie.201610441
apa: Bersch, B., Dörr, J. M., Hessel, A., Killian, J. A., & Schanda, P. (2017).
Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein
in native nanodiscs. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201610441
chicago: Bersch, Beate, Jonas M. Dörr, Audrey Hessel, J. Antoinette Killian, and
Paul Schanda. “Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion
Facilitator Protein in Native Nanodiscs.” Angewandte Chemie International Edition.
Wiley, 2017. https://doi.org/10.1002/anie.201610441.
ieee: B. Bersch, J. M. Dörr, A. Hessel, J. A. Killian, and P. Schanda, “Proton-detected
solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native
nanodiscs,” Angewandte Chemie International Edition, vol. 56, no. 9. Wiley,
pp. 2508–2512, 2017.
ista: Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. 2017. Proton-detected
solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native
nanodiscs. Angewandte Chemie International Edition. 56(9), 2508–2512.
mla: Bersch, Beate, et al. “Proton-Detected Solid-State NMR Spectroscopy of a Zinc
Diffusion Facilitator Protein in Native Nanodiscs.” Angewandte Chemie International
Edition, vol. 56, no. 9, Wiley, 2017, pp. 2508–12, doi:10.1002/anie.201610441.
short: B. Bersch, J.M. Dörr, A. Hessel, J.A. Killian, P. Schanda, Angewandte Chemie
International Edition 56 (2017) 2508–2512.
date_created: 2020-09-18T10:06:50Z
date_published: 2017-01-27T00:00:00Z
date_updated: 2021-01-12T08:19:22Z
day: '27'
doi: 10.1002/anie.201610441
extern: '1'
intvolume: ' 56'
issue: '9'
language:
- iso: eng
month: '01'
oa_version: None
page: 2508-2512
publication: Angewandte Chemie International Edition
publication_identifier:
issn:
- 1433-7851
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator
protein in native nanodiscs
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 56
year: '2017'
...
---
_id: '9065'
abstract:
- lang: eng
text: Magnetic anisotropy in strontium iridate (Sr2IrO4) is found to be large because
of the strong spin-orbit interactions. In our work, we studied the in-plane magnetic
anisotropy of Sr2IrO4 and traced the anisotropic exchange interactions between
the isospins in the crystal. The magnetic-field-dependent torque τ(H) showed a
prominent transition from the canted antiferromagnetic state to the weak ferromagnetic
(WFM) state. A comprehensive analysis was conducted to examine the isotropic and
anisotropic regimes and probe the easy magnetization axis along the a b plane.
The angle-dependent torque τ(θ) revealed a deviation from the sinusoidal behavior,
and small differences in hysteresis were observed around 0° and 90° in the low-magnetic-field
regime. This indicates that the orientation of the easy axis of the FM component
is along the b axis, where the antiferromagnetic to WFM spin-flop transition occurs.
We compared the coefficients of the magnetic susceptibility tensors and captured
the anisotropy of the material. The in-plane τ(θ) revealed a tendency toward isotropic
behavior for fields with values above the field value of the WFM transition.
article_number: '155102'
article_processing_charge: No
article_type: original
author:
- first_name: Muhammad
full_name: Nauman, Muhammad
id: 32c21954-2022-11eb-9d5f-af9f93c24e71
last_name: Nauman
orcid: 0000-0002-2111-4846
- first_name: Yunjeong
full_name: Hong, Yunjeong
last_name: Hong
- first_name: Tayyaba
full_name: Hussain, Tayyaba
last_name: Hussain
- first_name: M. S.
full_name: Seo, M. S.
last_name: Seo
- first_name: S. Y.
full_name: Park, S. Y.
last_name: Park
- first_name: N.
full_name: Lee, N.
last_name: Lee
- first_name: Y. J.
full_name: Choi, Y. J.
last_name: Choi
- first_name: Woun
full_name: Kang, Woun
last_name: Kang
- first_name: Younjung
full_name: Jo, Younjung
last_name: Jo
citation:
ama: Nauman M, Hong Y, Hussain T, et al. In-plane magnetic anisotropy in strontium
iridate Sr2IrO4. Physical Review B. 2017;96(15). doi:10.1103/physrevb.96.155102
apa: Nauman, M., Hong, Y., Hussain, T., Seo, M. S., Park, S. Y., Lee, N., … Jo,
Y. (2017). In-plane magnetic anisotropy in strontium iridate Sr2IrO4. Physical
Review B. American Physical Society. https://doi.org/10.1103/physrevb.96.155102
chicago: Nauman, Muhammad, Yunjeong Hong, Tayyaba Hussain, M. S. Seo, S. Y. Park,
N. Lee, Y. J. Choi, Woun Kang, and Younjung Jo. “In-Plane Magnetic Anisotropy
in Strontium Iridate Sr2IrO4.” Physical Review B. American Physical Society,
2017. https://doi.org/10.1103/physrevb.96.155102.
ieee: M. Nauman et al., “In-plane magnetic anisotropy in strontium iridate
Sr2IrO4,” Physical Review B, vol. 96, no. 15. American Physical Society,
2017.
ista: Nauman M, Hong Y, Hussain T, Seo MS, Park SY, Lee N, Choi YJ, Kang W, Jo Y.
2017. In-plane magnetic anisotropy in strontium iridate Sr2IrO4. Physical Review
B. 96(15), 155102.
mla: Nauman, Muhammad, et al. “In-Plane Magnetic Anisotropy in Strontium Iridate
Sr2IrO4.” Physical Review B, vol. 96, no. 15, 155102, American Physical
Society, 2017, doi:10.1103/physrevb.96.155102.
short: M. Nauman, Y. Hong, T. Hussain, M.S. Seo, S.Y. Park, N. Lee, Y.J. Choi, W.
Kang, Y. Jo, Physical Review B 96 (2017).
date_created: 2021-02-02T15:49:21Z
date_published: 2017-10-01T00:00:00Z
date_updated: 2021-02-03T12:53:00Z
day: '01'
doi: 10.1103/physrevb.96.155102
extern: '1'
intvolume: ' 96'
issue: '15'
language:
- iso: eng
month: '10'
oa_version: None
publication: Physical Review B
publication_identifier:
issn:
- 2469-9950
- 2469-9969
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
status: public
title: In-plane magnetic anisotropy in strontium iridate Sr2IrO4
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 96
year: '2017'
...
---
_id: '909'
abstract:
- lang: eng
text: We study the lengths of curves passing through a fixed number of points on
the boundary of a convex shape in the plane. We show that, for any convex shape
K, there exist four points on the boundary of K such that the length of any curve
passing through these points is at least half of the perimeter of K. It is also
shown that the same statement does not remain valid with the additional constraint
that the points are extreme points of K. Moreover, the factor ½ cannot
be achieved with any fixed number of extreme points. We conclude the paper with
a few other inequalities related to the perimeter of a convex shape.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Arseniy
full_name: Akopyan, Arseniy
id: 430D2C90-F248-11E8-B48F-1D18A9856A87
last_name: Akopyan
orcid: 0000-0002-2548-617X
- first_name: Vladislav
full_name: Vysotsky, Vladislav
last_name: Vysotsky
citation:
ama: Akopyan A, Vysotsky V. On the lengths of curves passing through boundary points
of a planar convex shape. The American Mathematical Monthly. 2017;124(7):588-596.
doi:10.4169/amer.math.monthly.124.7.588
apa: Akopyan, A., & Vysotsky, V. (2017). On the lengths of curves passing through
boundary points of a planar convex shape. The American Mathematical Monthly.
Mathematical Association of America. https://doi.org/10.4169/amer.math.monthly.124.7.588
chicago: Akopyan, Arseniy, and Vladislav Vysotsky. “On the Lengths of Curves Passing
through Boundary Points of a Planar Convex Shape.” The American Mathematical
Monthly. Mathematical Association of America, 2017. https://doi.org/10.4169/amer.math.monthly.124.7.588.
ieee: A. Akopyan and V. Vysotsky, “On the lengths of curves passing through boundary
points of a planar convex shape,” The American Mathematical Monthly, vol.
124, no. 7. Mathematical Association of America, pp. 588–596, 2017.
ista: Akopyan A, Vysotsky V. 2017. On the lengths of curves passing through boundary
points of a planar convex shape. The American Mathematical Monthly. 124(7), 588–596.
mla: Akopyan, Arseniy, and Vladislav Vysotsky. “On the Lengths of Curves Passing
through Boundary Points of a Planar Convex Shape.” The American Mathematical
Monthly, vol. 124, no. 7, Mathematical Association of America, 2017, pp. 588–96,
doi:10.4169/amer.math.monthly.124.7.588.
short: A. Akopyan, V. Vysotsky, The American Mathematical Monthly 124 (2017) 588–596.
date_created: 2018-12-11T11:49:09Z
date_published: 2017-01-01T00:00:00Z
date_updated: 2025-07-10T12:01:35Z
day: '01'
department:
- _id: HeEd
doi: 10.4169/amer.math.monthly.124.7.588
ec_funded: 1
external_id:
arxiv:
- '1605.07997'
isi:
- '000413947300002'
intvolume: ' 124'
isi: 1
issue: '7'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1605.07997
month: '01'
oa: 1
oa_version: Submitted Version
page: 588 - 596
project:
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
publication: The American Mathematical Monthly
publication_identifier:
issn:
- 0002-9890
publication_status: published
publisher: Mathematical Association of America
publist_id: '6534'
quality_controlled: '1'
scopus_import: '1'
status: public
title: On the lengths of curves passing through boundary points of a planar convex
shape
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 124
year: '2017'
...
---
_id: '910'
abstract:
- lang: eng
text: "Frequency-independent selection is generally considered as a force that acts
to reduce the genetic variation in evolving populations, yet rigorous arguments
for this idea are scarce. When selection fluctuates in time, it is unclear whether
frequency-independent selection may maintain genetic polymorphism without invoking
additional mechanisms. We show that constant frequency-independent selection with
arbitrary epistasis on a well-mixed haploid population eliminates genetic variation
if we assume linkage equilibrium between alleles. To this end, we introduce the
notion of frequency-independent selection at the level of alleles, which is sufficient
to prove our claim and contains the notion of frequency-independent selection
on haploids. When selection and recombination are weak but of the same order,
there may be strong linkage disequilibrium; numerical calculations show that stable
equilibria are highly unlikely. Using the example of a diallelic two-locus model,
we then demonstrate that frequency-independent selection that fluctuates in time
can maintain stable polymorphism if linkage disequilibrium changes its sign periodically.
We put our findings in the context of results from the existing literature and
point out those scenarios in which the possible role of frequency-independent
selection in maintaining genetic variation remains unclear.\r\n"
article_processing_charge: No
author:
- first_name: Sebastian
full_name: Novak, Sebastian
id: 461468AE-F248-11E8-B48F-1D18A9856A87
last_name: Novak
orcid: 0000-0002-2519-824X
- first_name: Nicholas H
full_name: Barton, Nicholas H
id: 4880FE40-F248-11E8-B48F-1D18A9856A87
last_name: Barton
orcid: 0000-0002-8548-5240
citation:
ama: Novak S, Barton NH. When does frequency-independent selection maintain genetic
variation? Genetics. 2017;207(2):653-668. doi:10.1534/genetics.117.300129
apa: Novak, S., & Barton, N. H. (2017). When does frequency-independent selection
maintain genetic variation? Genetics. Genetics Society of America. https://doi.org/10.1534/genetics.117.300129
chicago: Novak, Sebastian, and Nicholas H Barton. “When Does Frequency-Independent
Selection Maintain Genetic Variation?” Genetics. Genetics Society of America,
2017. https://doi.org/10.1534/genetics.117.300129.
ieee: S. Novak and N. H. Barton, “When does frequency-independent selection maintain
genetic variation?,” Genetics, vol. 207, no. 2. Genetics Society of America,
pp. 653–668, 2017.
ista: Novak S, Barton NH. 2017. When does frequency-independent selection maintain
genetic variation? Genetics. 207(2), 653–668.
mla: Novak, Sebastian, and Nicholas H. Barton. “When Does Frequency-Independent
Selection Maintain Genetic Variation?” Genetics, vol. 207, no. 2, Genetics
Society of America, 2017, pp. 653–68, doi:10.1534/genetics.117.300129.
short: S. Novak, N.H. Barton, Genetics 207 (2017) 653–668.
corr_author: '1'
date_created: 2018-12-11T11:49:09Z
date_published: 2017-10-01T00:00:00Z
date_updated: 2025-04-15T08:22:21Z
day: '01'
ddc:
- '576'
department:
- _id: NiBa
doi: 10.1534/genetics.117.300129
ec_funded: 1
external_id:
isi:
- '000412232600019'
file:
- access_level: open_access
checksum: f7c32dabf52e6d9e709d9203761e39fd
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:17:12Z
date_updated: 2020-07-14T12:48:15Z
file_id: '5264'
file_name: IST-2018-974-v1+1_manuscript.pdf
file_size: 494268
relation: main_file
file_date_updated: 2020-07-14T12:48:15Z
has_accepted_license: '1'
intvolume: ' 207'
isi: 1
issue: '2'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Submitted Version
page: 653 - 668
project:
- _id: 25B1EC9E-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '618091'
name: Speed of Adaptation in Population Genetics and Evolutionary Computation
publication: Genetics
publication_status: published
publisher: Genetics Society of America
publist_id: '6533'
pubrep_id: '974'
quality_controlled: '1'
scopus_import: '1'
status: public
title: When does frequency-independent selection maintain genetic variation?
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 207
year: '2017'
...
---
_id: '912'
abstract:
- lang: eng
text: "We consider a many-body system of fermionic atoms interacting via a local
pair potential and subject to an external potential within the framework of Bardeen-Cooper-Schrieffer
(BCS) theory. We measure the free energy of the whole sample with respect to the
free energy of a reference state which allows us to define a BCS functional with
boundary conditions at infinity. Our main result is a lower bound for this energy
functional in terms of expressions that typically appear in Ginzburg-Landau functionals.\r\n"
article_number: '081901'
article_processing_charge: No
arxiv: 1
author:
- first_name: Andreas
full_name: Deuchert, Andreas
id: 4DA65CD0-F248-11E8-B48F-1D18A9856A87
last_name: Deuchert
orcid: 0000-0003-3146-6746
citation:
ama: Deuchert A. A lower bound for the BCS functional with boundary conditions at
infinity. Journal of Mathematical Physics. 2017;58(8). doi:10.1063/1.4996580
apa: Deuchert, A. (2017). A lower bound for the BCS functional with boundary conditions
at infinity. Journal of Mathematical Physics. AIP Publishing. https://doi.org/10.1063/1.4996580
chicago: Deuchert, Andreas. “A Lower Bound for the BCS Functional with Boundary
Conditions at Infinity.” Journal of Mathematical Physics. AIP Publishing,
2017. https://doi.org/10.1063/1.4996580.
ieee: A. Deuchert, “A lower bound for the BCS functional with boundary conditions
at infinity,” Journal of Mathematical Physics, vol. 58, no. 8. AIP Publishing,
2017.
ista: Deuchert A. 2017. A lower bound for the BCS functional with boundary conditions
at infinity. Journal of Mathematical Physics. 58(8), 081901.
mla: Deuchert, Andreas. “A Lower Bound for the BCS Functional with Boundary Conditions
at Infinity.” Journal of Mathematical Physics, vol. 58, no. 8, 081901,
AIP Publishing, 2017, doi:10.1063/1.4996580.
short: A. Deuchert, Journal of Mathematical Physics 58 (2017).
corr_author: '1'
date_created: 2018-12-11T11:49:10Z
date_published: 2017-08-01T00:00:00Z
date_updated: 2025-06-04T08:19:58Z
day: '01'
department:
- _id: RoSe
doi: 10.1063/1.4996580
ec_funded: 1
external_id:
arxiv:
- '1703.04616'
isi:
- '000409197200015'
intvolume: ' 58'
isi: 1
issue: '8'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1703.04616
month: '08'
oa: 1
oa_version: Submitted Version
project:
- _id: 25C6DC12-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '694227'
name: Analysis of quantum many-body systems
publication: ' Journal of Mathematical Physics'
publication_identifier:
issn:
- 0022-2488
publication_status: published
publisher: AIP Publishing
publist_id: '6531'
quality_controlled: '1'
scopus_import: '1'
status: public
title: A lower bound for the BCS functional with boundary conditions at infinity
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 58
year: '2017'
...