---
_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.'
apa: 'Avarikioti, G., Kokoris Kogias, E., Wattenhofer, R., & Zindros, D. (n.d.).
Brick: Asynchronous payment channels. arXiv.'
chicago: 'Avarikioti, Georgia, Eleftherios Kokoris Kogias, Roger Wattenhofer, and
Dionysis Zindros. “Brick: Asynchronous Payment Channels.” ArXiv, n.d.'
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.'
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: 2021-01-12T08:18:04Z
day: '27'
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.'
apa: 'Avarikioti, G., Kokoris Kogias, E., & Wattenhofer, R. (n.d.). Divide and
scale: Formalization of distributed ledger sharding protocols. arXiv.'
chicago: 'Avarikioti, Georgia, Eleftherios Kokoris Kogias, and Roger Wattenhofer.
“Divide and Scale: Formalization of Distributed Ledger Sharding Protocols.” ArXiv,
n.d.'
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.'
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: 2021-01-12T08:18:05Z
day: '23'
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: '8570'
abstract:
- lang: eng
text: 'This report presents the results of a friendly competition for formal verification
of continuous and hybrid systems with linear continuous dynamics. The friendly
competition took place as part of the workshop Applied Verification for Continuous
and Hybrid Systems (ARCH) in 2019. In its third edition, seven tools have been
applied to solve six different benchmark problems in the category for linear continuous
dynamics (in alphabetical order): CORA, CORA/SX, HyDRA, Hylaa, JuliaReach, SpaceEx,
and XSpeed. This report is a snapshot of the current landscape of tools and the
types of benchmarks they are particularly suited for. Due to the diversity of
problems, we are not ranking tools, yet the presented results provide one of the
most complete assessments of tools for the safety verification of continuous and
hybrid systems with linear continuous dynamics up to this date.'
article_processing_charge: No
author:
- first_name: Matthias
full_name: Althoff, Matthias
last_name: Althoff
- first_name: Stanley
full_name: Bak, Stanley
last_name: Bak
- first_name: Marcelo
full_name: Forets, Marcelo
last_name: Forets
- first_name: Goran
full_name: Frehse, Goran
last_name: Frehse
- first_name: Niklas
full_name: Kochdumper, Niklas
last_name: Kochdumper
- first_name: Rajarshi
full_name: Ray, Rajarshi
last_name: Ray
- first_name: Christian
full_name: Schilling, Christian
id: 3A2F4DCE-F248-11E8-B48F-1D18A9856A87
last_name: Schilling
orcid: 0000-0003-3658-1065
- first_name: Stefan
full_name: Schupp, Stefan
last_name: Schupp
citation:
ama: 'Althoff M, Bak S, Forets M, et al. ARCH-COMP19 Category Report: Continuous
and hybrid systems with linear continuous dynamics. In: EPiC Series in Computing.
Vol 61. EasyChair; 2019:14-40. doi:10.29007/bj1w'
apa: 'Althoff, M., Bak, S., Forets, M., Frehse, G., Kochdumper, N., Ray, R., … Schupp,
S. (2019). ARCH-COMP19 Category Report: Continuous and hybrid systems with linear
continuous dynamics. In EPiC Series in Computing (Vol. 61, pp. 14–40).
Montreal, Canada: EasyChair. https://doi.org/10.29007/bj1w'
chicago: 'Althoff, Matthias, Stanley Bak, Marcelo Forets, Goran Frehse, Niklas Kochdumper,
Rajarshi Ray, Christian Schilling, and Stefan Schupp. “ARCH-COMP19 Category Report:
Continuous and Hybrid Systems with Linear Continuous Dynamics.” In EPiC Series
in Computing, 61:14–40. EasyChair, 2019. https://doi.org/10.29007/bj1w.'
ieee: 'M. Althoff et al., “ARCH-COMP19 Category Report: Continuous and hybrid
systems with linear continuous dynamics,” in EPiC Series in Computing,
Montreal, Canada, 2019, vol. 61, pp. 14–40.'
ista: 'Althoff M, Bak S, Forets M, Frehse G, Kochdumper N, Ray R, Schilling C, Schupp
S. 2019. ARCH-COMP19 Category Report: Continuous and hybrid systems with linear
continuous dynamics. EPiC Series in Computing. ARCH: International Workshop on
Applied Verification on Continuous and Hybrid Systems vol. 61, 14–40.'
mla: 'Althoff, Matthias, et al. “ARCH-COMP19 Category Report: Continuous and Hybrid
Systems with Linear Continuous Dynamics.” EPiC Series in Computing, vol.
61, EasyChair, 2019, pp. 14–40, doi:10.29007/bj1w.'
short: M. Althoff, S. Bak, M. Forets, G. Frehse, N. Kochdumper, R. Ray, C. Schilling,
S. Schupp, in:, EPiC Series in Computing, EasyChair, 2019, pp. 14–40.
conference:
end_date: 2019-04-15
location: Montreal, Canada
name: 'ARCH: International Workshop on Applied Verification on Continuous and Hybrid
Systems'
start_date: 2019-04-15
date_created: 2020-09-26T14:23:54Z
date_published: 2019-05-25T00:00:00Z
date_updated: 2021-01-12T08:20:05Z
day: '25'
department:
- _id: ToHe
doi: 10.29007/bj1w
intvolume: ' 61'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://easychair.org/publications/open/1gbP
month: '05'
oa: 1
oa_version: Published Version
page: 14-40
publication: EPiC Series in Computing
publication_identifier:
eissn:
- '23987340'
publication_status: published
publisher: EasyChair
quality_controlled: '1'
status: public
title: 'ARCH-COMP19 Category Report: Continuous and hybrid systems with linear continuous
dynamics'
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 61
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: '170'
abstract:
- lang: eng
text: Upper and lower bounds, of the expected order of magnitude, are obtained for
the number of rational points of bounded height on any quartic del Pezzo surface
over ℚ that contains a conic defined over ℚ .
arxiv: 1
author:
- first_name: Timothy D
full_name: Browning, Timothy D
id: 35827D50-F248-11E8-B48F-1D18A9856A87
last_name: Browning
orcid: 0000-0002-8314-0177
- first_name: Efthymios
full_name: Sofos, Efthymios
last_name: Sofos
citation:
ama: Browning TD, Sofos E. Counting rational points on quartic del Pezzo surfaces
with a rational conic. Mathematische Annalen. 2019;373(3-4):977-1016. doi:10.1007/s00208-018-1716-6
apa: Browning, T. D., & Sofos, E. (2019). Counting rational points on quartic
del Pezzo surfaces with a rational conic. Mathematische Annalen. Springer
Nature. https://doi.org/10.1007/s00208-018-1716-6
chicago: Browning, Timothy D, and Efthymios Sofos. “Counting Rational Points on
Quartic Del Pezzo Surfaces with a Rational Conic.” Mathematische Annalen.
Springer Nature, 2019. https://doi.org/10.1007/s00208-018-1716-6.
ieee: T. D. Browning and E. Sofos, “Counting rational points on quartic del Pezzo
surfaces with a rational conic,” Mathematische Annalen, vol. 373, no. 3–4.
Springer Nature, pp. 977–1016, 2019.
ista: Browning TD, Sofos E. 2019. Counting rational points on quartic del Pezzo
surfaces with a rational conic. Mathematische Annalen. 373(3–4), 977–1016.
mla: Browning, Timothy D., and Efthymios Sofos. “Counting Rational Points on Quartic
Del Pezzo Surfaces with a Rational Conic.” Mathematische Annalen, vol.
373, no. 3–4, Springer Nature, 2019, pp. 977–1016, doi:10.1007/s00208-018-1716-6.
short: T.D. Browning, E. Sofos, Mathematische Annalen 373 (2019) 977–1016.
date_created: 2018-12-11T11:44:59Z
date_published: 2019-04-01T00:00:00Z
date_updated: 2021-01-12T06:52:37Z
day: '01'
ddc:
- '510'
doi: 10.1007/s00208-018-1716-6
extern: '1'
external_id:
arxiv:
- '1609.09057'
file:
- access_level: open_access
checksum: 4061dc2fe99bee25d9adf2d2018cf608
content_type: application/pdf
creator: dernst
date_created: 2019-05-23T07:53:27Z
date_updated: 2020-07-14T12:45:12Z
file_id: '6479'
file_name: 2019_MathAnnalen_Browning.pdf
file_size: 712847
relation: main_file
file_date_updated: 2020-07-14T12:45:12Z
has_accepted_license: '1'
intvolume: ' 373'
issue: 3-4
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 977-1016
publication: Mathematische Annalen
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Counting rational points on quartic del Pezzo surfaces with a rational conic
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 373
year: '2019'
...
---
_id: '175'
abstract:
- lang: eng
text: An upper bound sieve for rational points on suitable varieties isdeveloped,
together with applications tocounting rational points in thin sets,to local solubility
in families, and to the notion of “friable” rational pointswith respect to divisors.
In the special case of quadrics, sharper estimates areobtained by developing a
version of the Selberg sieve for rational points.
article_processing_charge: No
arxiv: 1
author:
- first_name: Timothy D
full_name: Browning, Timothy D
id: 35827D50-F248-11E8-B48F-1D18A9856A87
last_name: Browning
orcid: 0000-0002-8314-0177
- first_name: Daniel
full_name: Loughran, Daniel
last_name: Loughran
citation:
ama: Browning TD, Loughran D. Sieving rational points on varieties. Transactions
of the American Mathematical Society. 2019;371(8):5757-5785. doi:10.1090/tran/7514
apa: Browning, T. D., & Loughran, D. (2019). Sieving rational points on varieties.
Transactions of the American Mathematical Society. American Mathematical
Society. https://doi.org/10.1090/tran/7514
chicago: Browning, Timothy D, and Daniel Loughran. “Sieving Rational Points on Varieties.”
Transactions of the American Mathematical Society. American Mathematical
Society, 2019. https://doi.org/10.1090/tran/7514.
ieee: T. D. Browning and D. Loughran, “Sieving rational points on varieties,” Transactions
of the American Mathematical Society, vol. 371, no. 8. American Mathematical
Society, pp. 5757–5785, 2019.
ista: Browning TD, Loughran D. 2019. Sieving rational points on varieties. Transactions
of the American Mathematical Society. 371(8), 5757–5785.
mla: Browning, Timothy D., and Daniel Loughran. “Sieving Rational Points on Varieties.”
Transactions of the American Mathematical Society, vol. 371, no. 8, American
Mathematical Society, 2019, pp. 5757–85, doi:10.1090/tran/7514.
short: T.D. Browning, D. Loughran, Transactions of the American Mathematical Society
371 (2019) 5757–5785.
date_created: 2018-12-11T11:45:01Z
date_published: 2019-04-15T00:00:00Z
date_updated: 2023-08-24T14:34:56Z
day: '15'
department:
- _id: TiBr
doi: 10.1090/tran/7514
external_id:
arxiv:
- '1705.01999'
isi:
- '000464034200019'
intvolume: ' 371'
isi: 1
issue: '8'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1705.01999
month: '04'
oa: 1
oa_version: Preprint
page: 5757-5785
publication: Transactions of the American Mathematical Society
publication_identifier:
eissn:
- '10886850'
issn:
- '00029947'
publication_status: published
publisher: American Mathematical Society
publist_id: '7746'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Sieving rational points on varieties
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 371
year: '2019'
...
---
_id: '196'
abstract:
- lang: eng
text: 'The abelian sandpile serves as a model to study self-organized criticality,
a phenomenon occurring in biological, physical and social processes. The identity
of the abelian group is a fractal composed of self-similar patches, and its limit
is subject of extensive collaborative research. Here, we analyze the evolution
of the sandpile identity under harmonic fields of different orders. We show that
this evolution corresponds to periodic cycles through the abelian group characterized
by the smooth transformation and apparent conservation of the patches constituting
the identity. The dynamics induced by second and third order harmonics resemble
smooth stretchings, respectively translations, of the identity, while the ones
induced by fourth order harmonics resemble magnifications and rotations. Starting
with order three, the dynamics pass through extended regions of seemingly random
configurations which spontaneously reassemble into accentuated patterns. We show
that the space of harmonic functions projects to the extended analogue of the
sandpile group, thus providing a set of universal coordinates identifying configurations
between different domains. Since the original sandpile group is a subgroup of
the extended one, this directly implies that it admits a natural renormalization.
Furthermore, we show that the harmonic fields can be induced by simple Markov
processes, and that the corresponding stochastic dynamics show remarkable robustness
over hundreds of periods. Finally, we encode information into seemingly random
configurations, and decode this information with an algorithm requiring minimal
prior knowledge. Our results suggest that harmonic fields might split the sandpile
group into sub-sets showing different critical coefficients, and that it might
be possible to extend the fractal structure of the identity beyond the boundaries
of its domain. '
acknowledgement: "M.L. is grateful to the members of the C Guet and G Tkacik groups
for valuable comments and support. M.S. is grateful to Nikita Kalinin for inspiring
communications.\r\n"
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Moritz
full_name: Lang, Moritz
id: 29E0800A-F248-11E8-B48F-1D18A9856A87
last_name: Lang
- first_name: Mikhail
full_name: Shkolnikov, Mikhail
id: 35084A62-F248-11E8-B48F-1D18A9856A87
last_name: Shkolnikov
orcid: 0000-0002-4310-178X
citation:
ama: Lang M, Shkolnikov M. Harmonic dynamics of the Abelian sandpile. Proceedings
of the National Academy of Sciences. 2019;116(8):2821-2830. doi:10.1073/pnas.1812015116
apa: Lang, M., & Shkolnikov, M. (2019). Harmonic dynamics of the Abelian sandpile.
Proceedings of the National Academy of Sciences. National Academy of Sciences.
https://doi.org/10.1073/pnas.1812015116
chicago: Lang, Moritz, and Mikhail Shkolnikov. “Harmonic Dynamics of the Abelian
Sandpile.” Proceedings of the National Academy of Sciences. National Academy
of Sciences, 2019. https://doi.org/10.1073/pnas.1812015116.
ieee: M. Lang and M. Shkolnikov, “Harmonic dynamics of the Abelian sandpile,” Proceedings
of the National Academy of Sciences, vol. 116, no. 8. National Academy of
Sciences, pp. 2821–2830, 2019.
ista: Lang M, Shkolnikov M. 2019. Harmonic dynamics of the Abelian sandpile. Proceedings
of the National Academy of Sciences. 116(8), 2821–2830.
mla: Lang, Moritz, and Mikhail Shkolnikov. “Harmonic Dynamics of the Abelian Sandpile.”
Proceedings of the National Academy of Sciences, vol. 116, no. 8, National
Academy of Sciences, 2019, pp. 2821–30, doi:10.1073/pnas.1812015116.
short: M. Lang, M. Shkolnikov, Proceedings of the National Academy of Sciences 116
(2019) 2821–2830.
date_created: 2018-12-11T11:45:08Z
date_published: 2019-02-19T00:00:00Z
date_updated: 2023-09-11T14:09:34Z
day: '19'
department:
- _id: CaGu
- _id: GaTk
- _id: TaHa
doi: 10.1073/pnas.1812015116
external_id:
arxiv:
- '1806.10823'
isi:
- '000459074400013'
pmid:
- ' 30728300'
intvolume: ' 116'
isi: 1
issue: '8'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1812015116
month: '02'
oa: 1
oa_version: Published Version
page: 2821-2830
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
related_material:
link:
- description: News on IST Webpage
relation: press_release
url: https://ist.ac.at/en/news/famous-sandpile-model-shown-to-move-like-a-traveling-sand-dune/
scopus_import: '1'
status: public
title: Harmonic dynamics of the Abelian sandpile
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 116
year: '2019'
...