---
_id: '8313'
abstract:
- lang: eng
text: The present invention concerns a computer-implemented method for secure data
exchange between a sender (A) and a recipient (B), wherein the method is performed
by the sender (A) and comprises encrypting data using a symmetric key k, creating
a write transaction T W , wherein the write transaction T W comprises information
usable to derive the symmetric key k and an access policy identifying the recipient
(B) as being allowed to decrypt the encrypted data, providing the recipient (B)
access to the encrypted data, and sending the write transaction T W to a first
group of servers (AC) for being stored in a blockchain data structure maintained
by the first group of servers (AC).
applicant:
- 'École Polytechnique Fédérale De Lausanne '
article_processing_charge: No
author:
- first_name: Bryan
full_name: Ford, Bryan
last_name: Ford
- first_name: Linus
full_name: Gasser, Linus
last_name: Gasser
- first_name: Eleftherios
full_name: Kokoris Kogias, Eleftherios
id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
last_name: Kokoris Kogias
- first_name: Philipp
full_name: Janovic, Philipp
last_name: Janovic
citation:
ama: Ford B, Gasser L, Kokoris Kogias E, Janovic P. Methods and systems for secure
data exchange. 2019.
apa: Ford, B., Gasser, L., Kokoris Kogias, E., & Janovic, P. (2019). Methods
and systems for secure data exchange.
chicago: Ford, Bryan, Linus Gasser, Eleftherios Kokoris Kogias, and Philipp Janovic.
“Methods and Systems for Secure Data Exchange,” 2019.
ieee: B. Ford, L. Gasser, E. Kokoris Kogias, and P. Janovic, “Methods and systems
for secure data exchange.” 2019.
ista: Ford B, Gasser L, Kokoris Kogias E, Janovic P. 2019. Methods and systems for
secure data exchange.
mla: Ford, Bryan, et al. Methods and Systems for Secure Data Exchange. 2019.
short: B. Ford, L. Gasser, E. Kokoris Kogias, P. Janovic, (2019).
date_created: 2020-08-27T11:24:44Z
date_published: 2019-08-22T00:00:00Z
date_updated: 2022-01-05T14:00:32Z
day: '22'
extern: '1'
ipc: G06F21/62 ; H04L9/08 ; H04L9/32
ipn: WO2019158209 (A1)
main_file_link:
- open_access: '1'
url: https://patents.google.com/patent/WO2019158209A1
month: '08'
oa: 1
oa_version: Published Version
publication_date: 2019-08-22
status: public
title: Methods and systems for secure data exchange
type: patent
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2019'
...
---
_id: '8314'
abstract:
- lang: eng
text: "Off-chain protocols (channels) are a promising solution to the scalability
and privacy challenges of blockchain payments. Current proposals, however, require
synchrony assumptions to preserve the safety of a channel, leaking to an adversary
the exact amount of time needed to control the network for a successful attack.
In this paper, we introduce Brick, the first payment channel that remains secure
under network asynchrony and concurrently provides correct incentives. The core
idea is to incorporate the conflict resolution process within the channel by introducing
a rational committee of external parties, called Wardens. Hence, if a party wants
to close a channel unilaterally, it can only get the committee's approval for
the last valid state. Brick provides sub-second latency because it does not employ
heavy-weight consensus. Instead,\r\nBrick uses consistent broadcast to announce
updates and close the channel, a light-weight abstraction that is powerful enough
to preserve safety and liveness to any rational parties. Furthermore, we consider
permissioned blockchains, where the additional property of auditability might
be desired for regulatory purposes. We introduce Brick+, an off-chain construction
that provides auditability on top of Brick without conflicting with its privacy
guarantees. We formally define the properties our payment channel construction
should fulfill, and prove that both Brick and Brick+ satisfy them. We also design
incentives for Brick such that honest and rational behavior aligns. Finally, we
provide a reference implementation of the smart contracts in Solidity."
article_number: '1905.11360'
article_processing_charge: No
arxiv: 1
author:
- first_name: Georgia
full_name: Avarikioti, Georgia
last_name: Avarikioti
- first_name: Eleftherios
full_name: Kokoris Kogias, Eleftherios
id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
last_name: Kokoris Kogias
- first_name: Roger
full_name: Wattenhofer, Roger
last_name: Wattenhofer
- first_name: Dionysis
full_name: Zindros, Dionysis
last_name: Zindros
citation:
ama: 'Avarikioti G, Kokoris Kogias E, Wattenhofer R, Zindros D. Brick: Asynchronous
payment channels. arXiv. doi:10.48550/arXiv.1905.11360'
apa: 'Avarikioti, G., Kokoris Kogias, E., Wattenhofer, R., & Zindros, D. (n.d.).
Brick: Asynchronous payment channels. arXiv. https://doi.org/10.48550/arXiv.1905.11360'
chicago: 'Avarikioti, Georgia, Eleftherios Kokoris Kogias, Roger Wattenhofer, and
Dionysis Zindros. “Brick: Asynchronous Payment Channels.” ArXiv, n.d. https://doi.org/10.48550/arXiv.1905.11360.'
ieee: 'G. Avarikioti, E. Kokoris Kogias, R. Wattenhofer, and D. Zindros, “Brick:
Asynchronous payment channels,” arXiv. .'
ista: 'Avarikioti G, Kokoris Kogias E, Wattenhofer R, Zindros D. Brick: Asynchronous
payment channels. arXiv, 1905.11360.'
mla: 'Avarikioti, Georgia, et al. “Brick: Asynchronous Payment Channels.” ArXiv,
1905.11360, doi:10.48550/arXiv.1905.11360.'
short: G. Avarikioti, E. Kokoris Kogias, R. Wattenhofer, D. Zindros, ArXiv (n.d.).
date_created: 2020-08-27T11:36:54Z
date_published: 2019-05-27T00:00:00Z
date_updated: 2025-06-26T11:26:45Z
day: '27'
doi: 10.48550/arXiv.1905.11360
extern: '1'
external_id:
arxiv:
- '1905.11360'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1905.11360
month: '05'
oa: 1
oa_version: Preprint
publication: arXiv
publication_status: submitted
status: public
title: 'Brick: Asynchronous payment channels'
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2019'
...
---
_id: '8315'
abstract:
- lang: eng
text: "Sharding distributed ledgers is the most promising on-chain solution for
scaling blockchain technology. In this work, we define and analyze the properties
a sharded distributed ledger should fulfill. More specifically, we show that a
sharded blockchain cannot be scalable under a fully adaptive adversary, but it
can scale up to $O(n/\\log n)$ under an epoch-adaptive adversary. This is possible
only if the distributed ledger creates succinct proofs of the valid state updates
at the end of each epoch. Our model builds upon and extends the Bitcoin backbone
protocol by defining consistency and\r\nscalability. Consistency encompasses the
need for atomic execution of cross-shard transactions to preserve safety, whereas
scalability encapsulates the speedup a sharded system can gain in comparison to
a non-sharded system. In\r\norder to show the power of our framework, we analyze
the most prominent sharded blockchains and either prove their correctness (OmniLedger,
RapidChain) under our model or pinpoint where they fail to balance the consistency
and\r\nscalability requirements (Elastico, Monoxide). "
article_number: '1910.10434'
article_processing_charge: No
arxiv: 1
author:
- first_name: Georgia
full_name: Avarikioti, Georgia
last_name: Avarikioti
- first_name: Eleftherios
full_name: Kokoris Kogias, Eleftherios
id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
last_name: Kokoris Kogias
- first_name: Roger
full_name: Wattenhofer, Roger
last_name: Wattenhofer
citation:
ama: 'Avarikioti G, Kokoris Kogias E, Wattenhofer R. Divide and scale: Formalization
of distributed ledger sharding protocols. arXiv. doi:10.48550/arXiv.1910.10434'
apa: 'Avarikioti, G., Kokoris Kogias, E., & Wattenhofer, R. (n.d.). Divide and
scale: Formalization of distributed ledger sharding protocols. arXiv. https://doi.org/10.48550/arXiv.1910.10434'
chicago: 'Avarikioti, Georgia, Eleftherios Kokoris Kogias, and Roger Wattenhofer.
“Divide and Scale: Formalization of Distributed Ledger Sharding Protocols.” ArXiv,
n.d. https://doi.org/10.48550/arXiv.1910.10434.'
ieee: 'G. Avarikioti, E. Kokoris Kogias, and R. Wattenhofer, “Divide and scale:
Formalization of distributed ledger sharding protocols,” arXiv. .'
ista: 'Avarikioti G, Kokoris Kogias E, Wattenhofer R. Divide and scale: Formalization
of distributed ledger sharding protocols. arXiv, 1910.10434.'
mla: 'Avarikioti, Georgia, et al. “Divide and Scale: Formalization of Distributed
Ledger Sharding Protocols.” ArXiv, 1910.10434, doi:10.48550/arXiv.1910.10434.'
short: G. Avarikioti, E. Kokoris Kogias, R. Wattenhofer, ArXiv (n.d.).
date_created: 2020-08-27T11:37:43Z
date_published: 2019-10-23T00:00:00Z
date_updated: 2025-06-26T11:28:33Z
day: '23'
doi: 10.48550/arXiv.1910.10434
extern: '1'
external_id:
arxiv:
- '1910.10434'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1910.10434
month: '10'
oa: 1
oa_version: Preprint
publication: arXiv
publication_status: submitted
status: public
title: 'Divide and scale: Formalization of distributed ledger sharding protocols'
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2019'
...
---
_id: '8405'
abstract:
- lang: eng
text: Atomic-resolution structure determination is crucial for understanding protein
function. Cryo-EM and NMR spectroscopy both provide structural information, but
currently cryo-EM does not routinely give access to atomic-level structural data,
and, generally, NMR structure determination is restricted to small (<30 kDa) proteins.
We introduce an integrated structure determination approach that simultaneously
uses NMR and EM data to overcome the limits of each of these methods. The approach
enables structure determination of the 468 kDa large dodecameric aminopeptidase
TET2 to a precision and accuracy below 1 Å by combining secondary-structure information
obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large
subunits, distance restraints from backbone amides and ILV methyl groups, and
a 4.1 Å resolution EM map. The resulting structure exceeds current standards of
NMR and EM structure determination in terms of molecular weight and precision.
Importantly, the approach is successful even in cases where only medium-resolution
cryo-EM data are available.
article_number: '2697'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Leandro F.
full_name: Estrozi, Leandro F.
last_name: Estrozi
- first_name: Charles D.
full_name: Schwieters, Charles D.
last_name: Schwieters
- first_name: Gregory
full_name: Effantin, Gregory
last_name: Effantin
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Remy
full_name: Sounier, Remy
last_name: Sounier
- first_name: Astrid C.
full_name: Sivertsen, Astrid C.
last_name: Sivertsen
- first_name: Elena
full_name: Schmidt, Elena
last_name: Schmidt
- first_name: Rime
full_name: Kerfah, Rime
last_name: Kerfah
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Peter
full_name: Güntert, Peter
last_name: Güntert
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution
structure determination of a half-megadalton enzyme complex. Nature Communications.
2019;10. doi:10.1038/s41467-019-10490-9
apa: Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier,
R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
chicago: Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin,
Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM
Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”
Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9.
ieee: D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex,” Nature Communications,
vol. 10. Springer Nature, 2019.
ista: Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen
AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G,
Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications. 10,
2697.
mla: Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure
Determination of a Half-Megadalton Enzyme Complex.” Nature Communications,
vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.
short: D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier,
A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A.
Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
date_created: 2020-09-17T10:28:25Z
date_published: 2019-06-19T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '19'
doi: 10.1038/s41467-019-10490-9
extern: '1'
external_id:
pmid:
- '31217444'
intvolume: ' 10'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-019-10490-9
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton
enzyme complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2019'
...
---
_id: '8406'
abstract:
- lang: eng
text: Coordinated conformational transitions in oligomeric enzymatic complexes modulate
function in response to substrates and play a crucial role in enzyme inhibition
and activation. Caseinolytic protease (ClpP) is a tetradecameric complex, which
has emerged as a drug target against multiple pathogenic bacteria. Activation
of different ClpPs by inhibitors has been independently reported from drug development
efforts, but no rationale for inhibitor-induced activation has been hitherto proposed.
Using an integrated approach that includes x-ray crystallography, solid- and solution-state
nuclear magnetic resonance, molecular dynamics simulations, and isothermal titration
calorimetry, we show that the proteasome inhibitor bortezomib binds to the ClpP
active-site serine, mimicking a peptide substrate, and induces a concerted allosteric
activation of the complex. The bortezomib-activated conformation also exhibits
a higher affinity for its cognate unfoldase ClpX. We propose a universal allosteric
mechanism, where substrate binding to a single subunit locks ClpP into an active
conformation optimized for chaperone association and protein processive degradation.
article_number: eaaw3818
article_processing_charge: No
article_type: original
author:
- first_name: Jan
full_name: Felix, Jan
last_name: Felix
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Cecile
full_name: Morlot, Cecile
last_name: Morlot
- first_name: Olga
full_name: Abian, Olga
last_name: Abian
- first_name: Irina
full_name: Gutsche, Irina
last_name: Gutsche
- first_name: Adrian
full_name: Velazquez-Campoy, Adrian
last_name: Velazquez-Campoy
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
citation:
ama: Felix J, Weinhäupl K, Chipot C, et al. Mechanism of the allosteric activation
of the ClpP protease machinery by substrates and active-site inhibitors. Science
Advances. 2019;5(9). doi:10.1126/sciadv.aaw3818
apa: Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F.,
… Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease
machinery by substrates and active-site inhibitors. Science Advances. American
Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw3818
chicago: Felix, Jan, Katharina Weinhäupl, Christophe Chipot, François Dehez, Audrey
Hessel, Diego F. Gauto, Cecile Morlot, et al. “Mechanism of the Allosteric Activation
of the ClpP Protease Machinery by Substrates and Active-Site Inhibitors.” Science
Advances. American Association for the Advancement of Science, 2019. https://doi.org/10.1126/sciadv.aaw3818.
ieee: J. Felix et al., “Mechanism of the allosteric activation of the ClpP
protease machinery by substrates and active-site inhibitors,” Science Advances,
vol. 5, no. 9. American Association for the Advancement of Science, 2019.
ista: Felix J, Weinhäupl K, Chipot C, Dehez F, Hessel A, Gauto DF, Morlot C, Abian
O, Gutsche I, Velazquez-Campoy A, Schanda P, Fraga H. 2019. Mechanism of the allosteric
activation of the ClpP protease machinery by substrates and active-site inhibitors.
Science Advances. 5(9), eaaw3818.
mla: Felix, Jan, et al. “Mechanism of the Allosteric Activation of the ClpP Protease
Machinery by Substrates and Active-Site Inhibitors.” Science Advances,
vol. 5, no. 9, eaaw3818, American Association for the Advancement of Science,
2019, doi:10.1126/sciadv.aaw3818.
short: J. Felix, K. Weinhäupl, C. Chipot, F. Dehez, A. Hessel, D.F. Gauto, C. Morlot,
O. Abian, I. Gutsche, A. Velazquez-Campoy, P. Schanda, H. Fraga, Science Advances
5 (2019).
date_created: 2020-09-17T10:28:36Z
date_published: 2019-09-04T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '04'
doi: 10.1126/sciadv.aaw3818
extern: '1'
intvolume: ' 5'
issue: '9'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.1126/sciadv.aaw3818'
month: '09'
oa: 1
oa_version: Published Version
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
status: public
title: Mechanism of the allosteric activation of the ClpP protease machinery by substrates
and active-site inhibitors
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2019'
...
---
_id: '8407'
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
citation:
ama: Schanda P. Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. 2019;306:180-186. doi:10.1016/j.jmr.2019.07.025
apa: Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2019.07.025
chicago: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
Dynamics.” Journal of Magnetic Resonance. Elsevier, 2019. https://doi.org/10.1016/j.jmr.2019.07.025.
ieee: P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular
dynamics,” Journal of Magnetic Resonance, vol. 306. Elsevier, pp. 180–186,
2019.
ista: Schanda P. 2019. Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. 306, 180–186.
mla: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
Dynamics.” Journal of Magnetic Resonance, vol. 306, Elsevier, 2019, pp.
180–86, doi:10.1016/j.jmr.2019.07.025.
short: P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186.
date_created: 2020-09-17T10:28:47Z
date_published: 2019-09-01T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '01'
doi: 10.1016/j.jmr.2019.07.025
extern: '1'
external_id:
pmid:
- '31350165'
intvolume: ' 306'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '09'
oa_version: Submitted Version
page: 180-186
pmid: 1
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Relaxing with liquids and solids – A perspective on biomolecular dynamics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 306
year: '2019'
...
---
_id: '8408'
abstract:
- lang: eng
text: Aromatic residues are located at structurally important sites of many proteins.
Probing their interactions and dynamics can provide important functional insight
but is challenging in large proteins. Here, we introduce approaches to characterize
dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning
(MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields
isolated two-spin systems that are ideally suited for artefact-free dynamics measurements,
and allows probing motions effectively without molecular-weight limitations. The
application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest
protein assigned by MAS NMR, provides insights into motions occurring on a wide
range of time scales (ps-ms). We quantitatively probe ring flip motions, and show
the temperature dependence by MAS NMR measurements down to 100 K. Interestingly,
favorable line widths are observed down to 100 K, with potential implications
for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion
measurements and detect structural excursions occurring on a microsecond time
scale in the entry pore to the catalytic chamber and at a trimer interface that
was proposed as exit pore. We show that the labeling scheme with deuteration at
ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments
with protonated, uniformly 13C-labeled samples.
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Alessandro
full_name: Barducci, Alessandro
last_name: Barducci
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Tsutomu
full_name: Terauchi, Tsutomu
last_name: Terauchi
- first_name: David
full_name: Gajan, David
last_name: Gajan
- first_name: Yohei
full_name: Miyanoiri, Yohei
last_name: Miyanoiri
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Masatsune
full_name: Kainosho, Masatsune
last_name: Kainosho
- 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, Macek P, Barducci A, et al. Aromatic ring dynamics, thermal activation,
and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and
fast magic-angle spinning NMR. Journal of the American Chemical Society.
2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
apa: Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T.,
… Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient
conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle
spinning NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.9b04219
chicago: Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel,
Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation,
and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and
Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society.
American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219.
ieee: D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and
transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast
magic-angle spinning NMR,” Journal of the American Chemical Society, vol.
141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
ista: Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri
Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics,
thermal activation, and transient conformations of a 468 kDa enzyme by specific
1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical
Society. 141(28), 11183–11195.
mla: Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient
Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle
Spinning NMR.” Journal of the American Chemical Society, vol. 141, no.
28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.
short: D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan,
Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal
of the American Chemical Society 141 (2019) 11183–11195.
date_created: 2020-09-17T10:29:00Z
date_published: 2019-06-14T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '14'
doi: 10.1021/jacs.9b04219
extern: '1'
external_id:
pmid:
- '31199882'
intvolume: ' 141'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: Submitted Version
page: 11183-11195
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Aromatic ring dynamics, thermal activation, and transient conformations of
a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '8409'
abstract:
- lang: eng
text: The bacterial cell wall is composed of the peptidoglycan (PG), a large polymer
that maintains the integrity of the bacterial cell. Due to its multi-gigadalton
size, heterogeneity, and dynamics, atomic-resolution studies are inherently complex.
Solid-state NMR is an important technique to gain insight into its structure,
dynamics and interactions. Here, we explore the possibilities to study the PG
with ultra-fast (100 kHz) magic-angle spinning NMR. We demonstrate that highly
resolved spectra can be obtained, and show strategies to obtain site-specific
resonance assignments and distance information. We also explore the use of proton-proton
correlation experiments, thus opening the way for NMR studies of intact cell walls
without the need for isotope labeling.
article_processing_charge: No
article_type: original
author:
- first_name: Catherine
full_name: Bougault, Catherine
last_name: Bougault
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Bougault C, Ayala I, Vollmer W, Simorre J-P, Schanda P. Studying intact bacterial
peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal
of Structural Biology. 2019;206(1):66-72. doi:10.1016/j.jsb.2018.07.009
apa: Bougault, C., Ayala, I., Vollmer, W., Simorre, J.-P., & Schanda, P. (2019).
Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at
100 kHz MAS frequency. Journal of Structural Biology. Elsevier. https://doi.org/10.1016/j.jsb.2018.07.009
chicago: Bougault, Catherine, Isabel Ayala, Waldemar Vollmer, Jean-Pierre Simorre,
and Paul Schanda. “Studying Intact Bacterial Peptidoglycan by Proton-Detected
NMR Spectroscopy at 100 kHz MAS Frequency.” Journal of Structural Biology.
Elsevier, 2019. https://doi.org/10.1016/j.jsb.2018.07.009.
ieee: C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, and P. Schanda, “Studying
intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz
MAS frequency,” Journal of Structural Biology, vol. 206, no. 1. Elsevier,
pp. 66–72, 2019.
ista: Bougault C, Ayala I, Vollmer W, Simorre J-P, Schanda P. 2019. Studying intact
bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency.
Journal of Structural Biology. 206(1), 66–72.
mla: Bougault, Catherine, et al. “Studying Intact Bacterial Peptidoglycan by Proton-Detected
NMR Spectroscopy at 100 kHz MAS Frequency.” Journal of Structural Biology,
vol. 206, no. 1, Elsevier, 2019, pp. 66–72, doi:10.1016/j.jsb.2018.07.009.
short: C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, P. Schanda, Journal of
Structural Biology 206 (2019) 66–72.
date_created: 2020-09-17T10:29:10Z
date_published: 2019-04-01T00:00:00Z
date_updated: 2021-01-12T08:19:05Z
day: '01'
doi: 10.1016/j.jsb.2018.07.009
extern: '1'
external_id:
pmid:
- '30031884'
intvolume: ' 206'
issue: '1'
keyword:
- Structural Biology
language:
- iso: eng
month: '04'
oa_version: Submitted Version
page: 66-72
pmid: 1
publication: Journal of Structural Biology
publication_identifier:
issn:
- 1047-8477
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy
at 100 kHz MAS frequency
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 206
year: '2019'
...
---
_id: '8410'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Eduard Y.
full_name: Chekmenev, Eduard Y.
last_name: Chekmenev
citation:
ama: Schanda P, Chekmenev EY. NMR for Biological Systems. ChemPhysChem. 2019;20(2):177-177.
doi:10.1002/cphc.201801100
apa: Schanda, P., & Chekmenev, E. Y. (2019). NMR for Biological Systems. ChemPhysChem.
Wiley. https://doi.org/10.1002/cphc.201801100
chicago: Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” ChemPhysChem.
Wiley, 2019. https://doi.org/10.1002/cphc.201801100.
ieee: P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” ChemPhysChem,
vol. 20, no. 2. Wiley, pp. 177–177, 2019.
ista: Schanda P, Chekmenev EY. 2019. NMR for Biological Systems. ChemPhysChem. 20(2),
177–177.
mla: Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” ChemPhysChem,
vol. 20, no. 2, Wiley, 2019, pp. 177–177, doi:10.1002/cphc.201801100.
short: P. Schanda, E.Y. Chekmenev, ChemPhysChem 20 (2019) 177–177.
date_created: 2020-09-17T10:29:26Z
date_published: 2019-01-21T00:00:00Z
date_updated: 2021-01-12T08:19:05Z
day: '21'
doi: 10.1002/cphc.201801100
extern: '1'
external_id:
pmid:
- '30556633'
intvolume: ' 20'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/cphc.201801100
month: '01'
oa: 1
oa_version: Published Version
page: 177-177
pmid: 1
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: NMR for Biological Systems
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '8411'
abstract:
- lang: eng
text: 'Studying protein dynamics on microsecond‐to‐millisecond (μs‐ms) time scales
can provide important insight into protein function. In magic‐angle‐spinning (MAS)
NMR, μs dynamics can be visualized by R1p rotating‐frame relaxation dispersion
experiments in different regimes of radio‐frequency field strengths: at low RF
field strength, isotropic‐chemical‐shift fluctuation leads to “Bloch‐McConnell‐type”
relaxation dispersion, while when the RF field approaches rotary resonance conditions
bond angle fluctuations manifest as increased R1p rate constants (“Near‐Rotary‐Resonance
Relaxation Dispersion”, NERRD). Here we explore the joint analysis of both regimes
to gain comprehensive insight into motion in terms of geometric amplitudes, chemical‐shift
changes, populations and exchange kinetics. We use a numerical simulation procedure
to illustrate these effects and the potential of extracting exchange parameters,
and apply the methodology to the study of a previously described conformational
exchange process in microcrystalline ubiquitin.'
article_processing_charge: No
article_type: original
author:
- first_name: Dominique
full_name: Marion, Dominique
last_name: Marion
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Karine
full_name: Giandoreggio-Barranco, Karine
last_name: Giandoreggio-Barranco
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. Microsecond
protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion
MAS NMR. ChemPhysChem. 2019;20(2):276-284. doi:10.1002/cphc.201800935
apa: Marion, D., Gauto, D. F., Ayala, I., Giandoreggio-Barranco, K., & Schanda,
P. (2019). Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
R1p relaxation-dispersion MAS NMR. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800935
chicago: Marion, Dominique, Diego F. Gauto, Isabel Ayala, Karine Giandoreggio-Barranco,
and Paul Schanda. “Microsecond Protein Dynamics from Combined Bloch-McConnell
and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” ChemPhysChem.
Wiley, 2019. https://doi.org/10.1002/cphc.201800935.
ieee: D. Marion, D. F. Gauto, I. Ayala, K. Giandoreggio-Barranco, and P. Schanda,
“Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
R1p relaxation-dispersion MAS NMR,” ChemPhysChem, vol. 20, no. 2. Wiley,
pp. 276–284, 2019.
ista: Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. 2019. Microsecond
protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion
MAS NMR. ChemPhysChem. 20(2), 276–284.
mla: Marion, Dominique, et al. “Microsecond Protein Dynamics from Combined Bloch-McConnell
and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” ChemPhysChem,
vol. 20, no. 2, Wiley, 2019, pp. 276–84, doi:10.1002/cphc.201800935.
short: D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem
20 (2019) 276–284.
date_created: 2020-09-17T10:29:36Z
date_published: 2019-01-21T00:00:00Z
date_updated: 2021-01-12T08:19:06Z
day: '21'
doi: 10.1002/cphc.201800935
extern: '1'
external_id:
pmid:
- '30444575'
intvolume: ' 20'
issue: '2'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 276-284
pmid: 1
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
R1p relaxation-dispersion MAS NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '8412'
abstract:
- lang: eng
text: Microsecond to millisecond timescale backbone dynamics of the amyloid core
residues in Y145Stop human prion protein (PrP) fibrils were investigated by using
15N rotating frame (R1ρ) relaxation dispersion solid‐state nuclear magnetic resonance
spectroscopy over a wide range of spin‐lock fields. Numerical simulations enabled
the experimental relaxation dispersion profiles for most of the fibril core residues
to be modelled by using a two‐state exchange process with a common exchange rate
of 1000 s−1, corresponding to protein backbone motion on the timescale of 1 ms,
and an excited‐state population of 2 %. We also found that the relaxation dispersion
profiles for several amino acids positioned near the edges of the most structured
regions of the amyloid core were better modelled by assuming somewhat higher excited‐state
populations (∼5–15 %) and faster exchange rate constants, corresponding to protein
backbone motions on the timescale of ∼100–300 μs. The slow backbone dynamics of
the core residues were evaluated in the context of the structural model of human
Y145Stop PrP amyloid.
article_processing_charge: No
article_type: original
author:
- first_name: Matthew D.
full_name: Shannon, Matthew D.
last_name: Shannon
- first_name: Theint
full_name: Theint, Theint
last_name: Theint
- first_name: Dwaipayan
full_name: Mukhopadhyay, Dwaipayan
last_name: Mukhopadhyay
- first_name: Krystyna
full_name: Surewicz, Krystyna
last_name: Surewicz
- first_name: Witold K.
full_name: Surewicz, Witold K.
last_name: Surewicz
- 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
- first_name: Christopher P.
full_name: Jaroniec, Christopher P.
last_name: Jaroniec
citation:
ama: Shannon MD, Theint T, Mukhopadhyay D, et al. Conformational dynamics in the
core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR.
ChemPhysChem. 2019;20(2):311-317. doi:10.1002/cphc.201800779
apa: Shannon, M. D., Theint, T., Mukhopadhyay, D., Surewicz, K., Surewicz, W. K.,
Marion, D., … Jaroniec, C. P. (2019). Conformational dynamics in the core of human
Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem.
Wiley. https://doi.org/10.1002/cphc.201800779
chicago: Shannon, Matthew D., Theint Theint, Dwaipayan Mukhopadhyay, Krystyna Surewicz,
Witold K. Surewicz, Dominique Marion, Paul Schanda, and Christopher P. Jaroniec.
“Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed
by Relaxation Dispersion NMR.” ChemPhysChem. Wiley, 2019. https://doi.org/10.1002/cphc.201800779.
ieee: M. D. Shannon et al., “Conformational dynamics in the core of human
Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” ChemPhysChem,
vol. 20, no. 2. Wiley, pp. 311–317, 2019.
ista: Shannon MD, Theint T, Mukhopadhyay D, Surewicz K, Surewicz WK, Marion D, Schanda
P, Jaroniec CP. 2019. Conformational dynamics in the core of human Y145Stop prion
protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. 20(2), 311–317.
mla: Shannon, Matthew D., et al. “Conformational Dynamics in the Core of Human Y145Stop
Prion Protein Amyloid Probed by Relaxation Dispersion NMR.” ChemPhysChem,
vol. 20, no. 2, Wiley, 2019, pp. 311–17, doi:10.1002/cphc.201800779.
short: M.D. Shannon, T. Theint, D. Mukhopadhyay, K. Surewicz, W.K. Surewicz, D.
Marion, P. Schanda, C.P. Jaroniec, ChemPhysChem 20 (2019) 311–317.
date_created: 2020-09-17T10:29:43Z
date_published: 2019-01-21T00:00:00Z
date_updated: 2021-01-12T08:19:06Z
day: '21'
doi: 10.1002/cphc.201800779
extern: '1'
external_id:
pmid:
- '30276945'
intvolume: ' 20'
issue: '2'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 311-317
pmid: 1
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Conformational dynamics in the core of human Y145Stop prion protein amyloid
probed by relaxation dispersion NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '8413'
abstract:
- lang: eng
text: NMR relaxation dispersion methods provide a holistic way to observe microsecond
time-scale protein backbone motion both in solution and in the solid state. Different
nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell
and near-rotary-resonance) give complementary information about the amplitudes
and time scales of the conformational dynamics and provide comprehensive insights
into the mechanistic details of the structural rearrangements. In this paper,
we exemplify the benefits of the combination of various solution- and solid-state
relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain),
for which we are able to identify and model the functionally relevant conformational
rearrangements around the ligand recognition loop occurring on multiple microsecond
time scales. The observed loop motions suggest that the SH3 domain exists in a
binding-competent conformation in dynamic equilibrium with a sterically impaired
ground-state conformation both in solution and in crystalline form. This inherent
plasticity between the interconverting macrostates is compatible with a conformational-preselection
model and provides new insights into the recognition mechanisms of SH3 domains.
article_processing_charge: No
article_type: original
author:
- first_name: Petra
full_name: Rovó, Petra
last_name: Rovó
- first_name: Colin A.
full_name: Smith, Colin A.
last_name: Smith
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Bert L.
full_name: de Groot, Bert L.
last_name: de Groot
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Rasmus
full_name: Linser, Rasmus
last_name: Linser
citation:
ama: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights
into microsecond time-scale motion of solid proteins using complementary 15N and
1H relaxation dispersion techniques. Journal of the American Chemical Society.
2019;141(2):858-869. doi:10.1021/jacs.8b09258
apa: Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser,
R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins
using complementary 15N and 1H relaxation dispersion techniques. Journal of
the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258
chicago: Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda,
and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of
Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society. American Chemical Society, 2019.
https://doi.org/10.1021/jacs.8b09258.
ieee: P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser,
“Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques,” Journal of the
American Chemical Society, vol. 141, no. 2. American Chemical Society, pp.
858–869, 2019.
ista: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic
insights into microsecond time-scale motion of solid proteins using complementary
15N and 1H relaxation dispersion techniques. Journal of the American Chemical
Society. 141(2), 858–869.
mla: Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion
of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society, vol. 141, no. 2, American Chemical
Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.
short: P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal
of the American Chemical Society 141 (2019) 858–869.
date_created: 2020-09-17T10:29:50Z
date_published: 2019-01-08T00:00:00Z
date_updated: 2021-01-12T08:19:07Z
day: '08'
doi: 10.1021/jacs.8b09258
extern: '1'
external_id:
pmid:
- '30620186'
intvolume: ' 141'
issue: '2'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 858-869
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '8415'
abstract:
- lang: eng
text: 'We consider billiards obtained by removing three strictly convex obstacles
satisfying the non-eclipse condition on the plane. The restriction of the dynamics
to the set of non-escaping orbits is conjugated to a subshift on three symbols
that provides a natural labeling of all periodic orbits. We study the following
inverse problem: does the Marked Length Spectrum (i.e., the set of lengths of
periodic orbits together with their labeling), determine the geometry of the billiard
table? We show that from the Marked Length Spectrum it is possible to recover
the curvature at periodic points of period two, as well as the Lyapunov exponent
of each periodic orbit.'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Péter
full_name: Bálint, Péter
last_name: Bálint
- 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: Martin
full_name: Leguil, Martin
last_name: Leguil
citation:
ama: Bálint P, De Simoi J, Kaloshin V, Leguil M. Marked length spectrum, homoclinic
orbits and the geometry of open dispersing billiards. Communications in Mathematical
Physics. 2019;374(3):1531-1575. doi:10.1007/s00220-019-03448-x
apa: Bálint, P., De Simoi, J., Kaloshin, V., & Leguil, M. (2019). Marked length
spectrum, homoclinic orbits and the geometry of open dispersing billiards. Communications
in Mathematical Physics. Springer Nature. https://doi.org/10.1007/s00220-019-03448-x
chicago: Bálint, Péter, Jacopo De Simoi, Vadim Kaloshin, and Martin Leguil. “Marked
Length Spectrum, Homoclinic Orbits and the Geometry of Open Dispersing Billiards.”
Communications in Mathematical Physics. Springer Nature, 2019. https://doi.org/10.1007/s00220-019-03448-x.
ieee: P. Bálint, J. De Simoi, V. Kaloshin, and M. Leguil, “Marked length spectrum,
homoclinic orbits and the geometry of open dispersing billiards,” Communications
in Mathematical Physics, vol. 374, no. 3. Springer Nature, pp. 1531–1575,
2019.
ista: Bálint P, De Simoi J, Kaloshin V, Leguil M. 2019. Marked length spectrum,
homoclinic orbits and the geometry of open dispersing billiards. Communications
in Mathematical Physics. 374(3), 1531–1575.
mla: Bálint, Péter, et al. “Marked Length Spectrum, Homoclinic Orbits and the Geometry
of Open Dispersing Billiards.” Communications in Mathematical Physics,
vol. 374, no. 3, Springer Nature, 2019, pp. 1531–75, doi:10.1007/s00220-019-03448-x.
short: P. Bálint, J. De Simoi, V. Kaloshin, M. Leguil, Communications in Mathematical
Physics 374 (2019) 1531–1575.
date_created: 2020-09-17T10:41:27Z
date_published: 2019-05-09T00:00:00Z
date_updated: 2021-01-12T08:19:08Z
day: '09'
doi: 10.1007/s00220-019-03448-x
extern: '1'
external_id:
arxiv:
- '1809.08947'
intvolume: ' 374'
issue: '3'
keyword:
- Mathematical Physics
- Statistical and Nonlinear Physics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1809.08947
month: '05'
oa: 1
oa_version: Preprint
page: 1531-1575
publication: Communications in Mathematical Physics
publication_identifier:
issn:
- 0010-3616
- 1432-0916
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Marked length spectrum, homoclinic orbits and the geometry of open dispersing
billiards
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 374
year: '2019'
...
---
_id: '8416'
abstract:
- lang: eng
text: In this paper, we show that any smooth one-parameter deformations of a strictly
convex integrable billiard table Ω0 preserving the integrability near the boundary
have to be tangent to a finite dimensional space passing through Ω0.
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
citation:
ama: Huang G, Kaloshin V. On the finite dimensionality of integrable deformations
of strictly convex integrable billiard tables. Moscow Mathematical Journal.
2019;19(2):307-327. doi:10.17323/1609-4514-2019-19-2-307-327
apa: Huang, G., & Kaloshin, V. (2019). On the finite dimensionality of integrable
deformations of strictly convex integrable billiard tables. Moscow Mathematical
Journal. American Mathematical Society. https://doi.org/10.17323/1609-4514-2019-19-2-307-327
chicago: Huang, Guan, and Vadim Kaloshin. “On the Finite Dimensionality of Integrable
Deformations of Strictly Convex Integrable Billiard Tables.” Moscow Mathematical
Journal. American Mathematical Society, 2019. https://doi.org/10.17323/1609-4514-2019-19-2-307-327.
ieee: G. Huang and V. Kaloshin, “On the finite dimensionality of integrable deformations
of strictly convex integrable billiard tables,” Moscow Mathematical Journal,
vol. 19, no. 2. American Mathematical Society, pp. 307–327, 2019.
ista: Huang G, Kaloshin V. 2019. On the finite dimensionality of integrable deformations
of strictly convex integrable billiard tables. Moscow Mathematical Journal. 19(2),
307–327.
mla: Huang, Guan, and Vadim Kaloshin. “On the Finite Dimensionality of Integrable
Deformations of Strictly Convex Integrable Billiard Tables.” Moscow Mathematical
Journal, vol. 19, no. 2, American Mathematical Society, 2019, pp. 307–27,
doi:10.17323/1609-4514-2019-19-2-307-327.
short: G. Huang, V. Kaloshin, Moscow Mathematical Journal 19 (2019) 307–327.
date_created: 2020-09-17T10:41:36Z
date_published: 2019-04-01T00:00:00Z
date_updated: 2021-01-12T08:19:08Z
day: '01'
doi: 10.17323/1609-4514-2019-19-2-307-327
extern: '1'
external_id:
arxiv:
- '1809.09341'
intvolume: ' 19'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1809.09341
month: '04'
oa: 1
oa_version: Preprint
page: 307-327
publication: Moscow Mathematical Journal
publication_identifier:
issn:
- 1609-4514
publication_status: published
publisher: American Mathematical Society
quality_controlled: '1'
status: public
title: On the finite dimensionality of integrable deformations of strictly convex
integrable billiard tables
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2019'
...
---
_id: '8418'
abstract:
- lang: eng
text: For the Restricted Circular Planar 3 Body Problem, we show that there exists
an open set U in phase space of fixed measure, where the set of initial points
which lead to collision is O(μ120) dense as μ→0.
article_processing_charge: No
article_type: original
author:
- first_name: Marcel
full_name: Guardia, Marcel
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: Jianlu
full_name: Zhang, Jianlu
last_name: Zhang
citation:
ama: Guardia M, Kaloshin V, Zhang J. Asymptotic density of collision orbits in the
Restricted Circular Planar 3 Body Problem. Archive for Rational Mechanics and
Analysis. 2019;233(2):799-836. doi:10.1007/s00205-019-01368-7
apa: Guardia, M., Kaloshin, V., & Zhang, J. (2019). Asymptotic density of collision
orbits in the Restricted Circular Planar 3 Body Problem. Archive for Rational
Mechanics and Analysis. Springer Nature. https://doi.org/10.1007/s00205-019-01368-7
chicago: Guardia, Marcel, Vadim Kaloshin, and Jianlu Zhang. “Asymptotic Density
of Collision Orbits in the Restricted Circular Planar 3 Body Problem.” Archive
for Rational Mechanics and Analysis. Springer Nature, 2019. https://doi.org/10.1007/s00205-019-01368-7.
ieee: M. Guardia, V. Kaloshin, and J. Zhang, “Asymptotic density of collision orbits
in the Restricted Circular Planar 3 Body Problem,” Archive for Rational Mechanics
and Analysis, vol. 233, no. 2. Springer Nature, pp. 799–836, 2019.
ista: Guardia M, Kaloshin V, Zhang J. 2019. Asymptotic density of collision orbits
in the Restricted Circular Planar 3 Body Problem. Archive for Rational Mechanics
and Analysis. 233(2), 799–836.
mla: Guardia, Marcel, et al. “Asymptotic Density of Collision Orbits in the Restricted
Circular Planar 3 Body Problem.” Archive for Rational Mechanics and Analysis,
vol. 233, no. 2, Springer Nature, 2019, pp. 799–836, doi:10.1007/s00205-019-01368-7.
short: M. Guardia, V. Kaloshin, J. Zhang, Archive for Rational Mechanics and Analysis
233 (2019) 799–836.
date_created: 2020-09-17T10:41:51Z
date_published: 2019-03-12T00:00:00Z
date_updated: 2021-01-12T08:19:09Z
day: '12'
doi: 10.1007/s00205-019-01368-7
extern: '1'
intvolume: ' 233'
issue: '2'
keyword:
- Mechanical Engineering
- Mathematics (miscellaneous)
- Analysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1007/s00205-019-01368-7
month: '03'
oa: 1
oa_version: Published Version
page: 799-836
publication: Archive for Rational Mechanics and Analysis
publication_identifier:
issn:
- 0003-9527
- 1432-0673
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Asymptotic density of collision orbits in the Restricted Circular Planar 3
Body Problem
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 233
year: '2019'
...
---
_id: '8693'
abstract:
- lang: eng
text: We review V. I. Arnold’s 1963 celebrated paper [1] Proof of A. N. Kolmogorov’s
Theorem on the Conservation of Conditionally Periodic Motions with a Small Variation
in the Hamiltonian, and prove that, optimising Arnold’s scheme, one can get “sharp”
asymptotic quantitative conditions (as ε → 0, ε being the strength of the perturbation).
All constants involved are explicitly computed.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Luigi
full_name: Chierchia, Luigi
last_name: Chierchia
- first_name: Edmond
full_name: Koudjinan, Edmond
id: 52DF3E68-AEFA-11EA-95A4-124A3DDC885E
last_name: Koudjinan
orcid: 0000-0003-2640-4049
citation:
ama: Chierchia L, Koudjinan E. V. I. Arnold’s “pointwise” KAM theorem. Regular
and Chaotic Dynamics. 2019;24:583–606. doi:10.1134/S1560354719060017
apa: Chierchia, L., & Koudjinan, E. (2019). V. I. Arnold’s “pointwise” KAM theorem.
Regular and Chaotic Dynamics. Springer. https://doi.org/10.1134/S1560354719060017
chicago: Chierchia, Luigi, and Edmond Koudjinan. “V. I. Arnold’s ‘Pointwise’ KAM
Theorem.” Regular and Chaotic Dynamics. Springer, 2019. https://doi.org/10.1134/S1560354719060017.
ieee: L. Chierchia and E. Koudjinan, “V. I. Arnold’s ‘pointwise’ KAM theorem,” Regular
and Chaotic Dynamics, vol. 24. Springer, pp. 583–606, 2019.
ista: Chierchia L, Koudjinan E. 2019. V. I. Arnold’s “pointwise” KAM theorem. Regular
and Chaotic Dynamics. 24, 583–606.
mla: Chierchia, Luigi, and Edmond Koudjinan. “V. I. Arnold’s ‘Pointwise’ KAM Theorem.”
Regular and Chaotic Dynamics, vol. 24, Springer, 2019, pp. 583–606, doi:10.1134/S1560354719060017.
short: L. Chierchia, E. Koudjinan, Regular and Chaotic Dynamics 24 (2019) 583–606.
date_created: 2020-10-21T15:25:45Z
date_published: 2019-12-10T00:00:00Z
date_updated: 2021-01-12T08:20:34Z
day: '10'
doi: 10.1134/S1560354719060017
extern: '1'
external_id:
arxiv:
- '1908.02523'
intvolume: ' 24'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1908.02523
month: '12'
oa: 1
oa_version: Preprint
page: 583–606
publication: Regular and Chaotic Dynamics
publication_status: published
publisher: Springer
quality_controlled: '1'
status: public
title: V. I. Arnold’s “pointwise” KAM theorem
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2019'
...
---
_id: '9016'
abstract:
- lang: eng
text: Inhibiting the histone H3–ASF1 (anti‐silencing function 1) protein–protein
interaction (PPI) represents a potential approach for treating numerous cancers.
As an α‐helix‐mediated PPI, constraining the key histone H3 helix (residues 118–135)
is a strategy through which chemical probes might be elaborated to test this hypothesis.
In this work, variant H3118–135 peptides bearing pentenylglycine residues at the
i and i+4 positions were constrained by olefin metathesis. Biophysical analyses
revealed that promotion of a bioactive helical conformation depends on the position
at which the constraint is introduced, but that the potency of binding towards
ASF1 is unaffected by the constraint and instead that enthalpy–entropy compensation
occurs.
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: Silvia
full_name: Rodriguez‐Marin, Silvia
last_name: Rodriguez‐Marin
- first_name: Zsófia
full_name: Hegedüs, Zsófia
last_name: Hegedüs
- first_name: Marie E.
full_name: Perrin, Marie E.
last_name: Perrin
- first_name: Françoise
full_name: Ochsenbein, Françoise
last_name: Ochsenbein
- first_name: Andrew J.
full_name: Wilson, Andrew J.
last_name: Wilson
citation:
ama: Bakail MM, Rodriguez‐Marin S, Hegedüs Z, Perrin ME, Ochsenbein F, Wilson AJ.
Recognition of ASF1 by using hydrocarbon‐constrained peptides. ChemBioChem.
2019;20(7):891-895. doi:10.1002/cbic.201800633
apa: Bakail, M. M., Rodriguez‐Marin, S., Hegedüs, Z., Perrin, M. E., Ochsenbein,
F., & Wilson, A. J. (2019). Recognition of ASF1 by using hydrocarbon‐constrained
peptides. ChemBioChem. Wiley. https://doi.org/10.1002/cbic.201800633
chicago: Bakail, May M, Silvia Rodriguez‐Marin, Zsófia Hegedüs, Marie E. Perrin,
Françoise Ochsenbein, and Andrew J. Wilson. “Recognition of ASF1 by Using Hydrocarbon‐constrained
Peptides.” ChemBioChem. Wiley, 2019. https://doi.org/10.1002/cbic.201800633.
ieee: M. M. Bakail, S. Rodriguez‐Marin, Z. Hegedüs, M. E. Perrin, F. Ochsenbein,
and A. J. Wilson, “Recognition of ASF1 by using hydrocarbon‐constrained peptides,”
ChemBioChem, vol. 20, no. 7. Wiley, pp. 891–895, 2019.
ista: Bakail MM, Rodriguez‐Marin S, Hegedüs Z, Perrin ME, Ochsenbein F, Wilson AJ.
2019. Recognition of ASF1 by using hydrocarbon‐constrained peptides. ChemBioChem.
20(7), 891–895.
mla: Bakail, May M., et al. “Recognition of ASF1 by Using Hydrocarbon‐constrained
Peptides.” ChemBioChem, vol. 20, no. 7, Wiley, 2019, pp. 891–95, doi:10.1002/cbic.201800633.
short: M.M. Bakail, S. Rodriguez‐Marin, Z. Hegedüs, M.E. Perrin, F. Ochsenbein,
A.J. Wilson, ChemBioChem 20 (2019) 891–895.
date_created: 2021-01-19T10:59:14Z
date_published: 2019-04-01T00:00:00Z
date_updated: 2023-02-23T13:46:48Z
day: '01'
doi: 10.1002/cbic.201800633
extern: '1'
intvolume: ' 20'
issue: '7'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.1002/cbic.201800633'
month: '04'
oa: 1
oa_version: Published Version
page: 891-895
publication: ChemBioChem
publication_identifier:
issn:
- 1439-4227
- 1439-7633
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Recognition of ASF1 by using hydrocarbon‐constrained peptides
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '9018'
abstract:
- lang: eng
text: Anti-silencing function 1 (ASF1) is a conserved H3-H4 histone chaperone involved
in histone dynamics during replication, transcription, and DNA repair. Overexpressed
in proliferating tissues including many tumors, ASF1 has emerged as a promising
therapeutic target. Here, we combine structural, computational, and biochemical
approaches to design peptides that inhibit the ASF1-histone interaction. Starting
from the structure of the human ASF1-histone complex, we developed a rational
design strategy combining epitope tethering and optimization of interface contacts
to identify a potent peptide inhibitor with a dissociation constant of 3 nM. When
introduced into cultured cells, the inhibitors impair cell proliferation, perturb
cell-cycle progression, and reduce cell migration and invasion in a manner commensurate
with their affinity for ASF1. Finally, we find that direct injection of the most
potent ASF1 peptide inhibitor in mouse allografts reduces tumor growth. Our results
open new avenues to use ASF1 inhibitors as promising leads for cancer therapy.
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: Albane
full_name: Gaubert, Albane
last_name: Gaubert
- first_name: Jessica
full_name: Andreani, Jessica
last_name: Andreani
- first_name: Gwenaëlle
full_name: Moal, Gwenaëlle
last_name: Moal
- first_name: Guillaume
full_name: Pinna, Guillaume
last_name: Pinna
- first_name: Ekaterina
full_name: Boyarchuk, Ekaterina
last_name: Boyarchuk
- first_name: Marie-Cécile
full_name: Gaillard, Marie-Cécile
last_name: Gaillard
- first_name: Regis
full_name: Courbeyrette, Regis
last_name: Courbeyrette
- first_name: Carl
full_name: Mann, Carl
last_name: Mann
- first_name: Jean-Yves
full_name: Thuret, Jean-Yves
last_name: Thuret
- first_name: Bérengère
full_name: Guichard, Bérengère
last_name: Guichard
- first_name: Brice
full_name: Murciano, Brice
last_name: Murciano
- first_name: Nicolas
full_name: Richet, Nicolas
last_name: Richet
- first_name: Adeline
full_name: Poitou, Adeline
last_name: Poitou
- first_name: Claire
full_name: Frederic, Claire
last_name: Frederic
- first_name: Marie-Hélène
full_name: Le Du, Marie-Hélène
last_name: Le Du
- first_name: Morgane
full_name: Agez, Morgane
last_name: Agez
- first_name: Caroline
full_name: Roelants, Caroline
last_name: Roelants
- first_name: Zachary A.
full_name: Gurard-Levin, Zachary A.
last_name: Gurard-Levin
- first_name: Geneviève
full_name: Almouzni, Geneviève
last_name: Almouzni
- first_name: Nadia
full_name: Cherradi, Nadia
last_name: Cherradi
- first_name: Raphael
full_name: Guerois, Raphael
last_name: Guerois
- first_name: Françoise
full_name: Ochsenbein, Françoise
last_name: Ochsenbein
citation:
ama: Bakail MM, Gaubert A, Andreani J, et al. Design on a rational basis of high-affinity
peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology.
2019;26(11):1573-1585.e10. doi:10.1016/j.chembiol.2019.09.002
apa: Bakail, M. M., Gaubert, A., Andreani, J., Moal, G., Pinna, G., Boyarchuk, E.,
… Ochsenbein, F. (2019). Design on a rational basis of high-affinity peptides
inhibiting the histone chaperone ASF1. Cell Chemical Biology. Elsevier.
https://doi.org/10.1016/j.chembiol.2019.09.002
chicago: Bakail, May M, Albane Gaubert, Jessica Andreani, Gwenaëlle Moal, Guillaume
Pinna, Ekaterina Boyarchuk, Marie-Cécile Gaillard, et al. “Design on a Rational
Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” Cell
Chemical Biology. Elsevier, 2019. https://doi.org/10.1016/j.chembiol.2019.09.002.
ieee: M. M. Bakail et al., “Design on a rational basis of high-affinity peptides
inhibiting the histone chaperone ASF1,” Cell Chemical Biology, vol. 26,
no. 11. Elsevier, p. 1573–1585.e10, 2019.
ista: Bakail MM, Gaubert A, Andreani J, Moal G, Pinna G, Boyarchuk E, Gaillard M-C,
Courbeyrette R, Mann C, Thuret J-Y, Guichard B, Murciano B, Richet N, Poitou A,
Frederic C, Le Du M-H, Agez M, Roelants C, Gurard-Levin ZA, Almouzni G, Cherradi
N, Guerois R, Ochsenbein F. 2019. Design on a rational basis of high-affinity
peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 26(11),
1573–1585.e10.
mla: Bakail, May M., et al. “Design on a Rational Basis of High-Affinity Peptides
Inhibiting the Histone Chaperone ASF1.” Cell Chemical Biology, vol. 26,
no. 11, Elsevier, 2019, p. 1573–1585.e10, doi:10.1016/j.chembiol.2019.09.002.
short: M.M. Bakail, A. Gaubert, J. Andreani, G. Moal, G. Pinna, E. Boyarchuk, M.-C.
Gaillard, R. Courbeyrette, C. Mann, J.-Y. Thuret, B. Guichard, B. Murciano, N.
Richet, A. Poitou, C. Frederic, M.-H. Le Du, M. Agez, C. Roelants, Z.A. Gurard-Levin,
G. Almouzni, N. Cherradi, R. Guerois, F. Ochsenbein, Cell Chemical Biology 26
(2019) 1573–1585.e10.
date_created: 2021-01-19T11:04:50Z
date_published: 2019-11-21T00:00:00Z
date_updated: 2023-02-23T13:46:53Z
day: '21'
doi: 10.1016/j.chembiol.2019.09.002
extern: '1'
external_id:
pmid:
- '31543461'
intvolume: ' 26'
issue: '11'
keyword:
- Clinical Biochemistry
- Molecular Medicine
- Biochemistry
- Molecular Biology
- Pharmacology
- Drug Discovery
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.chembiol.2019.09.002
month: '11'
oa: 1
oa_version: Published Version
page: 1573-1585.e10
pmid: 1
publication: Cell Chemical Biology
publication_identifier:
issn:
- 2451-9456
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Design on a rational basis of high-affinity peptides inhibiting the histone
chaperone ASF1
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 26
year: '2019'
...
---
_id: '9060'
abstract:
- lang: eng
text: Molecular motors are essential to the living, generating fluctuations that
boost transport and assist assembly. Active colloids, that consume energy to move,
hold similar potential for man-made materials controlled by forces generated from
within. Yet, their use as a powerhouse in materials science lacks. Here we show
a massive acceleration of the annealing of a monolayer of passive beads by moderate
addition of self-propelled microparticles. We rationalize our observations with
a model of collisions that drive active fluctuations and activate the annealing.
The experiment is quantitatively compared with Brownian dynamic simulations that
further unveil a dynamical transition in the mechanism of annealing. Active dopants
travel uniformly in the system or co-localize at the grain boundaries as a result
of the persistence of their motion. Our findings uncover the potential of internal
activity to control materials and lay the groundwork for the rise of materials
science beyond equilibrium.
article_number: '3380'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Sophie
full_name: Ramananarivo, Sophie
last_name: Ramananarivo
- first_name: Etienne
full_name: Ducrot, Etienne
last_name: Ducrot
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal
monolayers. Nature Communications. 2019;10(1). doi:10.1038/s41467-019-11362-y
apa: Ramananarivo, S., Ducrot, E., & Palacci, J. A. (2019). Activity-controlled
annealing of colloidal monolayers. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-019-11362-y
chicago: Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled
Annealing of Colloidal Monolayers.” Nature Communications. Springer Nature,
2019. https://doi.org/10.1038/s41467-019-11362-y.
ieee: S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing
of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer
Nature, 2019.
ista: Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing
of colloidal monolayers. Nature Communications. 10(1), 3380.
mla: Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.”
Nature Communications, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:10.1038/s41467-019-11362-y.
short: S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).
date_created: 2021-02-02T13:43:36Z
date_published: 2019-07-29T00:00:00Z
date_updated: 2023-02-23T13:47:59Z
day: '29'
ddc:
- '530'
doi: 10.1038/s41467-019-11362-y
extern: '1'
external_id:
arxiv:
- '1909.07382'
pmid:
- '31358762'
file:
- access_level: open_access
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creator: cziletti
date_created: 2021-02-02T13:47:21Z
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file_name: 2019_NatureComm_Ramananarivo.pdf
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intvolume: ' 10'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Activity-controlled annealing of colloidal monolayers
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: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 10
year: '2019'
...
---
_id: '9261'
abstract:
- lang: eng
text: 'Bending-active structures are able to efficiently produce complex curved
shapes starting from flat panels. The desired deformation of the panels derives
from the proper selection of their elastic properties. Optimized panels, called
FlexMaps, are designed such that, once they are bent and assembled, the resulting
static equilibrium configuration matches a desired input 3D shape. The FlexMaps
elastic properties are controlled by locally varying spiraling geometric mesostructures,
which are optimized in size and shape to match the global curvature (i.e., bending
requests) of the target shape. The design pipeline starts from a quad mesh representing
the input 3D shape, which defines the edge size and the total amount of spirals:
every quad will embed one spiral. Then, an optimization algorithm tunes the geometry
of the spirals by using a simplified pre-computed rod model. This rod model is
derived from a non-linear regression algorithm which approximates the non-linear
behavior of solid FEM spiral models subject to hundreds of load combinations.
This innovative pipeline has been applied to the project of a lightweight plywood
pavilion named FlexMaps Pavilion, which is a single-layer piecewise twisted arc
that fits a bounding box of 3.90x3.96x3.25 meters.'
article_processing_charge: No
author:
- first_name: Francesco
full_name: Laccone, Francesco
last_name: Laccone
- first_name: Luigi
full_name: Malomo, Luigi
last_name: Malomo
- first_name: Jesus
full_name: Perez Rodriguez, Jesus
id: 2DC83906-F248-11E8-B48F-1D18A9856A87
last_name: Perez Rodriguez
- first_name: Nico
full_name: Pietroni, Nico
last_name: Pietroni
- first_name: Federico
full_name: Ponchio, Federico
last_name: Ponchio
- first_name: Bernd
full_name: Bickel, Bernd
id: 49876194-F248-11E8-B48F-1D18A9856A87
last_name: Bickel
orcid: 0000-0001-6511-9385
- first_name: Paolo
full_name: Cignoni, Paolo
last_name: Cignoni
citation:
ama: 'Laccone F, Malomo L, Perez Rodriguez J, et al. FlexMaps Pavilion: A twisted
arc made of mesostructured flat flexible panels. In: IASS Symposium 2019 -
60th Anniversary Symposium of the International Association for Shell and Spatial
Structures; Structural Membranes 2019 - 9th International Conference on Textile
Composites and Inflatable Structures, FORM and FORCE. International Center
for Numerical Methods in Engineering; 2019:509-515.'
apa: 'Laccone, F., Malomo, L., Perez Rodriguez, J., Pietroni, N., Ponchio, F., Bickel,
B., & Cignoni, P. (2019). FlexMaps Pavilion: A twisted arc made of mesostructured
flat flexible panels. In IASS Symposium 2019 - 60th Anniversary Symposium of
the International Association for Shell and Spatial Structures; Structural Membranes
2019 - 9th International Conference on Textile Composites and Inflatable Structures,
FORM and FORCE (pp. 509–515). Barcelona, Spain: International Center for Numerical
Methods in Engineering.'
chicago: 'Laccone, Francesco, Luigi Malomo, Jesus Perez Rodriguez, Nico Pietroni,
Federico Ponchio, Bernd Bickel, and Paolo Cignoni. “FlexMaps Pavilion: A Twisted
Arc Made of Mesostructured Flat Flexible Panels.” In IASS Symposium 2019 -
60th Anniversary Symposium of the International Association for Shell and Spatial
Structures; Structural Membranes 2019 - 9th International Conference on Textile
Composites and Inflatable Structures, FORM and FORCE, 509–15. International
Center for Numerical Methods in Engineering, 2019.'
ieee: 'F. Laccone et al., “FlexMaps Pavilion: A twisted arc made of mesostructured
flat flexible panels,” in IASS Symposium 2019 - 60th Anniversary Symposium
of the International Association for Shell and Spatial Structures; Structural
Membranes 2019 - 9th International Conference on Textile Composites and Inflatable
Structures, FORM and FORCE, Barcelona, Spain, 2019, pp. 509–515.'
ista: 'Laccone F, Malomo L, Perez Rodriguez J, Pietroni N, Ponchio F, Bickel B,
Cignoni P. 2019. FlexMaps Pavilion: A twisted arc made of mesostructured flat
flexible panels. IASS Symposium 2019 - 60th Anniversary Symposium of the International
Association for Shell and Spatial Structures; Structural Membranes 2019 - 9th
International Conference on Textile Composites and Inflatable Structures, FORM
and FORCE. IASS: International Association for Shell and Spatial Structures, 509–515.'
mla: 'Laccone, Francesco, et al. “FlexMaps Pavilion: A Twisted Arc Made of Mesostructured
Flat Flexible Panels.” IASS Symposium 2019 - 60th Anniversary Symposium of
the International Association for Shell and Spatial Structures; Structural Membranes
2019 - 9th International Conference on Textile Composites and Inflatable Structures,
FORM and FORCE, International Center for Numerical Methods in Engineering,
2019, pp. 509–15.'
short: F. Laccone, L. Malomo, J. Perez Rodriguez, N. Pietroni, F. Ponchio, B. Bickel,
P. Cignoni, in:, IASS Symposium 2019 - 60th Anniversary Symposium of the International
Association for Shell and Spatial Structures; Structural Membranes 2019 - 9th
International Conference on Textile Composites and Inflatable Structures, FORM
and FORCE, International Center for Numerical Methods in Engineering, 2019, pp.
509–515.
conference:
end_date: 2019-10-10
location: Barcelona, Spain
name: 'IASS: International Association for Shell and Spatial Structures'
start_date: 2019-10-07
date_created: 2021-03-21T23:01:21Z
date_published: 2019-10-10T00:00:00Z
date_updated: 2023-09-08T11:21:54Z
day: '10'
department:
- _id: BeBi
external_id:
isi:
- '000563497600059'
isi: 1
language:
- iso: eng
month: '10'
oa_version: None
page: 509-515
publication: IASS Symposium 2019 - 60th Anniversary Symposium of the International
Association for Shell and Spatial Structures; Structural Membranes 2019 - 9th International
Conference on Textile Composites and Inflatable Structures, FORM and FORCE
publication_identifier:
isbn:
- '9788412110104'
issn:
- 2518-6582
publication_status: published
publisher: International Center for Numerical Methods in Engineering
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'FlexMaps Pavilion: A twisted arc made of mesostructured flat flexible panels'
type: conference
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2019'
...