[{"ipn":"WO2019158209 (A1)","year":"2019","main_file_link":[{"url":"https://patents.google.com/patent/WO2019158209A1","open_access":"1"}],"day":"22","status":"public","date_created":"2020-08-27T11:24:44Z","oa":1,"type":"patent","_id":"8313","author":[{"last_name":"Ford","first_name":"Bryan","full_name":"Ford, Bryan"},{"full_name":"Gasser, Linus","first_name":"Linus","last_name":"Gasser"},{"id":"f5983044-d7ef-11ea-ac6d-fd1430a26d30","full_name":"Kokoris Kogias, Eleftherios","first_name":"Eleftherios","last_name":"Kokoris Kogias"},{"full_name":"Janovic, Philipp","first_name":"Philipp","last_name":"Janovic"}],"applicant":["École Polytechnique Fédérale De Lausanne "],"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","ipc":"G06F21/62 ; H04L9/08 ; H04L9/32","date_updated":"2022-01-05T14:00:32Z","extern":"1","oa_version":"Published Version","citation":{"ieee":"B. Ford, L. Gasser, E. Kokoris Kogias, and P. Janovic, “Methods and systems for secure data exchange.” 2019.","chicago":"Ford, Bryan, Linus Gasser, Eleftherios Kokoris Kogias, and Philipp 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.","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.","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_published":"2019-08-22T00:00:00Z","publication_date":"2019-08-22","article_processing_charge":"No","title":"Methods and systems for secure data exchange","abstract":[{"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).","lang":"eng"}],"month":"08"},{"article_number":"1905.11360","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."}],"publication_status":"submitted","month":"05","article_processing_charge":"No","title":"Brick: Asynchronous payment channels","language":[{"iso":"eng"}],"date_published":"2019-05-27T00:00:00Z","oa_version":"Preprint","citation":{"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.).","apa":"Avarikioti, G., Kokoris Kogias, E., Wattenhofer, R., &#38; Zindros, D. (n.d.). Brick: Asynchronous payment channels. <i>arXiv</i>.","ista":"Avarikioti G, Kokoris Kogias E, Wattenhofer R, Zindros D. Brick: Asynchronous payment channels. arXiv, 1905.11360.","ama":"Avarikioti G, Kokoris Kogias E, Wattenhofer R, Zindros 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>. ."},"date_updated":"2021-01-12T08:18:04Z","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"arxiv":["1905.11360"]},"author":[{"last_name":"Avarikioti","first_name":"Georgia","full_name":"Avarikioti, Georgia"},{"full_name":"Kokoris Kogias, Eleftherios","id":"f5983044-d7ef-11ea-ac6d-fd1430a26d30","first_name":"Eleftherios","last_name":"Kokoris Kogias"},{"full_name":"Wattenhofer, Roger","first_name":"Roger","last_name":"Wattenhofer"},{"last_name":"Zindros","first_name":"Dionysis","full_name":"Zindros, Dionysis"}],"publication":"arXiv","arxiv":1,"_id":"8314","type":"preprint","date_created":"2020-08-27T11:36:54Z","oa":1,"day":"27","status":"public","year":"2019","main_file_link":[{"url":"https://arxiv.org/abs/1905.11360","open_access":"1"}]},{"article_number":"1910.10434","publication_status":"submitted","month":"10","abstract":[{"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). ","lang":"eng"}],"title":"Divide and scale: Formalization of distributed ledger sharding protocols","article_processing_charge":"No","language":[{"iso":"eng"}],"date_published":"2019-10-23T00:00:00Z","oa_version":"Preprint","citation":{"ista":"Avarikioti G, Kokoris Kogias E, Wattenhofer R. Divide and scale: Formalization of distributed ledger sharding protocols. arXiv, 1910.10434.","ama":"Avarikioti G, Kokoris Kogias E, Wattenhofer R. 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.","apa":"Avarikioti, G., Kokoris Kogias, E., &#38; Wattenhofer, R. (n.d.). Divide and scale: Formalization of distributed ledger sharding protocols. <i>arXiv</i>.","ieee":"G. Avarikioti, E. Kokoris Kogias, and R. Wattenhofer, “Divide and scale: Formalization of distributed ledger sharding protocols,” <i>arXiv</i>. .","short":"G. Avarikioti, E. Kokoris Kogias, R. Wattenhofer, ArXiv (n.d.).","mla":"Avarikioti, Georgia, et al. “Divide and Scale: Formalization of Distributed Ledger Sharding Protocols.” <i>ArXiv</i>, 1910.10434."},"extern":"1","date_updated":"2021-01-12T08:18:05Z","external_id":{"arxiv":["1910.10434"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Avarikioti, Georgia","first_name":"Georgia","last_name":"Avarikioti"},{"last_name":"Kokoris Kogias","first_name":"Eleftherios","id":"f5983044-d7ef-11ea-ac6d-fd1430a26d30","full_name":"Kokoris Kogias, Eleftherios"},{"full_name":"Wattenhofer, Roger","first_name":"Roger","last_name":"Wattenhofer"}],"publication":"arXiv","arxiv":1,"_id":"8315","type":"preprint","oa":1,"date_created":"2020-08-27T11:37:43Z","status":"public","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1910.10434"}],"year":"2019","day":"23"},{"oa_version":"Published Version","quality_controlled":"1","author":[{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"full_name":"Estrozi, Leandro F.","first_name":"Leandro F.","last_name":"Estrozi"},{"full_name":"Schwieters, Charles D.","last_name":"Schwieters","first_name":"Charles D."},{"first_name":"Gregory","last_name":"Effantin","full_name":"Effantin, Gregory"},{"full_name":"Macek, Pavel","last_name":"Macek","first_name":"Pavel"},{"full_name":"Sounier, Remy","last_name":"Sounier","first_name":"Remy"},{"full_name":"Sivertsen, Astrid C.","last_name":"Sivertsen","first_name":"Astrid C."},{"first_name":"Elena","last_name":"Schmidt","full_name":"Schmidt, Elena"},{"last_name":"Kerfah","first_name":"Rime","full_name":"Kerfah, Rime"},{"last_name":"Mas","first_name":"Guillaume","full_name":"Mas, Guillaume"},{"first_name":"Jacques-Philippe","last_name":"Colletier","full_name":"Colletier, Jacques-Philippe"},{"full_name":"Güntert, Peter","last_name":"Güntert","first_name":"Peter"},{"first_name":"Adrien","last_name":"Favier","full_name":"Favier, Adrien"},{"first_name":"Guy","last_name":"Schoehn","full_name":"Schoehn, Guy"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"},{"full_name":"Boisbouvier, Jerome","last_name":"Boisbouvier","first_name":"Jerome"}],"article_number":"2697","month":"06","volume":10,"article_processing_charge":"No","language":[{"iso":"eng"}],"article_type":"original","type":"journal_article","_id":"8405","date_created":"2020-09-17T10:28:25Z","publication_identifier":{"issn":["2041-1723"]},"status":"public","main_file_link":[{"url":"https://doi.org/10.1038/s41467-019-10490-9","open_access":"1"}],"citation":{"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.","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>","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>.","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>","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)."},"extern":"1","date_updated":"2021-01-12T08:19:03Z","external_id":{"pmid":["31217444"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","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."}],"title":"Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex","pmid":1,"date_published":"2019-06-19T00:00:00Z","publisher":"Springer Nature","oa":1,"doi":"10.1038/s41467-019-10490-9","day":"19","year":"2019","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"publication":"Nature Communications","intvolume":"        10"},{"article_type":"original","type":"journal_article","_id":"8406","date_created":"2020-09-17T10:28:36Z","publication_identifier":{"issn":["2375-2548"]},"main_file_link":[{"url":" https://doi.org/10.1126/sciadv.aaw3818","open_access":"1"}],"status":"public","article_number":"eaaw3818","issue":"9","month":"09","volume":5,"article_processing_charge":"No","language":[{"iso":"eng"}],"oa_version":"Published Version","quality_controlled":"1","author":[{"full_name":"Felix, Jan","last_name":"Felix","first_name":"Jan"},{"full_name":"Weinhäupl, Katharina","first_name":"Katharina","last_name":"Weinhäupl"},{"full_name":"Chipot, Christophe","first_name":"Christophe","last_name":"Chipot"},{"full_name":"Dehez, François","last_name":"Dehez","first_name":"François"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"full_name":"Gauto, Diego F.","last_name":"Gauto","first_name":"Diego F."},{"last_name":"Morlot","first_name":"Cecile","full_name":"Morlot, Cecile"},{"full_name":"Abian, Olga","first_name":"Olga","last_name":"Abian"},{"full_name":"Gutsche, Irina","last_name":"Gutsche","first_name":"Irina"},{"last_name":"Velazquez-Campoy","first_name":"Adrian","full_name":"Velazquez-Campoy, Adrian"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"},{"first_name":"Hugo","last_name":"Fraga","full_name":"Fraga, Hugo"}],"publication":"Science Advances","intvolume":"         5","oa":1,"day":"04","year":"2019","doi":"10.1126/sciadv.aaw3818","publication_status":"published","abstract":[{"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.","lang":"eng"}],"title":"Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors","publisher":"American Association for the Advancement of Science","date_published":"2019-09-04T00:00:00Z","citation":{"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.","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>","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.","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>","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>.","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)."},"extern":"1","date_updated":"2021-01-12T08:19:03Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"citation":{"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.","ista":"Schanda P. 2019. Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. 306, 180–186.","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>","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>.","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>","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."},"oa_version":"Submitted Version","quality_controlled":"1","extern":"1","date_updated":"2021-01-12T08:19:04Z","external_id":{"pmid":["31350165"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"}],"publication_status":"published","month":"09","volume":306,"title":"Relaxing with liquids and solids – A perspective on biomolecular dynamics","article_processing_charge":"No","pmid":1,"date_published":"2019-09-01T00:00:00Z","language":[{"iso":"eng"}],"publisher":"Elsevier","article_type":"original","type":"journal_article","_id":"8407","date_created":"2020-09-17T10:28:47Z","year":"2019","page":"180-186","day":"01","status":"public","publication_identifier":{"issn":["1090-7807"]},"doi":"10.1016/j.jmr.2019.07.025","keyword":["Nuclear and High Energy Physics","Biophysics","Biochemistry","Condensed Matter Physics"],"publication":"Journal of Magnetic Resonance","intvolume":"       306"},{"status":"public","publication_identifier":{"issn":["0002-7863","1520-5126"]},"date_created":"2020-09-17T10:29:00Z","article_type":"original","type":"journal_article","_id":"8408","author":[{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"last_name":"Macek","first_name":"Pavel","full_name":"Macek, Pavel"},{"full_name":"Barducci, Alessandro","first_name":"Alessandro","last_name":"Barducci"},{"full_name":"Fraga, Hugo","first_name":"Hugo","last_name":"Fraga"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"last_name":"Terauchi","first_name":"Tsutomu","full_name":"Terauchi, Tsutomu"},{"full_name":"Gajan, David","last_name":"Gajan","first_name":"David"},{"first_name":"Yohei","last_name":"Miyanoiri","full_name":"Miyanoiri, Yohei"},{"first_name":"Jerome","last_name":"Boisbouvier","full_name":"Boisbouvier, Jerome"},{"full_name":"Lichtenecker, Roman","first_name":"Roman","last_name":"Lichtenecker"},{"full_name":"Kainosho, Masatsune","last_name":"Kainosho","first_name":"Masatsune"},{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"}],"quality_controlled":"1","oa_version":"Submitted Version","language":[{"iso":"eng"}],"volume":141,"article_processing_charge":"No","month":"06","issue":"28","day":"14","doi":"10.1021/jacs.9b04219","page":"11183-11195","year":"2019","intvolume":"       141","publication":"Journal of the American Chemical Society","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"external_id":{"pmid":["31199882"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","date_updated":"2021-01-12T08:19:04Z","citation":{"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.","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>.","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.","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>","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.","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>","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>."},"pmid":1,"publisher":"American Chemical Society","date_published":"2019-06-14T00:00:00Z","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","publication_status":"published","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."}]},{"keyword":["Structural Biology"],"publication":"Journal of Structural Biology","intvolume":"       206","page":"66-72","doi":"10.1016/j.jsb.2018.07.009","year":"2019","day":"01","abstract":[{"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.","lang":"eng"}],"publication_status":"published","title":"Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency","date_published":"2019-04-01T00:00:00Z","publisher":"Elsevier","pmid":1,"citation":{"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.","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>.","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>","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.","short":"C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, P. Schanda, Journal of Structural Biology 206 (2019) 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>."},"date_updated":"2021-01-12T08:19:05Z","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["30031884"]},"type":"journal_article","_id":"8409","article_type":"original","date_created":"2020-09-17T10:29:10Z","publication_identifier":{"issn":["1047-8477"]},"status":"public","issue":"1","month":"04","article_processing_charge":"No","volume":206,"language":[{"iso":"eng"}],"oa_version":"Submitted Version","quality_controlled":"1","author":[{"first_name":"Catherine","last_name":"Bougault","full_name":"Bougault, Catherine"},{"full_name":"Ayala, Isabel","last_name":"Ayala","first_name":"Isabel"},{"full_name":"Vollmer, Waldemar","first_name":"Waldemar","last_name":"Vollmer"},{"full_name":"Simorre, Jean-Pierre","last_name":"Simorre","first_name":"Jean-Pierre"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"}]},{"oa":1,"day":"21","doi":"10.1002/cphc.201801100","year":"2019","page":"177-177","publication":"ChemPhysChem","intvolume":"        20","citation":{"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.","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>.","ista":"Schanda P, Chekmenev EY. 2019. NMR for Biological Systems. ChemPhysChem. 20(2), 177–177.","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>","ieee":"P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” <i>ChemPhysChem</i>, vol. 20, no. 2. Wiley, pp. 177–177, 2019."},"extern":"1","date_updated":"2021-01-12T08:19:05Z","external_id":{"pmid":["30556633"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","title":"NMR for Biological Systems","pmid":1,"publisher":"Wiley","date_published":"2019-01-21T00:00:00Z","article_type":"letter_note","_id":"8410","type":"journal_article","date_created":"2020-09-17T10:29:26Z","status":"public","publication_identifier":{"issn":["1439-4235"]},"main_file_link":[{"url":"https://doi.org/10.1002/cphc.201801100","open_access":"1"}],"oa_version":"Published Version","quality_controlled":"1","author":[{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"},{"last_name":"Chekmenev","first_name":"Eduard Y.","full_name":"Chekmenev, Eduard Y."}],"issue":"2","month":"01","volume":20,"article_processing_charge":"No","language":[{"iso":"eng"}]},{"abstract":[{"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.","lang":"eng"}],"publication_status":"published","publisher":"Wiley","date_published":"2019-01-21T00:00:00Z","pmid":1,"title":"Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR","date_updated":"2021-01-12T08:19:06Z","extern":"1","citation":{"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.","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>","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>.","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.","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>","short":"D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem 20 (2019) 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>."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["30444575"]},"keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"intvolume":"        20","publication":"ChemPhysChem","day":"21","doi":"10.1002/cphc.201800935","page":"276-284","year":"2019","month":"01","issue":"2","language":[{"iso":"eng"}],"article_processing_charge":"No","volume":20,"quality_controlled":"1","oa_version":"Submitted Version","author":[{"first_name":"Dominique","last_name":"Marion","full_name":"Marion, Dominique"},{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"full_name":"Giandoreggio-Barranco, Karine","first_name":"Karine","last_name":"Giandoreggio-Barranco"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"}],"date_created":"2020-09-17T10:29:36Z","_id":"8411","type":"journal_article","article_type":"original","status":"public","publication_identifier":{"issn":["1439-4235"]}},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["30276945"]},"citation":{"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.","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>","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.","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>.","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>","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_updated":"2021-01-12T08:19:06Z","extern":"1","title":"Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR","date_published":"2019-01-21T00:00:00Z","publisher":"Wiley","pmid":1,"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."}],"publication_status":"published","year":"2019","page":"311-317","doi":"10.1002/cphc.201800779","day":"21","publication":"ChemPhysChem","intvolume":"        20","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"author":[{"first_name":"Matthew D.","last_name":"Shannon","full_name":"Shannon, Matthew D."},{"full_name":"Theint, Theint","last_name":"Theint","first_name":"Theint"},{"full_name":"Mukhopadhyay, Dwaipayan","last_name":"Mukhopadhyay","first_name":"Dwaipayan"},{"first_name":"Krystyna","last_name":"Surewicz","full_name":"Surewicz, Krystyna"},{"last_name":"Surewicz","first_name":"Witold K.","full_name":"Surewicz, Witold K."},{"last_name":"Marion","first_name":"Dominique","full_name":"Marion, Dominique"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"},{"first_name":"Christopher P.","last_name":"Jaroniec","full_name":"Jaroniec, Christopher P."}],"oa_version":"Submitted Version","quality_controlled":"1","article_processing_charge":"No","volume":20,"language":[{"iso":"eng"}],"issue":"2","month":"01","status":"public","publication_identifier":{"issn":["1439-4235"]},"type":"journal_article","_id":"8412","article_type":"original","date_created":"2020-09-17T10:29:43Z"},{"author":[{"full_name":"Rovó, Petra","last_name":"Rovó","first_name":"Petra"},{"first_name":"Colin A.","last_name":"Smith","full_name":"Smith, Colin A."},{"full_name":"Gauto, Diego","last_name":"Gauto","first_name":"Diego"},{"first_name":"Bert L.","last_name":"de Groot","full_name":"de Groot, Bert L."},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Linser","first_name":"Rasmus","full_name":"Linser, Rasmus"}],"quality_controlled":"1","oa_version":"Submitted Version","language":[{"iso":"eng"}],"volume":141,"article_processing_charge":"No","month":"01","issue":"2","publication_identifier":{"issn":["0002-7863","1520-5126"]},"status":"public","date_created":"2020-09-17T10:29:50Z","article_type":"original","type":"journal_article","_id":"8413","external_id":{"pmid":["30620186"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","date_updated":"2021-01-12T08:19:07Z","citation":{"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.","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>.","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.","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>.","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>","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."},"pmid":1,"date_published":"2019-01-08T00:00:00Z","publisher":"American Chemical Society","title":"Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques","publication_status":"published","abstract":[{"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.","lang":"eng"}],"day":"08","doi":"10.1021/jacs.8b09258","page":"858-869","year":"2019","intvolume":"       141","publication":"Journal of the American Chemical Society","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"]},{"date_created":"2020-09-17T10:41:27Z","article_type":"original","type":"journal_article","_id":"8415","main_file_link":[{"url":"https://arxiv.org/abs/1809.08947","open_access":"1"}],"status":"public","publication_identifier":{"issn":["0010-3616","1432-0916"]},"quality_controlled":"1","oa_version":"Preprint","author":[{"last_name":"Bálint","first_name":"Péter","full_name":"Bálint, Péter"},{"full_name":"De Simoi, Jacopo","last_name":"De Simoi","first_name":"Jacopo"},{"full_name":"Kaloshin, Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","orcid":"0000-0002-6051-2628","last_name":"Kaloshin","first_name":"Vadim"},{"first_name":"Martin","last_name":"Leguil","full_name":"Leguil, Martin"}],"month":"05","issue":"3","language":[{"iso":"eng"}],"volume":374,"article_processing_charge":"No","oa":1,"doi":"10.1007/s00220-019-03448-x","page":"1531-1575","year":"2019","day":"09","keyword":["Mathematical Physics","Statistical and Nonlinear Physics"],"arxiv":1,"intvolume":"       374","publication":"Communications in Mathematical Physics","extern":"1","date_updated":"2021-01-12T08:19:08Z","citation":{"short":"P. Bálint, J. De Simoi, V. Kaloshin, M. Leguil, Communications in Mathematical Physics 374 (2019) 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>.","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>.","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.","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>","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."},"external_id":{"arxiv":["1809.08947"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","abstract":[{"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.","lang":"eng"}],"date_published":"2019-05-09T00:00:00Z","publisher":"Springer Nature","title":"Marked length spectrum, homoclinic orbits and the geometry of open dispersing billiards"},{"publication":"Moscow Mathematical Journal","arxiv":1,"intvolume":"        19","year":"2019","day":"01","page":"307-327","doi":"10.17323/1609-4514-2019-19-2-307-327","oa":1,"title":"On the finite dimensionality of integrable deformations of strictly convex integrable billiard tables","publisher":"American Mathematical Society","date_published":"2019-04-01T00:00:00Z","publication_status":"published","abstract":[{"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.","lang":"eng"}],"external_id":{"arxiv":["1809.09341"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"short":"G. Huang, V. Kaloshin, Moscow Mathematical Journal 19 (2019) 307–327.","mla":"Huang, Guan, and Vadim Kaloshin. “On the Finite Dimensionality of Integrable Deformations of Strictly Convex Integrable Billiard Tables.” <i>Moscow Mathematical Journal</i>, vol. 19, no. 2, American Mathematical Society, 2019, pp. 307–27, doi:<a href=\"https://doi.org/10.17323/1609-4514-2019-19-2-307-327\">10.17323/1609-4514-2019-19-2-307-327</a>.","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.","chicago":"Huang, Guan, and Vadim Kaloshin. “On the Finite Dimensionality of Integrable Deformations of Strictly Convex Integrable Billiard Tables.” <i>Moscow Mathematical Journal</i>. American Mathematical Society, 2019. <a href=\"https://doi.org/10.17323/1609-4514-2019-19-2-307-327\">https://doi.org/10.17323/1609-4514-2019-19-2-307-327</a>.","ama":"Huang G, Kaloshin V. On the finite dimensionality of integrable deformations of strictly convex integrable billiard tables. <i>Moscow Mathematical Journal</i>. 2019;19(2):307-327. doi:<a href=\"https://doi.org/10.17323/1609-4514-2019-19-2-307-327\">10.17323/1609-4514-2019-19-2-307-327</a>","apa":"Huang, G., &#38; Kaloshin, V. (2019). On the finite dimensionality of integrable deformations of strictly convex integrable billiard tables. <i>Moscow Mathematical Journal</i>. American Mathematical Society. <a href=\"https://doi.org/10.17323/1609-4514-2019-19-2-307-327\">https://doi.org/10.17323/1609-4514-2019-19-2-307-327</a>","ieee":"G. Huang and V. Kaloshin, “On the finite dimensionality of integrable deformations of strictly convex integrable billiard tables,” <i>Moscow Mathematical Journal</i>, vol. 19, no. 2. American Mathematical Society, pp. 307–327, 2019."},"extern":"1","date_updated":"2021-01-12T08:19:08Z","publication_identifier":{"issn":["1609-4514"]},"status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1809.09341","open_access":"1"}],"article_type":"original","type":"journal_article","_id":"8416","date_created":"2020-09-17T10:41:36Z","volume":19,"article_processing_charge":"No","language":[{"iso":"eng"}],"issue":"2","month":"04","author":[{"first_name":"Guan","last_name":"Huang","full_name":"Huang, Guan"},{"full_name":"Kaloshin, Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","orcid":"0000-0002-6051-2628","first_name":"Vadim","last_name":"Kaloshin"}],"oa_version":"Preprint","quality_controlled":"1"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:09Z","extern":"1","citation":{"short":"M. Guardia, V. Kaloshin, J. Zhang, Archive for Rational Mechanics and Analysis 233 (2019) 799–836.","mla":"Guardia, Marcel, et al. “Asymptotic Density of Collision Orbits in the Restricted Circular Planar 3 Body Problem.” <i>Archive for Rational Mechanics and Analysis</i>, vol. 233, no. 2, Springer Nature, 2019, pp. 799–836, doi:<a href=\"https://doi.org/10.1007/s00205-019-01368-7\">10.1007/s00205-019-01368-7</a>.","ama":"Guardia M, Kaloshin V, Zhang J. Asymptotic density of collision orbits in the Restricted Circular Planar 3 Body Problem. <i>Archive for Rational Mechanics and Analysis</i>. 2019;233(2):799-836. doi:<a href=\"https://doi.org/10.1007/s00205-019-01368-7\">10.1007/s00205-019-01368-7</a>","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.","chicago":"Guardia, Marcel, Vadim Kaloshin, and Jianlu Zhang. “Asymptotic Density of Collision Orbits in the Restricted Circular Planar 3 Body Problem.” <i>Archive for Rational Mechanics and Analysis</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1007/s00205-019-01368-7\">https://doi.org/10.1007/s00205-019-01368-7</a>.","apa":"Guardia, M., Kaloshin, V., &#38; Zhang, J. (2019). Asymptotic density of collision orbits in the Restricted Circular Planar 3 Body Problem. <i>Archive for Rational Mechanics and Analysis</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00205-019-01368-7\">https://doi.org/10.1007/s00205-019-01368-7</a>","ieee":"M. Guardia, V. Kaloshin, and J. Zhang, “Asymptotic density of collision orbits in the Restricted Circular Planar 3 Body Problem,” <i>Archive for Rational Mechanics and Analysis</i>, vol. 233, no. 2. Springer Nature, pp. 799–836, 2019."},"date_published":"2019-03-12T00:00:00Z","publisher":"Springer Nature","title":"Asymptotic density of collision orbits in the Restricted Circular Planar 3 Body Problem","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."}],"publication_status":"published","day":"12","doi":"10.1007/s00205-019-01368-7","year":"2019","page":"799-836","oa":1,"intvolume":"       233","publication":"Archive for Rational Mechanics and Analysis","keyword":["Mechanical Engineering","Mathematics (miscellaneous)","Analysis"],"author":[{"full_name":"Guardia, Marcel","last_name":"Guardia","first_name":"Marcel"},{"last_name":"Kaloshin","first_name":"Vadim","orcid":"0000-0002-6051-2628","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","full_name":"Kaloshin, Vadim"},{"full_name":"Zhang, Jianlu","first_name":"Jianlu","last_name":"Zhang"}],"quality_controlled":"1","oa_version":"Published Version","language":[{"iso":"eng"}],"article_processing_charge":"No","volume":233,"month":"03","issue":"2","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1007/s00205-019-01368-7"}],"status":"public","publication_identifier":{"issn":["0003-9527","1432-0673"]},"date_created":"2020-09-17T10:41:51Z","type":"journal_article","_id":"8418","article_type":"original"},{"oa":1,"date_created":"2020-09-26T14:23:54Z","_id":"8570","type":"conference","year":"2019","day":"25","doi":"10.29007/bj1w","status":"public","page":"14-40","main_file_link":[{"url":"https://easychair.org/publications/open/1gbP","open_access":"1"}],"publication_identifier":{"eissn":["23987340"]},"intvolume":"        61","conference":{"name":"ARCH: International Workshop on Applied Verification on Continuous and Hybrid Systems","location":"Montreal, Canada","start_date":"2019-04-15","end_date":"2019-04-15"},"publication":"EPiC Series in Computing","date_updated":"2021-01-12T08:20:05Z","quality_controlled":"1","department":[{"_id":"ToHe"}],"citation":{"ieee":"M. Althoff <i>et al.</i>, “ARCH-COMP19 Category Report: Continuous and hybrid systems with linear continuous dynamics,” in <i>EPiC Series in Computing</i>, Montreal, Canada, 2019, vol. 61, pp. 14–40.","ama":"Althoff M, Bak S, Forets M, et al. ARCH-COMP19 Category Report: Continuous and hybrid systems with linear continuous dynamics. In: <i>EPiC Series in Computing</i>. Vol 61. EasyChair; 2019:14-40. doi:<a href=\"https://doi.org/10.29007/bj1w\">10.29007/bj1w</a>","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 <i>EPiC Series in Computing</i>, 61:14–40. EasyChair, 2019. <a href=\"https://doi.org/10.29007/bj1w\">https://doi.org/10.29007/bj1w</a>.","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.","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 <i>EPiC Series in Computing</i> (Vol. 61, pp. 14–40). Montreal, Canada: EasyChair. <a href=\"https://doi.org/10.29007/bj1w\">https://doi.org/10.29007/bj1w</a>","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.","mla":"Althoff, Matthias, et al. “ARCH-COMP19 Category Report: Continuous and Hybrid Systems with Linear Continuous Dynamics.” <i>EPiC Series in Computing</i>, vol. 61, EasyChair, 2019, pp. 14–40, doi:<a href=\"https://doi.org/10.29007/bj1w\">10.29007/bj1w</a>."},"oa_version":"Published Version","author":[{"first_name":"Matthias","last_name":"Althoff","full_name":"Althoff, Matthias"},{"full_name":"Bak, Stanley","first_name":"Stanley","last_name":"Bak"},{"full_name":"Forets, Marcelo","first_name":"Marcelo","last_name":"Forets"},{"full_name":"Frehse, Goran","last_name":"Frehse","first_name":"Goran"},{"last_name":"Kochdumper","first_name":"Niklas","full_name":"Kochdumper, Niklas"},{"full_name":"Ray, Rajarshi","first_name":"Rajarshi","last_name":"Ray"},{"full_name":"Schilling, Christian","id":"3A2F4DCE-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-3658-1065","first_name":"Christian","last_name":"Schilling"},{"last_name":"Schupp","first_name":"Stefan","full_name":"Schupp, Stefan"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"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.</jats:p>","lang":"eng"}],"month":"05","publication_status":"published","date_published":"2019-05-25T00:00:00Z","publisher":"EasyChair","language":[{"iso":"eng"}],"article_processing_charge":"No","volume":61,"title":"ARCH-COMP19 Category Report: Continuous and hybrid systems with linear continuous dynamics"},{"author":[{"full_name":"Chierchia, Luigi","first_name":"Luigi","last_name":"Chierchia"},{"id":"52DF3E68-AEFA-11EA-95A4-124A3DDC885E","full_name":"Koudjinan, Edmond","last_name":"Koudjinan","first_name":"Edmond","orcid":"0000-0003-2640-4049"}],"quality_controlled":"1","oa_version":"Preprint","language":[{"iso":"eng"}],"article_processing_charge":"No","volume":24,"month":"12","status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1908.02523","open_access":"1"}],"date_created":"2020-10-21T15:25:45Z","type":"journal_article","_id":"8693","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"arxiv":["1908.02523"]},"date_updated":"2021-01-12T08:20:34Z","extern":"1","citation":{"ieee":"L. Chierchia and E. Koudjinan, “V. I. Arnold’s ‘pointwise’ KAM theorem,” <i>Regular and Chaotic Dynamics</i>, vol. 24. Springer, pp. 583–606, 2019.","apa":"Chierchia, L., &#38; Koudjinan, E. (2019). V. I. Arnold’s “pointwise” KAM theorem. <i>Regular and Chaotic Dynamics</i>. Springer. <a href=\"https://doi.org/10.1134/S1560354719060017\">https://doi.org/10.1134/S1560354719060017</a>","ista":"Chierchia L, Koudjinan E. 2019. V. I. Arnold’s “pointwise” KAM theorem. Regular and Chaotic Dynamics. 24, 583–606.","ama":"Chierchia L, Koudjinan E. V. I. Arnold’s “pointwise” KAM theorem. <i>Regular and Chaotic Dynamics</i>. 2019;24:583–606. doi:<a href=\"https://doi.org/10.1134/S1560354719060017\">10.1134/S1560354719060017</a>","chicago":"Chierchia, Luigi, and Edmond Koudjinan. “V. I. Arnold’s ‘Pointwise’ KAM Theorem.” <i>Regular and Chaotic Dynamics</i>. Springer, 2019. <a href=\"https://doi.org/10.1134/S1560354719060017\">https://doi.org/10.1134/S1560354719060017</a>.","short":"L. Chierchia, E. Koudjinan, Regular and Chaotic Dynamics 24 (2019) 583–606.","mla":"Chierchia, Luigi, and Edmond Koudjinan. “V. I. Arnold’s ‘Pointwise’ KAM Theorem.” <i>Regular and Chaotic Dynamics</i>, vol. 24, Springer, 2019, pp. 583–606, doi:<a href=\"https://doi.org/10.1134/S1560354719060017\">10.1134/S1560354719060017</a>."},"date_published":"2019-12-10T00:00:00Z","publisher":"Springer","title":"V. I. Arnold’s “pointwise” KAM theorem","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."}],"publication_status":"published","doi":"10.1134/S1560354719060017","year":"2019","page":"583–606","day":"10","oa":1,"intvolume":"        24","arxiv":1,"publication":"Regular and Chaotic Dynamics"},{"status":"public","date_created":"2018-12-11T11:44:59Z","type":"journal_article","_id":"170","author":[{"last_name":"Browning","first_name":"Timothy D","orcid":"0000-0002-8314-0177","id":"35827D50-F248-11E8-B48F-1D18A9856A87","full_name":"Browning, Timothy D"},{"full_name":"Sofos, Efthymios","last_name":"Sofos","first_name":"Efthymios"}],"quality_controlled":"1","oa_version":"Published Version","language":[{"iso":"eng"}],"volume":373,"month":"04","has_accepted_license":"1","file":[{"relation":"main_file","checksum":"4061dc2fe99bee25d9adf2d2018cf608","file_id":"6479","creator":"dernst","access_level":"open_access","file_size":712847,"content_type":"application/pdf","date_created":"2019-05-23T07:53:27Z","date_updated":"2020-07-14T12:45:12Z","file_name":"2019_MathAnnalen_Browning.pdf"}],"issue":"3-4","doi":"10.1007/s00208-018-1716-6","page":"977-1016","year":"2019","day":"01","oa":1,"arxiv":1,"intvolume":"       373","publication":"Mathematische Annalen","external_id":{"arxiv":["1609.09057"]},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","date_updated":"2021-01-12T06:52:37Z","citation":{"mla":"Browning, Timothy D., and Efthymios Sofos. “Counting Rational Points on Quartic Del Pezzo Surfaces with a Rational Conic.” <i>Mathematische Annalen</i>, vol. 373, no. 3–4, Springer Nature, 2019, pp. 977–1016, doi:<a href=\"https://doi.org/10.1007/s00208-018-1716-6\">10.1007/s00208-018-1716-6</a>.","short":"T.D. Browning, E. Sofos, Mathematische Annalen 373 (2019) 977–1016.","ieee":"T. D. Browning and E. Sofos, “Counting rational points on quartic del Pezzo surfaces with a rational conic,” <i>Mathematische Annalen</i>, 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.","chicago":"Browning, Timothy D, and Efthymios Sofos. “Counting Rational Points on Quartic Del Pezzo Surfaces with a Rational Conic.” <i>Mathematische Annalen</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1007/s00208-018-1716-6\">https://doi.org/10.1007/s00208-018-1716-6</a>.","ama":"Browning TD, Sofos E. Counting rational points on quartic del Pezzo surfaces with a rational conic. <i>Mathematische Annalen</i>. 2019;373(3-4):977-1016. doi:<a href=\"https://doi.org/10.1007/s00208-018-1716-6\">10.1007/s00208-018-1716-6</a>","apa":"Browning, T. D., &#38; Sofos, E. (2019). Counting rational points on quartic del Pezzo surfaces with a rational conic. <i>Mathematische Annalen</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00208-018-1716-6\">https://doi.org/10.1007/s00208-018-1716-6</a>"},"publisher":"Springer Nature","file_date_updated":"2020-07-14T12:45:12Z","date_published":"2019-04-01T00:00:00Z","title":"Counting rational points on quartic del Pezzo surfaces with a rational conic","publication_status":"published","abstract":[{"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 .","lang":"eng"}],"ddc":["510"]},{"language":[{"iso":"eng"}],"volume":371,"article_processing_charge":"No","month":"04","issue":"8","author":[{"orcid":"0000-0002-8314-0177","last_name":"Browning","first_name":"Timothy D","full_name":"Browning, Timothy D","id":"35827D50-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Loughran, Daniel","last_name":"Loughran","first_name":"Daniel"}],"quality_controlled":"1","oa_version":"Preprint","main_file_link":[{"url":"https://arxiv.org/abs/1705.01999","open_access":"1"}],"status":"public","publication_identifier":{"eissn":["10886850"],"issn":["00029947"]},"date_created":"2018-12-11T11:45:01Z","type":"journal_article","_id":"175","publisher":"American Mathematical Society","date_published":"2019-04-15T00:00:00Z","title":"Sieving rational points on varieties","publication_status":"published","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."}],"isi":1,"external_id":{"arxiv":["1705.01999"],"isi":["000464034200019"]},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","department":[{"_id":"TiBr"}],"date_updated":"2023-08-24T14:34:56Z","citation":{"apa":"Browning, T. D., &#38; Loughran, D. (2019). Sieving rational points on varieties. <i>Transactions of the American Mathematical Society</i>. American Mathematical Society. <a href=\"https://doi.org/10.1090/tran/7514\">https://doi.org/10.1090/tran/7514</a>","chicago":"Browning, Timothy D, and Daniel Loughran. “Sieving Rational Points on Varieties.” <i>Transactions of the American Mathematical Society</i>. American Mathematical Society, 2019. <a href=\"https://doi.org/10.1090/tran/7514\">https://doi.org/10.1090/tran/7514</a>.","ista":"Browning TD, Loughran D. 2019. Sieving rational points on varieties. Transactions of the American Mathematical Society. 371(8), 5757–5785.","ama":"Browning TD, Loughran D. Sieving rational points on varieties. <i>Transactions of the American Mathematical Society</i>. 2019;371(8):5757-5785. doi:<a href=\"https://doi.org/10.1090/tran/7514\">10.1090/tran/7514</a>","ieee":"T. D. Browning and D. Loughran, “Sieving rational points on varieties,” <i>Transactions of the American Mathematical Society</i>, vol. 371, no. 8. American Mathematical Society, pp. 5757–5785, 2019.","short":"T.D. Browning, D. Loughran, Transactions of the American Mathematical Society 371 (2019) 5757–5785.","mla":"Browning, Timothy D., and Daniel Loughran. “Sieving Rational Points on Varieties.” <i>Transactions of the American Mathematical Society</i>, vol. 371, no. 8, American Mathematical Society, 2019, pp. 5757–85, doi:<a href=\"https://doi.org/10.1090/tran/7514\">10.1090/tran/7514</a>."},"arxiv":1,"publist_id":"7746","intvolume":"       371","publication":"Transactions of the American Mathematical Society","scopus_import":"1","year":"2019","day":"15","doi":"10.1090/tran/7514","page":"5757-5785","oa":1},{"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1073/pnas.1812015116"}],"status":"public","publication_identifier":{"eissn":["1091-6490"]},"article_type":"original","_id":"196","type":"journal_article","date_created":"2018-12-11T11:45:08Z","volume":116,"article_processing_charge":"No","language":[{"iso":"eng"}],"issue":"8","month":"02","author":[{"id":"29E0800A-F248-11E8-B48F-1D18A9856A87","full_name":"Lang, Moritz","last_name":"Lang","first_name":"Moritz"},{"id":"35084A62-F248-11E8-B48F-1D18A9856A87","full_name":"Shkolnikov, Mikhail","first_name":"Mikhail","last_name":"Shkolnikov","orcid":"0000-0002-4310-178X"}],"oa_version":"Published Version","quality_controlled":"1","publication":"Proceedings of the National Academy of Sciences","arxiv":1,"intvolume":"       116","scopus_import":"1","related_material":{"link":[{"description":"News on IST Webpage","url":"https://ist.ac.at/en/news/famous-sandpile-model-shown-to-move-like-a-traveling-sand-dune/","relation":"press_release"}]},"page":"2821-2830","year":"2019","doi":"10.1073/pnas.1812015116","day":"19","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","oa":1,"title":"Harmonic dynamics of the Abelian sandpile","pmid":1,"date_published":"2019-02-19T00:00:00Z","publisher":"National Academy of Sciences","isi":1,"publication_status":"published","abstract":[{"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. ","lang":"eng"}],"external_id":{"pmid":[" 30728300"],"arxiv":["1806.10823"],"isi":["000459074400013"]},"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","citation":{"ieee":"M. Lang and M. Shkolnikov, “Harmonic dynamics of the Abelian sandpile,” <i>Proceedings of the National Academy of Sciences</i>, vol. 116, no. 8. National Academy of Sciences, pp. 2821–2830, 2019.","ama":"Lang M, Shkolnikov M. Harmonic dynamics of the Abelian sandpile. <i>Proceedings of the National Academy of Sciences</i>. 2019;116(8):2821-2830. doi:<a href=\"https://doi.org/10.1073/pnas.1812015116\">10.1073/pnas.1812015116</a>","ista":"Lang M, Shkolnikov M. 2019. Harmonic dynamics of the Abelian sandpile. Proceedings of the National Academy of Sciences. 116(8), 2821–2830.","chicago":"Lang, Moritz, and Mikhail Shkolnikov. “Harmonic Dynamics of the Abelian Sandpile.” <i>Proceedings of the National Academy of Sciences</i>. National Academy of Sciences, 2019. <a href=\"https://doi.org/10.1073/pnas.1812015116\">https://doi.org/10.1073/pnas.1812015116</a>.","apa":"Lang, M., &#38; Shkolnikov, M. (2019). Harmonic dynamics of the Abelian sandpile. <i>Proceedings of the National Academy of Sciences</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1812015116\">https://doi.org/10.1073/pnas.1812015116</a>","mla":"Lang, Moritz, and Mikhail Shkolnikov. “Harmonic Dynamics of the Abelian Sandpile.” <i>Proceedings of the National Academy of Sciences</i>, vol. 116, no. 8, National Academy of Sciences, 2019, pp. 2821–30, doi:<a href=\"https://doi.org/10.1073/pnas.1812015116\">10.1073/pnas.1812015116</a>.","short":"M. Lang, M. Shkolnikov, Proceedings of the National Academy of Sciences 116 (2019) 2821–2830."},"department":[{"_id":"CaGu"},{"_id":"GaTk"},{"_id":"TaHa"}],"date_updated":"2023-09-11T14:09:34Z"}]