---
_id: '8263'
abstract:
- lang: eng
  text: "Background: The genus Streptococcus comprises pathogens that strongly influence
    the health of humans and animals. Genome sequencing of multiple Streptococcus
    strains demonstrated high variability in gene content and order even in closely
    related strains of the same species and created a newly emerged object for genomic
    analysis, the pan-genome. Here we analysed the genome evolution of 25 strains
    of Streptococcus suis, 50 strains of Streptococcus pyogenes and 28 strains of
    Streptococcus pneumoniae.\r\n\r\nResults: Fractions of the pan-genome, unique,
    periphery, and universal genes differ in size, functional composition, the level
    of nucleotide substitutions, and predisposition to horizontal gene transfer and
    genomic rearrangements. The density of substitutions in intergenic regions appears
    to be correlated with selection acting on adjacent genes, implying that more conserved
    genes tend to have more conserved regulatory regions.\r\nThe total pan-genome
    of the genus is open, but only due to strain-specific genes, whereas other pan-genome
    fractions reach saturation. We have identified the set of genes with phylogenies
    inconsistent with species and non-conserved location in the chromosome; these
    genes are rare in at least one species and have likely experienced recent horizontal
    transfer between species. The strain-specific fraction is enriched with mobile
    elements and hypothetical proteins, but also contains a number of candidate virulence-related
    genes, so it may have a strong impact on adaptability and pathogenicity.\r\nMapping
    the rearrangements to the phylogenetic tree revealed large parallel inversions
    in all species. A parallel inversion of length 15 kB with breakpoints formed by
    genes encoding surface antigen proteins PhtD and PhtB in S. pneumoniae leads to
    replacement of gene fragments that likely indicates the action of an antigen variation
    mechanism.\r\n\r\nConclusions: Members of genus Streptococcus have a highly dynamic,
    open pan-genome, that potentially confers them with the ability to adapt to changing
    environmental conditions, i.e. antibiotic resistance or transmission between different
    hosts. Hence, integrated analysis of all aspects of genome evolution is important
    for the identification of potential pathogens and design of drugs and vaccines."
article_number: '83'
article_processing_charge: No
article_type: original
author:
- first_name: Pavel V.
  full_name: Shelyakin, Pavel V.
  last_name: Shelyakin
  orcid: 0000-0003-0120-9319
- first_name: Olga
  full_name: Bochkareva, Olga
  id: C4558D3C-6102-11E9-A62E-F418E6697425
  last_name: Bochkareva
  orcid: 0000-0003-1006-6639
- first_name: Anna A.
  full_name: Karan, Anna A.
  last_name: Karan
- first_name: Mikhail S.
  full_name: Gelfand, Mikhail S.
  last_name: Gelfand
citation:
  ama: 'Shelyakin PV, Bochkareva O, Karan AA, Gelfand MS. Micro-evolution of three
    Streptococcus species: Selection, antigenic variation, and horizontal gene inflow.
    <i>BMC Evolutionary Biology</i>. 2019;19. doi:<a href="https://doi.org/10.1186/s12862-019-1403-6">10.1186/s12862-019-1403-6</a>'
  apa: 'Shelyakin, P. V., Bochkareva, O., Karan, A. A., &#38; Gelfand, M. S. (2019).
    Micro-evolution of three Streptococcus species: Selection, antigenic variation,
    and horizontal gene inflow. <i>BMC Evolutionary Biology</i>. Springer Nature.
    <a href="https://doi.org/10.1186/s12862-019-1403-6">https://doi.org/10.1186/s12862-019-1403-6</a>'
  chicago: 'Shelyakin, Pavel V., Olga Bochkareva, Anna A. Karan, and Mikhail S. Gelfand.
    “Micro-Evolution of Three Streptococcus Species: Selection, Antigenic Variation,
    and Horizontal Gene Inflow.” <i>BMC Evolutionary Biology</i>. Springer Nature,
    2019. <a href="https://doi.org/10.1186/s12862-019-1403-6">https://doi.org/10.1186/s12862-019-1403-6</a>.'
  ieee: 'P. V. Shelyakin, O. Bochkareva, A. A. Karan, and M. S. Gelfand, “Micro-evolution
    of three Streptococcus species: Selection, antigenic variation, and horizontal
    gene inflow,” <i>BMC Evolutionary Biology</i>, vol. 19. Springer Nature, 2019.'
  ista: 'Shelyakin PV, Bochkareva O, Karan AA, Gelfand MS. 2019. Micro-evolution of
    three Streptococcus species: Selection, antigenic variation, and horizontal gene
    inflow. BMC Evolutionary Biology. 19, 83.'
  mla: 'Shelyakin, Pavel V., et al. “Micro-Evolution of Three Streptococcus Species:
    Selection, Antigenic Variation, and Horizontal Gene Inflow.” <i>BMC Evolutionary
    Biology</i>, vol. 19, 83, Springer Nature, 2019, doi:<a href="https://doi.org/10.1186/s12862-019-1403-6">10.1186/s12862-019-1403-6</a>.'
  short: P.V. Shelyakin, O. Bochkareva, A.A. Karan, M.S. Gelfand, BMC Evolutionary
    Biology 19 (2019).
date_created: 2020-08-15T11:04:07Z
date_published: 2019-03-27T00:00:00Z
date_updated: 2023-02-23T13:28:54Z
day: '27'
doi: 10.1186/s12862-019-1403-6
extern: '1'
intvolume: '        19'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1186/s12862-019-1403-6
month: '03'
oa: 1
oa_version: Published Version
publication: BMC Evolutionary Biology
publication_identifier:
  issn:
  - 1471-2148
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Micro-evolution of three Streptococcus species: Selection, antigenic variation,
  and horizontal gene inflow'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2019'
...
---
_id: '8281'
abstract:
- lang: eng
  text: We review the history of population genetics, starting with its origins a
    century ago from the synthesis between Mendel and Darwin's ideas, through to the
    recent development of sophisticated schemes of inference from sequence data, based
    on the coalescent. We explain the close relation between the coalescent and a
    diffusion process, which we illustrate by their application to understand spatial
    structure. We summarise the powerful methods available for analysis of multiple
    loci, when linkage equilibrium can be assumed, and then discuss approaches to
    the more challenging case, where associations between alleles require that we
    follow genotype, rather than allele, frequencies. Though we can hardly cover the
    whole of population genetics, we give an overview of the current state of the
    subject, and future challenges to it.
article_processing_charge: No
author:
- first_name: Nicholas H
  full_name: Barton, Nicholas H
  id: 4880FE40-F248-11E8-B48F-1D18A9856A87
  last_name: Barton
  orcid: 0000-0002-8548-5240
- first_name: Alison
  full_name: Etheridge, Alison
  last_name: Etheridge
citation:
  ama: 'Barton NH, Etheridge A. Mathematical models in population genetics. In: Balding
    D, Moltke I, Marioni J, eds. <i>Handbook of Statistical Genomics</i>. 4th ed.
    Wiley; 2019:115-144. doi:<a href="https://doi.org/10.1002/9781119487845.ch4">10.1002/9781119487845.ch4</a>'
  apa: Barton, N. H., &#38; Etheridge, A. (2019). Mathematical models in population
    genetics. In D. Balding, I. Moltke, &#38; J. Marioni (Eds.), <i>Handbook of statistical
    genomics</i> (4th ed., pp. 115–144). Wiley. <a href="https://doi.org/10.1002/9781119487845.ch4">https://doi.org/10.1002/9781119487845.ch4</a>
  chicago: Barton, Nicholas H, and Alison Etheridge. “Mathematical Models in Population
    Genetics.” In <i>Handbook of Statistical Genomics</i>, edited by David Balding,
    Ida Moltke, and John Marioni, 4th ed., 115–44. Wiley, 2019. <a href="https://doi.org/10.1002/9781119487845.ch4">https://doi.org/10.1002/9781119487845.ch4</a>.
  ieee: N. H. Barton and A. Etheridge, “Mathematical models in population genetics,”
    in <i>Handbook of statistical genomics</i>, 4th ed., D. Balding, I. Moltke, and
    J. Marioni, Eds. Wiley, 2019, pp. 115–144.
  ista: 'Barton NH, Etheridge A. 2019.Mathematical models in population genetics.
    In: Handbook of statistical genomics. , 115–144.'
  mla: Barton, Nicholas H., and Alison Etheridge. “Mathematical Models in Population
    Genetics.” <i>Handbook of Statistical Genomics</i>, edited by David Balding et
    al., 4th ed., Wiley, 2019, pp. 115–44, doi:<a href="https://doi.org/10.1002/9781119487845.ch4">10.1002/9781119487845.ch4</a>.
  short: N.H. Barton, A. Etheridge, in:, D. Balding, I. Moltke, J. Marioni (Eds.),
    Handbook of Statistical Genomics, 4th ed., Wiley, 2019, pp. 115–144.
date_created: 2020-08-21T04:25:39Z
date_published: 2019-07-29T00:00:00Z
date_updated: 2023-09-08T11:24:15Z
day: '29'
ddc:
- '576'
department:
- _id: NiBa
doi: 10.1002/9781119487845.ch4
edition: '4'
editor:
- first_name: David
  full_name: Balding, David
  last_name: Balding
- first_name: Ida
  full_name: Moltke, Ida
  last_name: Moltke
- first_name: John
  full_name: Marioni, John
  last_name: Marioni
external_id:
  isi:
  - '000261343000003'
isi: 1
language:
- iso: eng
month: '07'
oa_version: None
page: 115-144
publication: Handbook of statistical genomics
publication_identifier:
  isbn:
  - '9781119429142'
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Mathematical models in population genetics
type: book_chapter
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2019'
...
---
_id: '8296'
abstract:
- lang: eng
  text: While showing great promise, smart contracts are difficult to program correctly,
    as they need a deep understanding of cryptography and distributed algorithms,
    and offer limited functionality, as they have to be deterministic and cannot operate
    on secret data. In this paper we present Protean, a general-purpose decentralized
    computing platform that addresses these limitations by moving from a monolithic
    execution model, where all participating nodes store all the state and execute
    every computation, to a modular execution-model. Protean employs secure specialized
    modules, called functional units, for building decentralized applications that
    are currently insecure or impossible to implement with smart contracts. Each functional
    unit is a distributed system that provides a special-purpose functionality by
    exposing atomic transactions to the smart-contract developer. Combining these
    transactions into arbitrarily-defined workflows, developers can build a larger
    class of decentralized applications, such as provably-secure and fair lotteries
    or e-voting.
article_processing_charge: No
author:
- first_name: Enis Ceyhun
  full_name: Alp, Enis Ceyhun
  last_name: Alp
- first_name: Eleftherios
  full_name: Kokoris Kogias, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: Kokoris Kogias
- first_name: Georgia
  full_name: Fragkouli, Georgia
  last_name: Fragkouli
- first_name: Bryan
  full_name: Ford, Bryan
  last_name: Ford
citation:
  ama: 'Alp EC, Kokoris Kogias E, Fragkouli G, Ford B. Rethinking general-purpose
    decentralized computing. In: <i>Proceedings of the Workshop on Hot Topics in Operating
    Systems</i>. ACM; 2019:105-112. doi:<a href="https://doi.org/10.1145/3317550.3321448">10.1145/3317550.3321448</a>'
  apa: 'Alp, E. C., Kokoris Kogias, E., Fragkouli, G., &#38; Ford, B. (2019). Rethinking
    general-purpose decentralized computing. In <i>Proceedings of the Workshop on
    Hot Topics in Operating Systems</i> (pp. 105–112). Bertinoro, Italy: ACM. <a href="https://doi.org/10.1145/3317550.3321448">https://doi.org/10.1145/3317550.3321448</a>'
  chicago: Alp, Enis Ceyhun, Eleftherios Kokoris Kogias, Georgia Fragkouli, and Bryan
    Ford. “Rethinking General-Purpose Decentralized Computing.” In <i>Proceedings
    of the Workshop on Hot Topics in Operating Systems</i>, 105–12. ACM, 2019. <a
    href="https://doi.org/10.1145/3317550.3321448">https://doi.org/10.1145/3317550.3321448</a>.
  ieee: E. C. Alp, E. Kokoris Kogias, G. Fragkouli, and B. Ford, “Rethinking general-purpose
    decentralized computing,” in <i>Proceedings of the Workshop on Hot Topics in Operating
    Systems</i>, Bertinoro, Italy, 2019, pp. 105–112.
  ista: 'Alp EC, Kokoris Kogias E, Fragkouli G, Ford B. 2019. Rethinking general-purpose
    decentralized computing. Proceedings of the Workshop on Hot Topics in Operating
    Systems. HotOS: Workshop on Hot Topics in Operating Systems, 105–112.'
  mla: Alp, Enis Ceyhun, et al. “Rethinking General-Purpose Decentralized Computing.”
    <i>Proceedings of the Workshop on Hot Topics in Operating Systems</i>, ACM, 2019,
    pp. 105–12, doi:<a href="https://doi.org/10.1145/3317550.3321448">10.1145/3317550.3321448</a>.
  short: E.C. Alp, E. Kokoris Kogias, G. Fragkouli, B. Ford, in:, Proceedings of the
    Workshop on Hot Topics in Operating Systems, ACM, 2019, pp. 105–112.
conference:
  end_date: 2019-05-15
  location: Bertinoro, Italy
  name: 'HotOS: Workshop on Hot Topics in Operating Systems'
  start_date: 2019-05-13
date_created: 2020-08-26T11:45:45Z
date_published: 2019-05-01T00:00:00Z
date_updated: 2021-01-12T08:17:56Z
day: '01'
doi: 10.1145/3317550.3321448
extern: '1'
language:
- iso: eng
month: '05'
oa_version: None
page: 105-112
publication: Proceedings of the Workshop on Hot Topics in Operating Systems
publication_identifier:
  isbn:
  - '9781450367271'
publication_status: published
publisher: ACM
quality_controlled: '1'
scopus_import: '1'
status: public
title: Rethinking general-purpose decentralized computing
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2019'
...
---
_id: '8303'
abstract:
- lang: eng
  text: 'ByzCoin, a promising alternative of Bitcoin, is a scalable consensus protocol
    used as a building block of many research and enterprise-level decentralized systems.
    In this paper, we show that ByzCoin is unsuitable for deployment in an anopen,
    adversarial network and instead introduceMOTOR. MOTORis designed as a secure,
    robust, and scalable consensus suitable for permissionless sharded blockchains.
    MOTORachieves these properties by making four key design choices: (a) it prioritizes
    robustness in adversarial environments while maintaining adequate scalability,
    (b) it employees provably correct cryptography that resists DoS attacks from individual
    nodes, (c) it deploys unpredictable rotating leaders to defend against mildly-adaptive
    adversaries and prevents censorship, and (d) it creates an incentive compatible
    reward mechanism. These choices are materialized as (a) a “rotating subleader”
    communication pattern that balances the scalability needs with the robustness
    requirements under failures, (b) deployment of provable secure BLS multi-signatures,
    (c) use of deterministic thresh-old signatures as a source of randomness and (d)
    careful design of the reward allocation mechanism. We have implemented MOTORand
    compare it withByzCoin. We show that MOTORcan scale similar to ByzCoin with an
    at most2xoverhead whereas it maintains good performance even under high-percentage
    of faults, unlike ByzCoin.'
article_number: 2019/676
article_processing_charge: No
author:
- first_name: Eleftherios
  full_name: Kokoris Kogias, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: Kokoris Kogias
citation:
  ama: Kokoris Kogias E. Robust and scalable consensus for sharded distributed ledgers.
    <i>Cryptology ePrint Archive</i>.
  apa: Kokoris Kogias, E. (n.d.). Robust and scalable consensus for sharded distributed
    ledgers. <i>Cryptology ePrint Archive</i>.
  chicago: Kokoris Kogias, Eleftherios. “Robust and Scalable Consensus for Sharded
    Distributed Ledgers.” <i>Cryptology EPrint Archive</i>, n.d.
  ieee: E. Kokoris Kogias, “Robust and scalable consensus for sharded distributed
    ledgers,” <i>Cryptology ePrint Archive</i>. .
  ista: Kokoris Kogias E. Robust and scalable consensus for sharded distributed ledgers.
    Cryptology ePrint Archive, 2019/676.
  mla: Kokoris Kogias, Eleftherios. “Robust and Scalable Consensus for Sharded Distributed
    Ledgers.” <i>Cryptology EPrint Archive</i>, 2019/676.
  short: E. Kokoris Kogias, Cryptology EPrint Archive (n.d.).
date_created: 2020-08-26T12:13:56Z
date_published: 2019-06-06T00:00:00Z
date_updated: 2021-09-24T12:07:11Z
day: '06'
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://eprint.iacr.org/2019/676
month: '06'
oa: 1
oa_version: Preprint
publication: Cryptology ePrint Archive
publication_status: submitted
status: public
title: Robust and scalable consensus for sharded distributed ledgers
type: preprint
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2019'
...
---
_id: '8304'
abstract:
- lang: eng
  text: "Enabling secure communication across distributed systems is usually studied
    under the assumption of trust between the different systems and an external adversary
    trying to compromise the messages. With the appearance of distributed ledgers
    or blockchains, numerous protocols have emerged, which attempt to achieve trustless
    communication between distrusting ledgers and participants. Cross-chain communication
    (CCC) thereby plays a fundamental role in cryptocurrency exchanges, sharding,
    bootstrapping of new and feature-extension of existing distributed ledgers. Unfortunately,
    existing proposals are designed ad-hoc for specific use-cases, making it hard
    to gain confidence on their correctness and composability.\r\nWe provide the first
    systematic exposition of protocols for CCC. First, we formalize the underlying
    research problem and show that CCC is impossible without a trusted third party,
    contrary to common beliefs in the blockchain community. We then develop a framework
    to evaluate existing and to design new cross-chain protocols. The framework is
    based on the use case, the trust model, and the security assumptions of interlinked
    blockchains. Finally, we identify security and privacy challenges faced by protocols
    in the cross-chain setting.\r\nThis Systematization of Knowledge (SoK) offers
    a comprehensive guide for designing protocols bridging the numerous distributed
    ledgers available today. It aims to facilitate clearer communication between academia
    and industry in the field."
article_number: 2019/1128
article_processing_charge: No
author:
- first_name: Alexei
  full_name: Zamyatin, Alexei
  last_name: Zamyatin
- first_name: Mustafa
  full_name: Al-Bassam, Mustafa
  last_name: Al-Bassam
- first_name: Dionysis
  full_name: Zindros, Dionysis
  last_name: Zindros
- first_name: Eleftherios
  full_name: Kokoris Kogias, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: Kokoris Kogias
- first_name: Pedro
  full_name: Moreno-Sanchez, Pedro
  last_name: Moreno-Sanchez
- first_name: Aggelos
  full_name: Kiayias, Aggelos
  last_name: Kiayias
- first_name: William J.
  full_name: Knottenbelt, William J.
  last_name: Knottenbelt
citation:
  ama: 'Zamyatin A, Al-Bassam M, Zindros D, et al. SoK: Communication across distributed
    ledgers. <i>Cryptology ePrint Archive</i>.'
  apa: 'Zamyatin, A., Al-Bassam, M., Zindros, D., Kokoris Kogias, E., Moreno-Sanchez,
    P., Kiayias, A., &#38; Knottenbelt, W. J. (n.d.). SoK: Communication across distributed
    ledgers. <i>Cryptology ePrint Archive</i>.'
  chicago: 'Zamyatin, Alexei, Mustafa Al-Bassam, Dionysis Zindros, Eleftherios Kokoris
    Kogias, Pedro Moreno-Sanchez, Aggelos Kiayias, and William J. Knottenbelt. “SoK:
    Communication across Distributed Ledgers.” <i>Cryptology EPrint Archive</i>, n.d.'
  ieee: 'A. Zamyatin <i>et al.</i>, “SoK: Communication across distributed ledgers,”
    <i>Cryptology ePrint Archive</i>. .'
  ista: 'Zamyatin A, Al-Bassam M, Zindros D, Kokoris Kogias E, Moreno-Sanchez P, Kiayias
    A, Knottenbelt WJ. SoK: Communication across distributed ledgers. Cryptology ePrint
    Archive, 2019/1128.'
  mla: 'Zamyatin, Alexei, et al. “SoK: Communication across Distributed Ledgers.”
    <i>Cryptology EPrint Archive</i>, 2019/1128.'
  short: A. Zamyatin, M. Al-Bassam, D. Zindros, E. Kokoris Kogias, P. Moreno-Sanchez,
    A. Kiayias, W.J. Knottenbelt, Cryptology EPrint Archive (n.d.).
date_created: 2020-08-26T12:16:38Z
date_published: 2019-10-01T00:00:00Z
date_updated: 2021-09-24T12:08:14Z
day: '01'
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: 'https://eprint.iacr.org/2019/1128 '
month: '10'
oa: 1
oa_version: Preprint
publication: Cryptology ePrint Archive
publication_status: submitted
status: public
title: 'SoK: Communication across distributed ledgers'
type: preprint
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2019'
...
---
_id: '8305'
abstract:
- lang: eng
  text: In this paper, we present the first fully asynchronous distributed key generation
    (ADKG) algorithm as well as the first distributed key generation algorithm that
    can create keys with a dual (f,2f+1)−threshold that are necessary for scalable
    consensus (which so far needs a trusted dealer assumption). In order to create
    a DKG with a dual (f,2f+1)− threshold we first answer in the affirmative the open
    question posed by Cachin et al. how to create an AVSS protocol with recovery thresholds
    f+1<k≤2f+1, which is of independent interest. Our High-threshold-AVSS (HAVSS)
    uses an asymmetric bi-variate polynomial, where the secret shared is hidden from
    any set of k nodes but an honest node that did not participate in the sharing
    phase can still recover his share with only n−2f shares, hence be able to contribute
    in the secret reconstruction. Another building block for ADKG is a novel Eventually
    Perfect Common Coin (EPCC) abstraction and protocol that enables the participants
    to create a common coin that might fail to agree at most f+1 times (even if invoked
    a polynomial number of times). Using EPCC we implement an Eventually Efficient
    Asynchronous Binary Agreement (EEABA) in which each instance takes O(n2) bits
    and O(1) rounds in expectation, except for at most f+1 instances which may take
    O(n4) bits and O(n) rounds in total. Using EEABA we construct the first fully
    Asynchronous Distributed Key Generation (ADKG) which has the same overhead and
    expected runtime as the best partially-synchronous DKG (O(n4) words, O(n) rounds).
    As a corollary of our ADKG we can also create the first Validated Asynchronous
    Byzantine Agreement (VABA) in the authenticated setting that does not need a trusted
    dealer to setup threshold signatures of degree n−f. Our VABA has an overhead of
    expected O(n2) words and O(1) time per instance after an initial O(n4) words and
    O(n) time bootstrap via ADKG.
article_number: 2019/1015
article_processing_charge: No
author:
- first_name: Eleftherios
  full_name: KOKORIS KOGIAS, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: KOKORIS KOGIAS
- first_name: Alexander
  full_name: Spiegelman, Alexander
  last_name: Spiegelman
- first_name: Dahlia
  full_name: Malkhi, Dahlia
  last_name: Malkhi
- first_name: Ittai
  full_name: Abraham, Ittai
  last_name: Abraham
citation:
  ama: 'Kokoris Kogias E, Spiegelman A, Malkhi D, Abraham I. Bootstrapping consensus
    without trusted setup: fully asynchronous distributed key generation. <i>Cryptology
    ePrint Archive</i>.'
  apa: 'Kokoris Kogias, E., Spiegelman, A., Malkhi, D., &#38; Abraham, I. (n.d.).
    Bootstrapping consensus without trusted setup: fully asynchronous distributed
    key generation. <i>Cryptology ePrint Archive</i>.'
  chicago: 'Kokoris Kogias, Eleftherios, Alexander Spiegelman, Dahlia Malkhi, and
    Ittai Abraham. “Bootstrapping Consensus without Trusted Setup: Fully Asynchronous
    Distributed Key Generation.” <i>Cryptology EPrint Archive</i>, n.d.'
  ieee: 'E. Kokoris Kogias, A. Spiegelman, D. Malkhi, and I. Abraham, “Bootstrapping
    consensus without trusted setup: fully asynchronous distributed key generation,”
    <i>Cryptology ePrint Archive</i>. .'
  ista: 'Kokoris Kogias E, Spiegelman A, Malkhi D, Abraham I. Bootstrapping consensus
    without trusted setup: fully asynchronous distributed key generation. Cryptology
    ePrint Archive, 2019/1015.'
  mla: 'Kokoris Kogias, Eleftherios, et al. “Bootstrapping Consensus without Trusted
    Setup: Fully Asynchronous Distributed Key Generation.” <i>Cryptology EPrint Archive</i>,
    2019/1015.'
  short: E. Kokoris Kogias, A. Spiegelman, D. Malkhi, I. Abraham, Cryptology EPrint
    Archive (n.d.).
date_created: 2020-08-26T12:18:00Z
date_published: 2019-09-10T00:00:00Z
date_updated: 2023-05-10T09:27:54Z
day: '10'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://eprint.iacr.org/2019/1015
month: '09'
oa: 1
oa_version: Preprint
publication: Cryptology ePrint Archive
publication_status: submitted
status: public
title: 'Bootstrapping consensus without trusted setup: fully asynchronous distributed
  key generation'
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2019'
...
---
_id: '8311'
abstract:
- lang: eng
  text: 'One of the core promises of blockchain technology is that of enabling trustworthy
    data dissemination in a trustless environment. What current blockchain systems
    deliver, however, is slow dissemination of public data, rendering blockchain technology
    unusable in settings where latency, transaction capacity, or data confidentiality
    are important. In this thesis we focus on providing solutions on two of the most
    pressing problems blockchain technology currently faces: scalability and data
    confidentiality. To address the scalability issue, we present OMNILEDGER, a novel
    scale-out distributed ledger that preserves long-term security under permissionless
    operation. It ensures security and correctness by using a bias-resistant public-randomness
    protocol for choosing large, statistically representative shards that process
    transactions, and by introducing an efficient cross-shard commit protocol that
    atomically handles transactions affecting multiple shards. To enable secure sharing
    of confidential data we present CALYPSO, the first fully decentralized, auditable
    access-control framework for secure blockchain-based data sharing which builds
    upon two abstractions. First, on-chain secrets enable collective management of
    (verifiably shared) secrets under a Byzantine adversary where an access-control
    blockchain enforces user-specific access rules and a secret-management cothority
    administers encrypted data. Second, skipchain-based identity and access management
    enables efficient administration of dynamic, sovereign identities and access policies
    and, in particular, permits clients to maintain long-term relationships with respect
    to evolving user identities thanks to the trust-delegating forward links of skipchains.
    In order to build OMNILEDGER and CALYPSO, we first build a set of tools for efficient
    decentralization, which are presented in Part II of this dissertation. These tools
    can be used in decentralized and distributed systems to achieve (1) scalable consensus
    (BYZCOIN), (2) bias- resistant distributed randomness creations (RANDHOUND), and
    (3) relationship-keeping between independently updating communication endpoints
    (SKIPCHAINIAC). Although we use this tools in the scope off this thesis, they
    can be (and already have been) used in a far wider scope.'
article_processing_charge: No
author:
- first_name: Eleftherios
  full_name: Kokoris Kogias, Eleftherios
  id: f5983044-d7ef-11ea-ac6d-fd1430a26d30
  last_name: Kokoris Kogias
citation:
  ama: Kokoris Kogias E. Secure, confidential blockchains providing high throughput
    and low latency. 2019. doi:<a href="https://doi.org/10.5075/epfl-thesis-7101">10.5075/epfl-thesis-7101</a>
  apa: Kokoris Kogias, E. (2019). <i>Secure, confidential blockchains providing high
    throughput and low latency</i>. École Polytechnique Fédérale de Lausanne. <a href="https://doi.org/10.5075/epfl-thesis-7101">https://doi.org/10.5075/epfl-thesis-7101</a>
  chicago: Kokoris Kogias, Eleftherios. “Secure, Confidential Blockchains Providing
    High Throughput and Low Latency.” École Polytechnique Fédérale de Lausanne, 2019.
    <a href="https://doi.org/10.5075/epfl-thesis-7101">https://doi.org/10.5075/epfl-thesis-7101</a>.
  ieee: E. Kokoris Kogias, “Secure, confidential blockchains providing high throughput
    and low latency,” École Polytechnique Fédérale de Lausanne, 2019.
  ista: Kokoris Kogias E. 2019. Secure, confidential blockchains providing high throughput
    and low latency. École Polytechnique Fédérale de Lausanne.
  mla: Kokoris Kogias, Eleftherios. <i>Secure, Confidential Blockchains Providing
    High Throughput and Low Latency</i>. École Polytechnique Fédérale de Lausanne,
    2019, doi:<a href="https://doi.org/10.5075/epfl-thesis-7101">10.5075/epfl-thesis-7101</a>.
  short: E. Kokoris Kogias, Secure, Confidential Blockchains Providing High Throughput
    and Low Latency, École Polytechnique Fédérale de Lausanne, 2019.
date_created: 2020-08-27T11:22:24Z
date_published: 2019-09-27T00:00:00Z
date_updated: 2021-12-20T15:30:47Z
day: '27'
degree_awarded: PhD
doi: 10.5075/epfl-thesis-7101
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.doi.org/10.5075/epfl-thesis-7101
month: '09'
oa: 1
oa_version: Published Version
page: '244'
publication_status: published
publisher: École Polytechnique Fédérale de Lausanne
status: public
supervisor:
- first_name: Bryan Alexander
  full_name: Ford, Bryan Alexander
  last_name: Ford
title: Secure, confidential blockchains providing high throughput and low latency
type: dissertation
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2019'
...
---
_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., &#38; 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. <i>Methods and Systems for Secure Data Exchange</i>. 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. <i>arXiv</i>.'
  apa: 'Avarikioti, G., Kokoris Kogias, E., Wattenhofer, R., &#38; Zindros, D. (n.d.).
    Brick: Asynchronous payment channels. <i>arXiv</i>.'
  chicago: 'Avarikioti, Georgia, Eleftherios Kokoris Kogias, Roger Wattenhofer, and
    Dionysis Zindros. “Brick: Asynchronous Payment Channels.” <i>ArXiv</i>, n.d.'
  ieee: 'G. Avarikioti, E. Kokoris Kogias, R. Wattenhofer, and D. Zindros, “Brick:
    Asynchronous payment channels,” <i>arXiv</i>. .'
  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.” <i>ArXiv</i>,
    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. <i>arXiv</i>.'
  apa: 'Avarikioti, G., Kokoris Kogias, E., &#38; Wattenhofer, R. (n.d.). Divide and
    scale: Formalization of distributed ledger sharding protocols. <i>arXiv</i>.'
  chicago: 'Avarikioti, Georgia, Eleftherios Kokoris Kogias, and Roger Wattenhofer.
    “Divide and Scale: Formalization of Distributed Ledger Sharding Protocols.” <i>ArXiv</i>,
    n.d.'
  ieee: 'G. Avarikioti, E. Kokoris Kogias, and R. Wattenhofer, “Divide and scale:
    Formalization of distributed ledger sharding protocols,” <i>arXiv</i>. .'
  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.” <i>ArXiv</i>, 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. <i>Nature Communications</i>.
    2019;10. doi:<a href="https://doi.org/10.1038/s41467-019-10490-9">10.1038/s41467-019-10490-9</a>
  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. <i>Nature Communications</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41467-019-10490-9">https://doi.org/10.1038/s41467-019-10490-9</a>
  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.”
    <i>Nature Communications</i>. Springer Nature, 2019. <a href="https://doi.org/10.1038/s41467-019-10490-9">https://doi.org/10.1038/s41467-019-10490-9</a>.
  ieee: D. F. Gauto <i>et al.</i>, “Integrated NMR and cryo-EM atomic-resolution structure
    determination of a half-megadalton enzyme complex,” <i>Nature Communications</i>,
    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.” <i>Nature Communications</i>,
    vol. 10, 2697, Springer Nature, 2019, doi:<a href="https://doi.org/10.1038/s41467-019-10490-9">10.1038/s41467-019-10490-9</a>.
  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. <i>Science
    Advances</i>. 2019;5(9). doi:<a href="https://doi.org/10.1126/sciadv.aaw3818">10.1126/sciadv.aaw3818</a>
  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. <i>Science Advances</i>. American
    Association for the Advancement of Science. <a href="https://doi.org/10.1126/sciadv.aaw3818">https://doi.org/10.1126/sciadv.aaw3818</a>
  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.” <i>Science
    Advances</i>. American Association for the Advancement of Science, 2019. <a href="https://doi.org/10.1126/sciadv.aaw3818">https://doi.org/10.1126/sciadv.aaw3818</a>.
  ieee: J. Felix <i>et al.</i>, “Mechanism of the allosteric activation of the ClpP
    protease machinery by substrates and active-site inhibitors,” <i>Science Advances</i>,
    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.” <i>Science Advances</i>,
    vol. 5, no. 9, eaaw3818, American Association for the Advancement of Science,
    2019, doi:<a href="https://doi.org/10.1126/sciadv.aaw3818">10.1126/sciadv.aaw3818</a>.
  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. <i>Journal of Magnetic Resonance</i>. 2019;306:180-186. doi:<a href="https://doi.org/10.1016/j.jmr.2019.07.025">10.1016/j.jmr.2019.07.025</a>
  apa: Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular
    dynamics. <i>Journal of Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2019.07.025">https://doi.org/10.1016/j.jmr.2019.07.025</a>
  chicago: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
    Dynamics.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2019. <a href="https://doi.org/10.1016/j.jmr.2019.07.025">https://doi.org/10.1016/j.jmr.2019.07.025</a>.
  ieee: P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular
    dynamics,” <i>Journal of Magnetic Resonance</i>, 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.” <i>Journal of Magnetic Resonance</i>, vol. 306, Elsevier, 2019, pp.
    180–86, doi:<a href="https://doi.org/10.1016/j.jmr.2019.07.025">10.1016/j.jmr.2019.07.025</a>.
  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. <i>Journal of the American Chemical Society</i>.
    2019;141(28):11183-11195. doi:<a href="https://doi.org/10.1021/jacs.9b04219">10.1021/jacs.9b04219</a>
  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. <i>Journal of the American Chemical Society</i>. American Chemical
    Society. <a href="https://doi.org/10.1021/jacs.9b04219">https://doi.org/10.1021/jacs.9b04219</a>
  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.” <i>Journal of the American Chemical Society</i>.
    American Chemical Society, 2019. <a href="https://doi.org/10.1021/jacs.9b04219">https://doi.org/10.1021/jacs.9b04219</a>.
  ieee: D. F. Gauto <i>et al.</i>, “Aromatic ring dynamics, thermal activation, and
    transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast
    magic-angle spinning NMR,” <i>Journal of the American Chemical Society</i>, 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.” <i>Journal of the American Chemical Society</i>, vol. 141, no.
    28, American Chemical Society, 2019, pp. 11183–95, doi:<a href="https://doi.org/10.1021/jacs.9b04219">10.1021/jacs.9b04219</a>.
  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. <i>Journal
    of Structural Biology</i>. 2019;206(1):66-72. doi:<a href="https://doi.org/10.1016/j.jsb.2018.07.009">10.1016/j.jsb.2018.07.009</a>
  apa: Bougault, C., Ayala, I., Vollmer, W., Simorre, J.-P., &#38; Schanda, P. (2019).
    Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at
    100 kHz MAS frequency. <i>Journal of Structural Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.jsb.2018.07.009">https://doi.org/10.1016/j.jsb.2018.07.009</a>
  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.” <i>Journal of Structural Biology</i>.
    Elsevier, 2019. <a href="https://doi.org/10.1016/j.jsb.2018.07.009">https://doi.org/10.1016/j.jsb.2018.07.009</a>.
  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,” <i>Journal of Structural Biology</i>, 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.” <i>Journal of Structural Biology</i>,
    vol. 206, no. 1, Elsevier, 2019, pp. 66–72, doi:<a href="https://doi.org/10.1016/j.jsb.2018.07.009">10.1016/j.jsb.2018.07.009</a>.
  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. <i>ChemPhysChem</i>. 2019;20(2):177-177.
    doi:<a href="https://doi.org/10.1002/cphc.201801100">10.1002/cphc.201801100</a>
  apa: Schanda, P., &#38; Chekmenev, E. Y. (2019). NMR for Biological Systems. <i>ChemPhysChem</i>.
    Wiley. <a href="https://doi.org/10.1002/cphc.201801100">https://doi.org/10.1002/cphc.201801100</a>
  chicago: Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” <i>ChemPhysChem</i>.
    Wiley, 2019. <a href="https://doi.org/10.1002/cphc.201801100">https://doi.org/10.1002/cphc.201801100</a>.
  ieee: P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” <i>ChemPhysChem</i>,
    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.” <i>ChemPhysChem</i>,
    vol. 20, no. 2, Wiley, 2019, pp. 177–177, doi:<a href="https://doi.org/10.1002/cphc.201801100">10.1002/cphc.201801100</a>.
  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. <i>ChemPhysChem</i>. 2019;20(2):276-284. doi:<a href="https://doi.org/10.1002/cphc.201800935">10.1002/cphc.201800935</a>
  apa: Marion, D., Gauto, D. F., Ayala, I., Giandoreggio-Barranco, K., &#38; Schanda,
    P. (2019). Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
    R1p relaxation-dispersion MAS NMR. <i>ChemPhysChem</i>. Wiley. <a href="https://doi.org/10.1002/cphc.201800935">https://doi.org/10.1002/cphc.201800935</a>
  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.” <i>ChemPhysChem</i>.
    Wiley, 2019. <a href="https://doi.org/10.1002/cphc.201800935">https://doi.org/10.1002/cphc.201800935</a>.
  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,” <i>ChemPhysChem</i>, 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.” <i>ChemPhysChem</i>,
    vol. 20, no. 2, Wiley, 2019, pp. 276–84, doi:<a href="https://doi.org/10.1002/cphc.201800935">10.1002/cphc.201800935</a>.
  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.
    <i>ChemPhysChem</i>. 2019;20(2):311-317. doi:<a href="https://doi.org/10.1002/cphc.201800779">10.1002/cphc.201800779</a>
  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. <i>ChemPhysChem</i>.
    Wiley. <a href="https://doi.org/10.1002/cphc.201800779">https://doi.org/10.1002/cphc.201800779</a>
  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.” <i>ChemPhysChem</i>. Wiley, 2019. <a href="https://doi.org/10.1002/cphc.201800779">https://doi.org/10.1002/cphc.201800779</a>.
  ieee: M. D. Shannon <i>et al.</i>, “Conformational dynamics in the core of human
    Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” <i>ChemPhysChem</i>,
    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.” <i>ChemPhysChem</i>,
    vol. 20, no. 2, Wiley, 2019, pp. 311–17, doi:<a href="https://doi.org/10.1002/cphc.201800779">10.1002/cphc.201800779</a>.
  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. <i>Journal of the American Chemical Society</i>.
    2019;141(2):858-869. doi:<a href="https://doi.org/10.1021/jacs.8b09258">10.1021/jacs.8b09258</a>
  apa: Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., &#38; Linser,
    R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins
    using complementary 15N and 1H relaxation dispersion techniques. <i>Journal of
    the American Chemical Society</i>. American Chemical Society. <a href="https://doi.org/10.1021/jacs.8b09258">https://doi.org/10.1021/jacs.8b09258</a>
  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.”
    <i>Journal of the American Chemical Society</i>. American Chemical Society, 2019.
    <a href="https://doi.org/10.1021/jacs.8b09258">https://doi.org/10.1021/jacs.8b09258</a>.
  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,” <i>Journal of the
    American Chemical Society</i>, 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.”
    <i>Journal of the American Chemical Society</i>, vol. 141, no. 2, American Chemical
    Society, 2019, pp. 858–69, doi:<a href="https://doi.org/10.1021/jacs.8b09258">10.1021/jacs.8b09258</a>.
  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. <i>Communications in Mathematical
    Physics</i>. 2019;374(3):1531-1575. doi:<a href="https://doi.org/10.1007/s00220-019-03448-x">10.1007/s00220-019-03448-x</a>
  apa: Bálint, P., De Simoi, J., Kaloshin, V., &#38; Leguil, M. (2019). Marked length
    spectrum, homoclinic orbits and the geometry of open dispersing billiards. <i>Communications
    in Mathematical Physics</i>. Springer Nature. <a href="https://doi.org/10.1007/s00220-019-03448-x">https://doi.org/10.1007/s00220-019-03448-x</a>
  chicago: Bálint, Péter, Jacopo De Simoi, Vadim Kaloshin, and Martin Leguil. “Marked
    Length Spectrum, Homoclinic Orbits and the Geometry of Open Dispersing Billiards.”
    <i>Communications in Mathematical Physics</i>. Springer Nature, 2019. <a href="https://doi.org/10.1007/s00220-019-03448-x">https://doi.org/10.1007/s00220-019-03448-x</a>.
  ieee: P. Bálint, J. De Simoi, V. Kaloshin, and M. Leguil, “Marked length spectrum,
    homoclinic orbits and the geometry of open dispersing billiards,” <i>Communications
    in Mathematical Physics</i>, 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.” <i>Communications in Mathematical Physics</i>,
    vol. 374, no. 3, Springer Nature, 2019, pp. 1531–75, doi:<a href="https://doi.org/10.1007/s00220-019-03448-x">10.1007/s00220-019-03448-x</a>.
  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'
...
