[{"file_date_updated":"2020-07-14T12:48:12Z","doi":"10.15479/AT:ISTA:th_858","department":[{"_id":"JoCs"}],"date_published":"2017-08-23T00:00:00Z","publication_identifier":{"issn":["2663-337X"]},"status":"public","publisher":"Institute of Science and Technology Austria","degree_awarded":"PhD","citation":{"chicago":"Xu, Haibing. “Reactivation of the Hippocampal Cognitive Map in Goal-Directed Spatial Tasks.” Institute of Science and Technology Austria, 2017. <a href=\"https://doi.org/10.15479/AT:ISTA:th_858\">https://doi.org/10.15479/AT:ISTA:th_858</a>.","apa":"Xu, H. (2017). <i>Reactivation of the hippocampal cognitive map in goal-directed spatial tasks</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:th_858\">https://doi.org/10.15479/AT:ISTA:th_858</a>","ieee":"H. Xu, “Reactivation of the hippocampal cognitive map in goal-directed spatial tasks,” Institute of Science and Technology Austria, 2017.","short":"H. Xu, Reactivation of the Hippocampal Cognitive Map in Goal-Directed Spatial Tasks, Institute of Science and Technology Austria, 2017.","mla":"Xu, Haibing. <i>Reactivation of the Hippocampal Cognitive Map in Goal-Directed Spatial Tasks</i>. Institute of Science and Technology Austria, 2017, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:th_858\">10.15479/AT:ISTA:th_858</a>.","ista":"Xu H. 2017. Reactivation of the hippocampal cognitive map in goal-directed spatial tasks. Institute of Science and Technology Austria.","ama":"Xu H. Reactivation of the hippocampal cognitive map in goal-directed spatial tasks. 2017. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:th_858\">10.15479/AT:ISTA:th_858</a>"},"author":[{"last_name":"Xu","id":"310349D0-F248-11E8-B48F-1D18A9856A87","full_name":"Xu, Haibing","first_name":"Haibing"}],"page":"93","OA_place":"publisher","_id":"837","pubrep_id":"858","oa_version":"Published Version","language":[{"iso":"eng"}],"corr_author":"1","date_created":"2018-12-11T11:48:46Z","day":"23","ddc":["571"],"oa":1,"publication_status":"published","tmp":{"short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"fulldoi":"https://doi.org/10.15479/AT:ISTA:th_858","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","has_accepted_license":"1","title":"Reactivation of the hippocampal cognitive map in goal-directed spatial tasks","related_material":{"record":[{"id":"5828","status":"public","relation":"part_of_dissertation"}]},"abstract":[{"text":"The hippocampus is a key brain region for memory and notably for spatial memory, and is needed for both spatial working and reference memories. Hippocampal place cells selectively discharge in specific locations of the environment to form mnemonic represen tations of space. Several behavioral protocols have been designed to test spatial memory which requires the experimental subject to utilize working memory and reference memory. However, less is known about how these memory traces are presented in the hippo campus, especially considering tasks that require both spatial working and long -term reference memory demand. The aim of my thesis was to elucidate how spatial working memory, reference memory, and the combination of both are represented in the hippocampus. In this thesis, using a radial eight -arm maze, I examined how the combined demand on these memories influenced place cell assemblies while reference memories were partially updated by changing some of the reward- arms. This was contrasted with task varian ts requiring working or reference memories only. Reference memory update led to gradual place field shifts towards the rewards on the switched arms. Cells developed enhanced firing in passes between newly -rewarded arms as compared to those containing an unchanged reward. The working memory task did not show such gradual changes. Place assemblies on occasions replayed trajectories of the maze; at decision points the next arm choice was preferentially replayed in tasks needing reference memory while in the pure working memory task the previously visited arm was replayed. Hence trajectory replay only reflected the decision of the animal in tasks needing reference memory update. At the reward locations, in all three tasks outbound trajectories of the current arm were preferentially replayed, showing the animals’ next path to the center. At reward locations trajectories were replayed preferentially in reverse temporal order. Moreover, in the center reverse replay was seen in the working memory task but in the other tasks forward replay was seen. Hence, the direction of reactivation was determined by the goal locations so that part of the trajectory which was closer to the goal was reactivated later in an HSE while places further away from the goal were reactivated earlier. Altogether my work demonstrated that reference memory update triggers several levels of reorganization of the hippocampal cognitive map which are not seen in simpler working memory demand s. Moreover, hippocampus is likely to be involved in spatial decisions through reactivating planned trajectories when reference memory recall is required for such a decision. ","lang":"eng"}],"license":"https://creativecommons.org/licenses/by/4.0/","year":"2017","publist_id":"6811","month":"08","file":[{"date_updated":"2020-07-14T12:48:12Z","file_name":"2017_Xu_Haibing_Thesis_Source.docx","file_id":"6213","access_level":"closed","file_size":3589490,"date_created":"2019-04-05T08:59:51Z","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","checksum":"f11925fbbce31e495124b6bc4f10573c","creator":"dernst","relation":"source_file"},{"creator":"dernst","relation":"main_file","file_size":11668613,"date_created":"2019-04-05T08:59:51Z","checksum":"ffb10749a537d615fab1ef0937ccb157","content_type":"application/pdf","file_id":"6214","access_level":"open_access","date_updated":"2020-07-14T12:48:12Z","file_name":"2017_Xu_Thesis_IST.pdf"}],"alternative_title":["ISTA Thesis"],"date_updated":"2026-06-18T18:56:25Z","supervisor":[{"last_name":"Csicsvari","id":"3FA14672-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-5193-4036","full_name":"Csicsvari, Jozsef L","first_name":"Jozsef L"}],"acknowledgement":"I am very grateful for the opportunity I have had as a graduate student to explore and incredibly interesting branch of neuroscience, and for the people who made it possible. Firstly, I would like to offer my thanks to my supervisor Professor Jozsef Csicsvari for his great support, guidance and patience offered over the years. The door to his office was always open whenever I had questions. I have learned a lot from him about carefully designing experiments, asking interesting questions and how to integrate results into a broader picture. I also express my gratitude to the remarkable post- doc , Dr. Joseph O’Neill. He is a gre at scientific role model who is always willing to teach , and advice and talk through problems with his full attention. Many thanks to my wonderful “office mates” over the years and their support and encouragement, Alice Avernhe, Philipp Schönenberger, Desiree Dickerson, Karel Blahna, Charlotte Boccara, Igor Gridchyn, Peter Baracskay, Krisztián Kovács, Dámaris Rangel, Karola Käfer and Federico Stella. They were the ones in the lab for the many useful discussions about science and for making the laboratory such a nice and friendly place to work in. A special thank goes to Michael LoBianco and Jago Wallenschus for wonderful technical support. I would also like to thank Professor Peter Jonas and Professor David M Bannerman for being my qualifying exam and thesi s committee members despite their busy schedule. I am also very thankful to IST Austria for their support all throughout my PhD. ","article_processing_charge":"No","type":"dissertation"},{"doi":"10.15479/AT:ISTA:th_828","file_date_updated":"2020-07-14T12:48:12Z","department":[{"_id":"KrPi"}],"date_published":"2017-06-26T00:00:00Z","publication_identifier":{"issn":["2663-337X"]},"publisher":"Institute of Science and Technology Austria","status":"public","author":[{"full_name":"Rybar, Michal","first_name":"Michal","last_name":"Rybar","id":"2B3E3DE8-F248-11E8-B48F-1D18A9856A87"}],"OA_place":"publisher","page":"86","citation":{"apa":"Rybar, M. (2017). <i>(The exact security of) Message authentication codes</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:th_828\">https://doi.org/10.15479/AT:ISTA:th_828</a>","chicago":"Rybar, Michal. “(The Exact Security of) Message Authentication Codes.” Institute of Science and Technology Austria, 2017. <a href=\"https://doi.org/10.15479/AT:ISTA:th_828\">https://doi.org/10.15479/AT:ISTA:th_828</a>.","short":"M. Rybar, (The Exact Security of) Message Authentication Codes, Institute of Science and Technology Austria, 2017.","ieee":"M. Rybar, “(The exact security of) Message authentication codes,” Institute of Science and Technology Austria, 2017.","ista":"Rybar M. 2017. (The exact security of) Message authentication codes. Institute of Science and Technology Austria.","mla":"Rybar, Michal. <i>(The Exact Security of) Message Authentication Codes</i>. Institute of Science and Technology Austria, 2017, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:th_828\">10.15479/AT:ISTA:th_828</a>.","ama":"Rybar M. (The exact security of) Message authentication codes. 2017. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:th_828\">10.15479/AT:ISTA:th_828</a>"},"degree_awarded":"PhD","pubrep_id":"828","corr_author":"1","language":[{"iso":"eng"}],"oa_version":"Published Version","_id":"838","ddc":["000"],"day":"26","date_created":"2018-12-11T11:48:46Z","publication_status":"published","oa":1,"user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","fulldoi":"https://doi.org/10.15479/AT:ISTA:th_828","related_material":{"record":[{"status":"public","relation":"part_of_dissertation","id":"2082"},{"id":"6196","status":"public","relation":"part_of_dissertation"}]},"has_accepted_license":"1","title":"(The exact security of) Message authentication codes","year":"2017","publist_id":"6810","abstract":[{"text":"In this thesis we discuss the exact security of message authentications codes HMAC , NMAC , and PMAC . NMAC is a mode of operation which turns a fixed input-length keyed hash function f into a variable input-length function. A practical single-key variant of NMAC called HMAC is a very popular and widely deployed message authentication code (MAC). PMAC is a block-cipher based mode of operation, which also happens to be the most famous fully parallel MAC. NMAC was introduced by Bellare, Canetti and Krawczyk Crypto’96, who proved it to be a secure pseudorandom function (PRF), and thus also a MAC, under two assumptions. Unfortunately, for many instantiations of HMAC one of them has been found to be wrong. To restore the provable guarantees for NMAC , Bellare [Crypto’06] showed its security without this assumption. PMAC was introduced by Black and Rogaway at Eurocrypt 2002. If instantiated with a pseudorandom permutation over n -bit strings, PMAC constitutes a provably secure variable input-length PRF. For adversaries making q queries, each of length at most ` (in n -bit blocks), and of total length σ ≤ q` , the original paper proves an upper bound on the distinguishing advantage of O ( σ 2 / 2 n ), while the currently best bound is O ( qσ/ 2 n ). In this work we show that this bound is tight by giving an attack with advantage Ω( q 2 `/ 2 n ). In the PMAC construction one initially XORs a mask to every message block, where the mask for the i th block is computed as τ i := γ i · L , where L is a (secret) random value, and γ i is the i -th codeword of the Gray code. Our attack applies more generally to any sequence of γ i ’s which contains a large coset of a subgroup of GF (2 n ). As for NMAC , our first contribution is a simpler and uniform proof: If f is an ε -secure PRF (against q queries) and a δ - non-adaptively secure PRF (against q queries), then NMAC f is an ( ε + `qδ )-secure PRF against q queries of length at most ` blocks each. We also show that this ε + `qδ bound is basically tight by constructing an f for which an attack with advantage `qδ exists. Moreover, we analyze the PRF-security of a modification of NMAC called NI by An and Bellare that avoids the constant rekeying on multi-block messages in NMAC and allows for an information-theoretic analysis. We carry out such an analysis, obtaining a tight `q 2 / 2 c bound for this step, improving over the trivial bound of ` 2 q 2 / 2 c . Finally, we investigate, if the security of PMAC can be further improved by using τ i ’s that are k -wise independent, for k &gt; 1 (the original has k = 1). We observe that the security of PMAC will not increase in general if k = 2, and then prove that the security increases to O ( q 2 / 2 n ), if the k = 4. Due to simple extension attacks, this is the best bound one can hope for, using any distribution on the masks. Whether k = 3 is already sufficient to get this level of security is left as an open problem. Keywords: Message authentication codes, Pseudorandom functions, HMAC, PMAC. ","lang":"eng"}],"file":[{"content_type":"application/pdf","checksum":"ff8639ec4bded6186f44c7bd3ee26804","date_created":"2018-12-12T10:10:13Z","file_size":847400,"relation":"main_file","creator":"system","file_name":"IST-2017-828-v1+3_2017_Rybar_thesis.pdf","date_updated":"2020-07-14T12:48:12Z","access_level":"open_access","file_id":"4799"},{"date_created":"2019-04-05T08:24:11Z","file_size":26054879,"checksum":"3462101745ce8ad199c2d0f75dae4a7e","content_type":"application/zip","creator":"dernst","relation":"source_file","file_name":"2017_Thesis_Rybar_source.zip","date_updated":"2020-07-14T12:48:12Z","access_level":"closed","file_id":"6202"}],"month":"06","alternative_title":["ISTA Thesis"],"date_updated":"2026-04-08T14:18:39Z","article_processing_charge":"No","type":"dissertation"},{"article_processing_charge":"No","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1201/9781315119601","type":"book_chapter","scopus_import":"1","oa_version":"None","language":[{"iso":"eng"}],"_id":"84","date_created":"2018-12-11T11:44:32Z","day":"09","publisher":"Taylor & Francis","status":"public","month":"11","page":"1709 - 1735","author":[{"orcid":"0000-0002-9823-6833","id":"3FB178DA-F248-11E8-B48F-1D18A9856A87","last_name":"Edelsbrunner","first_name":"Herbert","full_name":"Edelsbrunner, Herbert"},{"last_name":"Koehl","first_name":"Patrice","full_name":"Koehl, Patrice"}],"date_updated":"2023-10-16T11:15:22Z","publication":"Handbook of Discrete and Computational Geometry, Third Edition","quality_controlled":"1","citation":{"ama":"Edelsbrunner H, Koehl P. Computational topology for structural molecular biology. In: Toth C, O’Rourke J, Goodman J, eds. <i>Handbook of Discrete and Computational Geometry, Third Edition</i>. Handbook of Discrete and Computational Geometry. Taylor &#38; Francis; 2017:1709-1735. doi:<a href=\"https://doi.org/10.1201/9781315119601\">10.1201/9781315119601</a>","ista":"Edelsbrunner H, Koehl P. 2017.Computational topology for structural molecular biology. In: Handbook of Discrete and Computational Geometry, Third Edition. , 1709–1735.","mla":"Edelsbrunner, Herbert, and Patrice Koehl. “Computational Topology for Structural Molecular Biology.” <i>Handbook of Discrete and Computational Geometry, Third Edition</i>, edited by Csaba Toth et al., Taylor &#38; Francis, 2017, pp. 1709–35, doi:<a href=\"https://doi.org/10.1201/9781315119601\">10.1201/9781315119601</a>.","short":"H. Edelsbrunner, P. Koehl, in:, C. Toth, J. O’Rourke, J. Goodman (Eds.), Handbook of Discrete and Computational Geometry, Third Edition, Taylor &#38; Francis, 2017, pp. 1709–1735.","ieee":"H. Edelsbrunner and P. Koehl, “Computational topology for structural molecular biology,” in <i>Handbook of Discrete and Computational Geometry, Third Edition</i>, C. Toth, J. O’Rourke, and J. Goodman, Eds. Taylor &#38; Francis, 2017, pp. 1709–1735.","apa":"Edelsbrunner, H., &#38; Koehl, P. (2017). Computational topology for structural molecular biology. In C. Toth, J. O’Rourke, &#38; J. Goodman (Eds.), <i>Handbook of Discrete and Computational Geometry, Third Edition</i> (pp. 1709–1735). Taylor &#38; Francis. <a href=\"https://doi.org/10.1201/9781315119601\">https://doi.org/10.1201/9781315119601</a>","chicago":"Edelsbrunner, Herbert, and Patrice Koehl. “Computational Topology for Structural Molecular Biology.” In <i>Handbook of Discrete and Computational Geometry, Third Edition</i>, edited by Csaba Toth, Joseph O’Rourke, and Jacob Goodman, 1709–35. Handbook of Discrete and Computational Geometry. Taylor &#38; Francis, 2017. <a href=\"https://doi.org/10.1201/9781315119601\">https://doi.org/10.1201/9781315119601</a>."},"doi":"10.1201/9781315119601","editor":[{"full_name":"Toth, Csaba","first_name":"Csaba","last_name":"Toth"},{"first_name":"Joseph","full_name":"O'Rourke, Joseph","last_name":"O'Rourke"},{"last_name":"Goodman","full_name":"Goodman, Jacob","first_name":"Jacob"}],"department":[{"_id":"HeEd"}],"title":"Computational topology for structural molecular biology","year":"2017","publist_id":"7970","date_published":"2017-11-09T00:00:00Z","series_title":"Handbook of Discrete and Computational Geometry","publication_identifier":{"eisbn":["9781498711425"]},"abstract":[{"text":"The advent of high-throughput technologies and the concurrent advances in information sciences have led to a data revolution in biology. This revolution is most significant in molecular biology, with an increase in the number and scale of the “omics” projects over the last decade. Genomics projects, for example, have produced impressive advances in our knowledge of the information concealed into genomes, from the many genes that encode for the proteins that are responsible for most if not all cellular functions, to the noncoding regions that are now known to provide regulatory functions. Proteomics initiatives help to decipher the role of post-translation modifications on the protein structures and provide maps of protein-protein interactions, while functional genomics is the field that attempts to make use of the data produced by these projects to understand protein functions. The biggest challenge today is to assimilate the wealth of information provided by these initiatives into a conceptual framework that will help us decipher life. For example, the current views of the relationship between protein structure and function remain fragmented. We know of their sequences, more and more about their structures, we have information on their biological activities, but we have difficulties connecting this dotted line into an informed whole. We lack the experimental and computational tools for directly studying protein structure, function, and dynamics at the molecular and supra-molecular levels. In this chapter, we review some of the current developments in building the computational tools that are needed, focusing on the role that geometry and topology play in these efforts. One of our goals is to raise the general awareness about the importance of geometric methods in elucidating the mysterious foundations of our very existence. Another goal is the broadening of what we consider a geometric algorithm. There is plenty of valuable no-man’s-land between combinatorial and numerical algorithms, and it seems opportune to explore this land with a computational-geometric frame of mind.","lang":"eng"}]},{"publist_id":"6808","year":"2017","abstract":[{"lang":"eng","text":"Heavy holes confined in quantum dots are predicted to be promising candidates for the realization of spin qubits with long coherence times. Here we focus on such heavy-hole states confined in germanium hut wires. By tuning the growth density of the latter we can realize a T-like structure between two neighboring wires. Such a structure allows the realization of a charge sensor, which is electrostatically and tunnel coupled to a quantum dot, with charge-transfer signals as high as 0.3 e. By integrating the T-like structure into a radiofrequency reflectometry setup, single-shot measurements allowing the extraction of hole tunneling times are performed. The extracted tunneling times of less than 10 μs are attributed to the small effective mass of Ge heavy-hole states and pave the way toward projective spin readout measurements."}],"related_material":{"record":[{"id":"7977","relation":"popular_science"},{"id":"7996","relation":"dissertation_contains","status":"public"},{"relation":"dissertation_contains","status":"public","id":"69"}]},"title":"Fast hole tunneling times in germanium hut wires probed by single-shot reflectometry","intvolume":"        17","has_accepted_license":"1","date_updated":"2026-04-08T14:09:47Z","month":"08","file":[{"access_level":"open_access","file_id":"4951","file_name":"IST-2017-865-v1+1_acs.nanolett.7b02627.pdf","date_updated":"2020-07-14T12:48:13Z","creator":"system","relation":"main_file","date_created":"2018-12-12T10:12:33Z","file_size":2449546,"content_type":"application/pdf","checksum":"761371a0129b2aa442424b9561450ece"}],"publication":"Nano Letters","issue":"9","type":"journal_article","article_processing_charge":"No","external_id":{"isi":["000411043500078"]},"publication_identifier":{"issn":["1530-6984"]},"date_published":"2017-08-10T00:00:00Z","department":[{"_id":"GeKa"}],"doi":"10.1021/acs.nanolett.7b02627","file_date_updated":"2020-07-14T12:48:13Z","author":[{"id":"31E9F056-F248-11E8-B48F-1D18A9856A87","last_name":"Vukusic","orcid":"0000-0003-2424-8636","first_name":"Lada","full_name":"Vukusic, Lada"},{"full_name":"Kukucka, Josip","first_name":"Josip","last_name":"Kukucka","id":"3F5D8856-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Watzinger","id":"35DF8E50-F248-11E8-B48F-1D18A9856A87","full_name":"Watzinger, Hannes","first_name":"Hannes"},{"full_name":"Katsaros, Georgios","first_name":"Georgios","last_name":"Katsaros","id":"38DB5788-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-8342-202X"}],"page":"5706 - 5710","citation":{"ama":"Vukušić L, Kukucka J, Watzinger H, Katsaros G. Fast hole tunneling times in germanium hut wires probed by single-shot reflectometry. <i>Nano Letters</i>. 2017;17(9):5706-5710. doi:<a href=\"https://doi.org/10.1021/acs.nanolett.7b02627\">10.1021/acs.nanolett.7b02627</a>","mla":"Vukušić, Lada, et al. “Fast Hole Tunneling Times in Germanium Hut Wires Probed by Single-Shot Reflectometry.” <i>Nano Letters</i>, vol. 17, no. 9, American Chemical Society, 2017, pp. 5706–10, doi:<a href=\"https://doi.org/10.1021/acs.nanolett.7b02627\">10.1021/acs.nanolett.7b02627</a>.","ista":"Vukušić L, Kukucka J, Watzinger H, Katsaros G. 2017. Fast hole tunneling times in germanium hut wires probed by single-shot reflectometry. Nano Letters. 17(9), 5706–5710.","ieee":"L. Vukušić, J. Kukucka, H. Watzinger, and G. Katsaros, “Fast hole tunneling times in germanium hut wires probed by single-shot reflectometry,” <i>Nano Letters</i>, vol. 17, no. 9. American Chemical Society, pp. 5706–5710, 2017.","short":"L. Vukušić, J. Kukucka, H. Watzinger, G. Katsaros, Nano Letters 17 (2017) 5706–5710.","chicago":"Vukušić, Lada, Josip Kukucka, Hannes Watzinger, and Georgios Katsaros. “Fast Hole Tunneling Times in Germanium Hut Wires Probed by Single-Shot Reflectometry.” <i>Nano Letters</i>. American Chemical Society, 2017. <a href=\"https://doi.org/10.1021/acs.nanolett.7b02627\">https://doi.org/10.1021/acs.nanolett.7b02627</a>.","apa":"Vukušić, L., Kukucka, J., Watzinger, H., &#38; Katsaros, G. (2017). Fast hole tunneling times in germanium hut wires probed by single-shot reflectometry. <i>Nano Letters</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.nanolett.7b02627\">https://doi.org/10.1021/acs.nanolett.7b02627</a>"},"isi":1,"quality_controlled":"1","publisher":"American Chemical Society","status":"public","acknowledged_ssus":[{"_id":"M-Shop"}],"ddc":["539"],"ec_funded":1,"date_created":"2018-12-11T11:48:47Z","day":"10","corr_author":"1","language":[{"iso":"eng"}],"oa_version":"Published Version","pubrep_id":"865","scopus_import":"1","_id":"840","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1021/acs.nanolett.7b02627","tmp":{"short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"project":[{"grant_number":"335497","name":"Towards Spin qubits and Majorana fermions in Germanium self assembled hut-wires","_id":"25517E86-B435-11E9-9278-68D0E5697425","call_identifier":"FP7"}],"volume":17,"publication_status":"published","oa":1},{"doi":"10.1215/00127094-2017-0038","article_type":"original","date_published":"2017-12-08T00:00:00Z","external_id":{"arxiv":["1603.08838"]},"publication_identifier":{"issn":["0012-7094"]},"status":"public","publisher":"Duke University Press","quality_controlled":"1","citation":{"apa":"Huang, G., Kaloshin, V., &#38; Sorrentino, A. (2017). On the marked length spectrum of generic strictly convex billiard tables. <i>Duke Mathematical Journal</i>. Duke University Press. <a href=\"https://doi.org/10.1215/00127094-2017-0038\">https://doi.org/10.1215/00127094-2017-0038</a>","chicago":"Huang, Guan, Vadim Kaloshin, and Alfonso Sorrentino. “On the Marked Length Spectrum of Generic Strictly Convex Billiard Tables.” <i>Duke Mathematical Journal</i>. Duke University Press, 2017. <a href=\"https://doi.org/10.1215/00127094-2017-0038\">https://doi.org/10.1215/00127094-2017-0038</a>.","short":"G. Huang, V. Kaloshin, A. Sorrentino, Duke Mathematical Journal 167 (2017) 175–209.","ieee":"G. Huang, V. Kaloshin, and A. Sorrentino, “On the marked length spectrum of generic strictly convex billiard tables,” <i>Duke Mathematical Journal</i>, vol. 167, no. 1. Duke University Press, pp. 175–209, 2017.","ista":"Huang G, Kaloshin V, Sorrentino A. 2017. On the marked length spectrum of generic strictly convex billiard tables. Duke Mathematical Journal. 167(1), 175–209.","mla":"Huang, Guan, et al. “On the Marked Length Spectrum of Generic Strictly Convex Billiard Tables.” <i>Duke Mathematical Journal</i>, vol. 167, no. 1, Duke University Press, 2017, pp. 175–209, doi:<a href=\"https://doi.org/10.1215/00127094-2017-0038\">10.1215/00127094-2017-0038</a>.","ama":"Huang G, Kaloshin V, Sorrentino A. On the marked length spectrum of generic strictly convex billiard tables. <i>Duke Mathematical Journal</i>. 2017;167(1):175-209. doi:<a href=\"https://doi.org/10.1215/00127094-2017-0038\">10.1215/00127094-2017-0038</a>"},"page":"175-209","author":[{"first_name":"Guan","full_name":"Huang, Guan","last_name":"Huang"},{"first_name":"Vadim","full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","last_name":"Kaloshin"},{"last_name":"Sorrentino","first_name":"Alfonso","full_name":"Sorrentino, Alfonso"}],"_id":"8423","language":[{"iso":"eng"}],"oa_version":"Preprint","day":"08","date_created":"2020-09-17T10:42:42Z","publication_status":"published","oa":1,"volume":167,"fulldoi":"https://doi.org/10.1215/00127094-2017-0038","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"On the marked length spectrum of generic strictly convex billiard tables","intvolume":"       167","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1603.08838"}],"abstract":[{"lang":"eng","text":"In this paper we show that for a generic strictly convex domain, one can recover the eigendata corresponding to Aubry–Mather periodic orbits of the induced billiard map from the (maximal) marked length spectrum of the domain."}],"year":"2017","publication":"Duke Mathematical Journal","month":"12","arxiv":1,"date_updated":"2021-01-12T08:19:11Z","issue":"1","article_processing_charge":"No","type":"journal_article","extern":"1"},{"issue":"1","type":"journal_article","extern":"1","article_processing_charge":"No","abstract":[{"text":"We show that any sufficiently (finitely) smooth ℤ₂-symmetric strictly convex domain sufficiently close to a circle is dynamically spectrally rigid; i.e., all deformations among domains in the same class that preserve the length of all periodic orbits of the associated billiard flow must necessarily be isometric deformations. This gives a partial answer to a question of P. Sarnak.","lang":"eng"}],"main_file_link":[{"url":"https://arxiv.org/abs/1606.00230","open_access":"1"}],"year":"2017","intvolume":"       186","title":"Dynamical spectral rigidity among Z2-symmetric strictly convex domains close to a circle","publication":"Annals of Mathematics","month":"07","date_updated":"2021-01-12T08:19:12Z","arxiv":1,"date_created":"2020-09-17T10:46:42Z","day":"01","_id":"8427","language":[{"iso":"eng"}],"oa_version":"Preprint","fulldoi":"https://doi.org/10.4007/annals.2017.186.1.7","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","oa":1,"volume":186,"article_type":"original","date_published":"2017-07-01T00:00:00Z","publication_identifier":{"issn":["0003-486X"]},"external_id":{"arxiv":["1606.00230"]},"doi":"10.4007/annals.2017.186.1.7","quality_controlled":"1","citation":{"short":"J. De Simoi, V. Kaloshin, Q. Wei, Annals of Mathematics 186 (2017) 277–314.","ieee":"J. De Simoi, V. Kaloshin, and Q. Wei, “Dynamical spectral rigidity among Z2-symmetric strictly convex domains close to a circle,” <i>Annals of Mathematics</i>, vol. 186, no. 1. Annals of Mathematics, pp. 277–314, 2017.","apa":"De Simoi, J., Kaloshin, V., &#38; Wei, Q. (2017). Dynamical spectral rigidity among Z2-symmetric strictly convex domains close to a circle. <i>Annals of Mathematics</i>. Annals of Mathematics. <a href=\"https://doi.org/10.4007/annals.2017.186.1.7\">https://doi.org/10.4007/annals.2017.186.1.7</a>","chicago":"De Simoi, Jacopo, Vadim Kaloshin, and Qiaoling Wei. “Dynamical Spectral Rigidity among Z2-Symmetric Strictly Convex Domains Close to a Circle.” <i>Annals of Mathematics</i>. Annals of Mathematics, 2017. <a href=\"https://doi.org/10.4007/annals.2017.186.1.7\">https://doi.org/10.4007/annals.2017.186.1.7</a>.","ama":"De Simoi J, Kaloshin V, Wei Q. Dynamical spectral rigidity among Z2-symmetric strictly convex domains close to a circle. <i>Annals of Mathematics</i>. 2017;186(1):277-314. doi:<a href=\"https://doi.org/10.4007/annals.2017.186.1.7\">10.4007/annals.2017.186.1.7</a>","ista":"De Simoi J, Kaloshin V, Wei Q. 2017. Dynamical spectral rigidity among Z2-symmetric strictly convex domains close to a circle. Annals of Mathematics. 186(1), 277–314.","mla":"De Simoi, Jacopo, et al. “Dynamical Spectral Rigidity among Z2-Symmetric Strictly Convex Domains Close to a Circle.” <i>Annals of Mathematics</i>, vol. 186, no. 1, Annals of Mathematics, 2017, pp. 277–314, doi:<a href=\"https://doi.org/10.4007/annals.2017.186.1.7\">10.4007/annals.2017.186.1.7</a>."},"page":"277-314","author":[{"full_name":"De Simoi, Jacopo","first_name":"Jacopo","last_name":"De Simoi"},{"last_name":"Kaloshin","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","orcid":"0000-0002-6051-2628","full_name":"Kaloshin, Vadim","first_name":"Vadim"},{"first_name":"Qiaoling","full_name":"Wei, Qiaoling","last_name":"Wei"}],"status":"public","publisher":"Annals of Mathematics"},{"issue":"11","extern":"1","type":"journal_article","article_processing_charge":"No","year":"2017","abstract":[{"lang":"eng","text":"Biophysical investigation of membrane proteins generally requires their extraction from native sources using detergents, a step that can lead, possibly irreversibly, to protein denaturation. The propensity of dodecylphosphocholine (DPC), a detergent widely utilized in NMR studies of membrane proteins, to distort their structure has been the subject of much controversy. It has been recently proposed that the binding specificity of the yeast mitochondrial ADP/ATP carrier (yAAC3) toward cardiolipins is preserved in DPC, thereby suggesting that DPC is a suitable environment in which to study membrane proteins. In this communication, we used all-atom molecular dynamics simulations to investigate the specific binding of cardiolipins to yAAC3. Our data demonstrate that the interaction interface observed in a native-like environment differs markedly from that inferred from an NMR investigation in DPC, implying that in this detergent, the protein structure is distorted. We further investigated yAAC3 solubilized in DPC and in the milder dodecylmaltoside with thermal-shift assays. The loss of thermal transition observed in DPC confirms that the protein is no longer properly folded in this environment."}],"intvolume":"       113","title":"Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity","date_updated":"2021-01-12T08:19:18Z","month":"12","publication":"Biophysical Journal","date_created":"2020-09-18T10:05:54Z","day":"05","language":[{"iso":"eng"}],"oa_version":"None","_id":"8444","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1016/j.bpj.2017.09.019","volume":113,"publication_status":"published","publication_identifier":{"issn":["0006-3495"]},"date_published":"2017-12-05T00:00:00Z","article_type":"original","doi":"10.1016/j.bpj.2017.09.019","keyword":["Biophysics"],"author":[{"full_name":"Dehez, François","first_name":"François","last_name":"Dehez"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"King","full_name":"King, Martin S.","first_name":"Martin S."},{"last_name":"Kunji","first_name":"Edmund R.S.","full_name":"Kunji, Edmund R.S."},{"last_name":"Chipot","first_name":"Christophe","full_name":"Chipot, Christophe"}],"page":"2311-2315","citation":{"mla":"Dehez, François, et al. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-Native Affinity.” <i>Biophysical Journal</i>, vol. 113, no. 11, Elsevier, 2017, pp. 2311–15, doi:<a href=\"https://doi.org/10.1016/j.bpj.2017.09.019\">10.1016/j.bpj.2017.09.019</a>.","ista":"Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. 2017. Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical Journal. 113(11), 2311–2315.","ama":"Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. <i>Biophysical Journal</i>. 2017;113(11):2311-2315. doi:<a href=\"https://doi.org/10.1016/j.bpj.2017.09.019\">10.1016/j.bpj.2017.09.019</a>","chicago":"Dehez, François, Paul Schanda, Martin S. King, Edmund R.S. Kunji, and Christophe Chipot. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-Native Affinity.” <i>Biophysical Journal</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.bpj.2017.09.019\">https://doi.org/10.1016/j.bpj.2017.09.019</a>.","apa":"Dehez, F., Schanda, P., King, M. S., Kunji, E. R. S., &#38; Chipot, C. (2017). Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. <i>Biophysical Journal</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.bpj.2017.09.019\">https://doi.org/10.1016/j.bpj.2017.09.019</a>","ieee":"F. Dehez, P. Schanda, M. S. King, E. R. S. Kunji, and C. Chipot, “Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity,” <i>Biophysical Journal</i>, vol. 113, no. 11. Elsevier, pp. 2311–2315, 2017.","short":"F. Dehez, P. Schanda, M.S. King, E.R.S. Kunji, C. Chipot, Biophysical Journal 113 (2017) 2311–2315."},"quality_controlled":"1","publisher":"Elsevier","status":"public"},{"article_number":"145","extern":"1","type":"journal_article","OA_type":"gold","article_processing_charge":"Yes","year":"2017","abstract":[{"lang":"eng","text":"Proteins perform their functions in solution but their structures are most frequently studied inside crystals. Here we probe how the crystal packing alters microsecond dynamics, using solid-state NMR measurements and multi-microsecond MD simulations of different crystal forms of ubiquitin. In particular, near-rotary-resonance relaxation dispersion (NERRD) experiments probe angular backbone motion, while Bloch–McConnell relaxation dispersion data report on fluctuations of the local electronic environment. These experiments and simulations reveal that the packing of the protein can significantly alter the thermodynamics and kinetics of local conformational exchange. Moreover, we report small-amplitude reorientational motion of protein molecules in the crystal lattice with an ~3–5° amplitude on a tens-of-microseconds time scale in one of the crystals, but not in others. An intriguing possibility arises that overall motion is to some extent coupled to local dynamics. Our study highlights the importance of considering the packing when analyzing dynamics of crystalline proteins."}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-017-00165-8"}],"title":"Slow conformational exchange and overall rocking motion in ubiquitin protein crystals","intvolume":"         8","date_updated":"2025-01-22T14:32:38Z","month":"07","publication":"Nature Communications","date_created":"2020-09-18T10:06:01Z","day":"27","language":[{"iso":"eng"}],"oa_version":"Published Version","scopus_import":"1","_id":"8445","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1038/s41467-017-00165-8","volume":8,"publication_status":"published","oa":1,"publication_identifier":{"issn":["2041-1723"]},"date_published":"2017-07-27T00:00:00Z","article_type":"original","doi":"10.1038/s41467-017-00165-8","author":[{"last_name":"Kurauskas","full_name":"Kurauskas, Vilius","first_name":"Vilius"},{"last_name":"Izmailov","first_name":"Sergei A.","full_name":"Izmailov, Sergei A."},{"last_name":"Rogacheva","first_name":"Olga N.","full_name":"Rogacheva, Olga N."},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"last_name":"Woodhouse","first_name":"Joyce","full_name":"Woodhouse, Joyce"},{"last_name":"Shilova","full_name":"Shilova, Anastasya","first_name":"Anastasya"},{"last_name":"Xue","full_name":"Xue, Yi","first_name":"Yi"},{"full_name":"Yuwen, Tairan","first_name":"Tairan","last_name":"Yuwen"},{"last_name":"Coquelle","first_name":"Nicolas","full_name":"Coquelle, Nicolas"},{"full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe","last_name":"Colletier"},{"first_name":"Nikolai R.","full_name":"Skrynnikov, Nikolai R.","last_name":"Skrynnikov"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul"}],"OA_place":"publisher","citation":{"short":"V. Kurauskas, S.A. Izmailov, O.N. Rogacheva, A. Hessel, I. Ayala, J. Woodhouse, A. Shilova, Y. Xue, T. Yuwen, N. Coquelle, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 8 (2017).","ieee":"V. Kurauskas <i>et al.</i>, “Slow conformational exchange and overall rocking motion in ubiquitin protein crystals,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","apa":"Kurauskas, V., Izmailov, S. A., Rogacheva, O. N., Hessel, A., Ayala, I., Woodhouse, J., … Schanda, P. (2017). Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-00165-8\">https://doi.org/10.1038/s41467-017-00165-8</a>","chicago":"Kurauskas, Vilius, Sergei A. Izmailov, Olga N. Rogacheva, Audrey Hessel, Isabel Ayala, Joyce Woodhouse, Anastasya Shilova, et al. “Slow Conformational Exchange and Overall Rocking Motion in Ubiquitin Protein Crystals.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/s41467-017-00165-8\">https://doi.org/10.1038/s41467-017-00165-8</a>.","ama":"Kurauskas V, Izmailov SA, Rogacheva ON, et al. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/s41467-017-00165-8\">10.1038/s41467-017-00165-8</a>","ista":"Kurauskas V, Izmailov SA, Rogacheva ON, Hessel A, Ayala I, Woodhouse J, Shilova A, Xue Y, Yuwen T, Coquelle N, Colletier J-P, Skrynnikov NR, Schanda P. 2017. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. 8, 145.","mla":"Kurauskas, Vilius, et al. “Slow Conformational Exchange and Overall Rocking Motion in Ubiquitin Protein Crystals.” <i>Nature Communications</i>, vol. 8, 145, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/s41467-017-00165-8\">10.1038/s41467-017-00165-8</a>."},"quality_controlled":"1","publisher":"Springer Nature","status":"public"},{"author":[{"full_name":"Fraga, Hugo","first_name":"Hugo","last_name":"Fraga"},{"full_name":"Arnaud, Charles‐Adrien","first_name":"Charles‐Adrien","last_name":"Arnaud"},{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"last_name":"Audin","full_name":"Audin, Maxime","first_name":"Maxime"},{"full_name":"Kurauskas, Vilius","first_name":"Vilius","last_name":"Kurauskas"},{"first_name":"Pavel","full_name":"Macek, Pavel","last_name":"Macek"},{"last_name":"Krichel","first_name":"Carsten","full_name":"Krichel, Carsten"},{"last_name":"Guan","first_name":"Jia‐Ying","full_name":"Guan, Jia‐Ying"},{"last_name":"Boisbouvier","full_name":"Boisbouvier, Jerome","first_name":"Jerome"},{"last_name":"Sprangers","first_name":"Remco","full_name":"Sprangers, Remco"},{"first_name":"Cécile","full_name":"Breyton, Cécile","last_name":"Breyton"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"page":"2697-2703","citation":{"apa":"Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., … Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201700572\">https://doi.org/10.1002/cphc.201700572</a>","chicago":"Fraga, Hugo, Charles‐Adrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” <i>ChemPhysChem</i>. Wiley, 2017. <a href=\"https://doi.org/10.1002/cphc.201700572\">https://doi.org/10.1002/cphc.201700572</a>.","short":"H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel, J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18 (2017) 2697–2703.","ieee":"H. Fraga <i>et al.</i>, “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins,” <i>ChemPhysChem</i>, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.","ista":"Fraga H, Arnaud C, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan J, Boisbouvier J, Sprangers R, Breyton C, Schanda P. 2017. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 18(19), 2697–2703.","mla":"Fraga, Hugo, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” <i>ChemPhysChem</i>, vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:<a href=\"https://doi.org/10.1002/cphc.201700572\">10.1002/cphc.201700572</a>.","ama":"Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. <i>ChemPhysChem</i>. 2017;18(19):2697-2703. doi:<a href=\"https://doi.org/10.1002/cphc.201700572\">10.1002/cphc.201700572</a>"},"quality_controlled":"1","publisher":"Wiley","status":"public","publication_identifier":{"issn":["1439-4235","1439-7641"]},"date_published":"2017-08-09T00:00:00Z","article_type":"original","doi":"10.1002/cphc.201700572","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1002/cphc.201700572","volume":18,"publication_status":"published","day":"09","date_created":"2020-09-18T10:06:09Z","language":[{"iso":"eng"}],"oa_version":"None","_id":"8446","date_updated":"2021-01-12T08:19:19Z","month":"08","publication":"ChemPhysChem","year":"2017","abstract":[{"lang":"eng","text":"Solid‐state NMR spectroscopy can provide insight into protein structure and dynamics at the atomic level without inherent protein size limitations. However, a major hurdle to studying large proteins by solid‐state NMR spectroscopy is related to spectral complexity and resonance overlap, which increase with molecular weight and severely hamper the assignment process. Here the use of two sets of experiments is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH), or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be extended to 5D). The experiments are based on efficient coherence transfers between backbone atoms using INEPT transfers between carbons and cross‐polarization for heteronuclear transfers. The utility of these experiments is exemplified with application to assemblies of deuterated, fully amide‐protonated proteins from approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies from approximately 40 to 55 kHz. These experiments will also be applicable to protonated proteins at higher MAS frequencies. The resonance assignment of a domain within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is compared to NMR assignments of the isolated domain in solution. This comparison reveals contacts of this domain to the core of the polymeric tail tube assembly."}],"intvolume":"        18","title":"Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins","extern":"1","type":"journal_article","article_processing_charge":"No","issue":"19"},{"date_updated":"2021-01-12T08:19:20Z","month":"10","publication":"Solid State Nuclear Magnetic Resonance","title":"Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals","intvolume":"        87","year":"2017","abstract":[{"lang":"eng","text":"Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility."}],"article_processing_charge":"No","extern":"1","type":"journal_article","issue":"10","publisher":"Elsevier","status":"public","page":"86-95","author":[{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"full_name":"Rovó, Petra","first_name":"Petra","last_name":"Rovó"},{"last_name":"Kurauskas","first_name":"Vilius","full_name":"Kurauskas, Vilius"},{"full_name":"Linser, Rasmus","first_name":"Rasmus","last_name":"Linser"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"citation":{"ieee":"D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.","short":"D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.","chicago":"Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser, and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>.","apa":"Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &#38; Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>","ama":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. 2017;87(10):86-95. doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>","mla":"Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10, Elsevier, 2017, pp. 86–95, doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>.","ista":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 87(10), 86–95."},"quality_controlled":"1","doi":"10.1016/j.ssnmr.2017.04.002","keyword":["Nuclear and High Energy Physics","Instrumentation","General Chemistry","Radiation"],"publication_identifier":{"issn":["0926-2040"]},"date_published":"2017-10-01T00:00:00Z","article_type":"original","volume":87,"publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1016/j.ssnmr.2017.04.002","language":[{"iso":"eng"}],"oa_version":"None","_id":"8447","date_created":"2020-09-18T10:06:18Z","day":"01"},{"publication":"Journal of Magnetic Resonance","date_updated":"2021-01-12T08:19:20Z","month":"08","intvolume":"       281","title":"Optimized fast mixing device for real-time NMR applications","abstract":[{"text":"We present an improved fast mixing device based on the rapid mixing of two solutions inside the NMR probe, as originally proposed by Hore and coworkers (J. Am. Chem. Soc. 125 (2003) 12484–12492). Such a device is important for off-equilibrium studies of molecular kinetics by multidimensional real-time NMR spectrsocopy. The novelty of this device is that it allows removing the injector from the NMR detection volume after mixing, and thus provides good magnetic field homogeneity independently of the initial sample volume placed in the NMR probe. The apparatus is simple to build, inexpensive, and can be used without any hardware modification on any type of liquid-state NMR spectrometer. We demonstrate the performance of our fast mixing device in terms of improved magnetic field homogeneity, and show an application to the study of protein folding and the structural characterization of transiently populated folding intermediates.","lang":"eng"}],"year":"2017","article_processing_charge":"No","type":"journal_article","extern":"1","issue":"8","status":"public","publisher":"Elsevier","citation":{"chicago":"Franco, Rémi, Adrien Favier, Paul Schanda, and Bernhard Brutscher. “Optimized Fast Mixing Device for Real-Time NMR Applications.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">https://doi.org/10.1016/j.jmr.2017.05.016</a>.","apa":"Franco, R., Favier, A., Schanda, P., &#38; Brutscher, B. (2017). Optimized fast mixing device for real-time NMR applications. <i>Journal of Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">https://doi.org/10.1016/j.jmr.2017.05.016</a>","ieee":"R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing device for real-time NMR applications,” <i>Journal of Magnetic Resonance</i>, vol. 281, no. 8. Elsevier, pp. 125–129, 2017.","short":"R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 281 (2017) 125–129.","mla":"Franco, Rémi, et al. “Optimized Fast Mixing Device for Real-Time NMR Applications.” <i>Journal of Magnetic Resonance</i>, vol. 281, no. 8, Elsevier, 2017, pp. 125–29, doi:<a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">10.1016/j.jmr.2017.05.016</a>.","ista":"Franco R, Favier A, Schanda P, Brutscher B. 2017. Optimized fast mixing device for real-time NMR applications. Journal of Magnetic Resonance. 281(8), 125–129.","ama":"Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for real-time NMR applications. <i>Journal of Magnetic Resonance</i>. 2017;281(8):125-129. doi:<a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">10.1016/j.jmr.2017.05.016</a>"},"quality_controlled":"1","author":[{"full_name":"Franco, Rémi","first_name":"Rémi","last_name":"Franco"},{"first_name":"Adrien","full_name":"Favier, Adrien","last_name":"Favier"},{"first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"},{"first_name":"Bernhard","full_name":"Brutscher, Bernhard","last_name":"Brutscher"}],"page":"125-129","keyword":["Nuclear and High Energy Physics","Biophysics","Biochemistry","Condensed Matter Physics"],"doi":"10.1016/j.jmr.2017.05.016","article_type":"original","publication_identifier":{"issn":["1090-7807"]},"date_published":"2017-08-01T00:00:00Z","publication_status":"published","volume":281,"fulldoi":"https://doi.org/10.1016/j.jmr.2017.05.016","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8448","language":[{"iso":"eng"}],"oa_version":"None","date_created":"2020-09-18T10:06:27Z","day":"01"},{"publication_status":"published","article_processing_charge":"No","volume":45,"fulldoi":"https://doi.org/10.1093/nar/gkx044","type":"journal_article","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8449","oa_version":"None","language":[{"iso":"eng"}],"day":"20","date_created":"2020-09-18T10:06:34Z","issue":"7","status":"public","publisher":"Oxford University Press","quality_controlled":"1","publication":"Nucleic Acids Research","citation":{"ama":"Rennella E, Sára T, Juen M, et al. RNA binding and chaperone activity of the E.coli cold-shock protein CspA. <i>Nucleic Acids Research</i>. 2017;45(7):4255-4268. doi:<a href=\"https://doi.org/10.1093/nar/gkx044\">10.1093/nar/gkx044</a>","mla":"Rennella, Enrico, et al. “RNA Binding and Chaperone Activity of the E.Coli Cold-Shock Protein CspA.” <i>Nucleic Acids Research</i>, vol. 45, no. 7, Oxford University Press, 2017, pp. 4255–68, doi:<a href=\"https://doi.org/10.1093/nar/gkx044\">10.1093/nar/gkx044</a>.","ista":"Rennella E, Sára T, Juen M, Wunderlich C, Imbert L, Solyom Z, Favier A, Ayala I, Weinhäupl K, Schanda P, Konrat R, Kreutz C, Brutscher B. 2017. RNA binding and chaperone activity of the E.coli cold-shock protein CspA. Nucleic Acids Research. 45(7), 4255–4268.","ieee":"E. Rennella <i>et al.</i>, “RNA binding and chaperone activity of the E.coli cold-shock protein CspA,” <i>Nucleic Acids Research</i>, vol. 45, no. 7. Oxford University Press, pp. 4255–4268, 2017.","short":"E. Rennella, T. Sára, M. Juen, C. Wunderlich, L. Imbert, Z. Solyom, A. Favier, I. Ayala, K. Weinhäupl, P. Schanda, R. Konrat, C. Kreutz, B. Brutscher, Nucleic Acids Research 45 (2017) 4255–4268.","chicago":"Rennella, Enrico, Tomáš Sára, Michael Juen, Christoph Wunderlich, Lionel Imbert, Zsofia Solyom, Adrien Favier, et al. “RNA Binding and Chaperone Activity of the E.Coli Cold-Shock Protein CspA.” <i>Nucleic Acids Research</i>. Oxford University Press, 2017. <a href=\"https://doi.org/10.1093/nar/gkx044\">https://doi.org/10.1093/nar/gkx044</a>.","apa":"Rennella, E., Sára, T., Juen, M., Wunderlich, C., Imbert, L., Solyom, Z., … Brutscher, B. (2017). RNA binding and chaperone activity of the E.coli cold-shock protein CspA. <i>Nucleic Acids Research</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/nar/gkx044\">https://doi.org/10.1093/nar/gkx044</a>"},"month":"04","date_updated":"2021-01-12T08:19:20Z","page":"4255-4268","author":[{"full_name":"Rennella, Enrico","first_name":"Enrico","last_name":"Rennella"},{"last_name":"Sára","full_name":"Sára, Tomáš","first_name":"Tomáš"},{"last_name":"Juen","full_name":"Juen, Michael","first_name":"Michael"},{"full_name":"Wunderlich, Christoph","first_name":"Christoph","last_name":"Wunderlich"},{"last_name":"Imbert","first_name":"Lionel","full_name":"Imbert, Lionel"},{"last_name":"Solyom","first_name":"Zsofia","full_name":"Solyom, Zsofia"},{"full_name":"Favier, Adrien","first_name":"Adrien","last_name":"Favier"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"last_name":"Weinhäupl","first_name":"Katharina","full_name":"Weinhäupl, Katharina"},{"first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606"},{"last_name":"Konrat","first_name":"Robert","full_name":"Konrat, Robert"},{"last_name":"Kreutz","first_name":"Christoph","full_name":"Kreutz, Christoph"},{"first_name":"Bernhard","full_name":"Brutscher, Bernhard","last_name":"Brutscher"}],"intvolume":"        45","title":"RNA binding and chaperone activity of the E.coli cold-shock protein CspA","doi":"10.1093/nar/gkx044","abstract":[{"lang":"eng","text":"Ensuring the correct folding of RNA molecules in the cell is of major importance for a large variety of biological functions. Therefore, chaperone proteins that assist RNA in adopting their functionally active states are abundant in all living organisms. An important feature of RNA chaperone proteins is that they do not require an external energy source to perform their activity, and that they interact transiently and non-specifically with their RNA targets. So far, little is known about the mechanistic details of the RNA chaperone activity of these proteins. Prominent examples of RNA chaperones are bacterial cold shock proteins (Csp) that have been reported to bind single-stranded RNA and DNA. Here, we have used advanced NMR spectroscopy techniques to investigate at atomic resolution the RNA-melting activity of CspA, the major cold shock protein of Escherichia coli, upon binding to different RNA hairpins. Real-time NMR provides detailed information on the folding kinetics and folding pathways. Finally, comparison of wild-type CspA with single-point mutants and small peptides yields insights into the complementary roles of aromatic and positively charged amino-acid side chains for the RNA chaperone activity of the protein."}],"article_type":"original","date_published":"2017-04-20T00:00:00Z","year":"2017","publication_identifier":{"issn":["0305-1048","1362-4962"]}},{"article_processing_charge":"No","publication_status":"published","volume":1635,"type":"book_chapter","fulldoi":"https://doi.org/10.1007/978-1-4939-7151-0_6","extern":"1","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","_id":"8450","language":[{"iso":"eng"}],"oa_version":"None","day":"29","date_created":"2020-09-18T10:06:44Z","status":"public","publisher":"Springer Nature","citation":{"mla":"Kurauskas, Vilius, et al. “Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins.” <i>Membrane Protein Structure and Function Characterization</i>, vol. 1635, Springer Nature, 2017, pp. 109–23, doi:<a href=\"https://doi.org/10.1007/978-1-4939-7151-0_6\">10.1007/978-1-4939-7151-0_6</a>.","ista":"Kurauskas V, Schanda P, Sounier R. 2017.Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In: Membrane protein structure and function characterization. Methods in Molecular Biology, vol. 1635, 109–123.","ama":"Kurauskas V, Schanda P, Sounier R. Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In: <i>Membrane Protein Structure and Function Characterization</i>. Vol 1635. Springer Nature; 2017:109-123. doi:<a href=\"https://doi.org/10.1007/978-1-4939-7151-0_6\">10.1007/978-1-4939-7151-0_6</a>","chicago":"Kurauskas, Vilius, Paul Schanda, and Remy Sounier. “Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins.” In <i>Membrane Protein Structure and Function Characterization</i>, 1635:109–23. Springer Nature, 2017. <a href=\"https://doi.org/10.1007/978-1-4939-7151-0_6\">https://doi.org/10.1007/978-1-4939-7151-0_6</a>.","apa":"Kurauskas, V., Schanda, P., &#38; Sounier, R. (2017). Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In <i>Membrane protein structure and function characterization</i> (Vol. 1635, pp. 109–123). Springer Nature. <a href=\"https://doi.org/10.1007/978-1-4939-7151-0_6\">https://doi.org/10.1007/978-1-4939-7151-0_6</a>","ieee":"V. Kurauskas, P. Schanda, and R. Sounier, “Methyl-specific isotope labeling strategies for NMR studies of membrane proteins,” in <i>Membrane protein structure and function characterization</i>, vol. 1635, Springer Nature, 2017, pp. 109–123.","short":"V. Kurauskas, P. Schanda, R. Sounier, in:, Membrane Protein Structure and Function Characterization, Springer Nature, 2017, pp. 109–123."},"publication":"Membrane protein structure and function characterization","quality_controlled":"1","author":[{"last_name":"Kurauskas","first_name":"Vilius","full_name":"Kurauskas, Vilius"},{"first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606"},{"first_name":"Remy","full_name":"Sounier, Remy","last_name":"Sounier"}],"page":"109-123","alternative_title":["Methods in Molecular Biology"],"date_updated":"2022-08-26T09:14:20Z","month":"07","title":"Methyl-specific isotope labeling strategies for NMR studies of membrane proteins","intvolume":"      1635","doi":"10.1007/978-1-4939-7151-0_6","abstract":[{"text":"Methyl groups are very useful probes of structure, dynamics, and interactions in protein NMR spectroscopy. In particular, methyl-directed experiments provide high sensitivity even in very large proteins, such as membrane proteins in a membrane-mimicking environment. In this chapter, we discuss the approach for labeling methyl groups in E. coli-based protein expression, as exemplified with the mitochondrial carrier GGC.","lang":"eng"}],"publication_identifier":{"isbn":["9781493971497","9781493971510"],"issn":["1064-3745","1940-6029"]},"year":"2017","date_published":"2017-07-29T00:00:00Z"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","fulldoi":"https://doi.org/10.1002/anie.201610441","type":"journal_article","volume":56,"publication_status":"published","article_processing_charge":"No","issue":"9","date_created":"2020-09-18T10:06:50Z","day":"27","oa_version":"None","language":[{"iso":"eng"}],"_id":"8451","page":"2508-2512","date_updated":"2021-01-12T08:19:22Z","author":[{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"last_name":"Dörr","full_name":"Dörr, Jonas M.","first_name":"Jonas M."},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"last_name":"Killian","full_name":"Killian, J. Antoinette","first_name":"J. Antoinette"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul"}],"month":"01","citation":{"ama":"Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. <i>Angewandte Chemie International Edition</i>. 2017;56(9):2508-2512. doi:<a href=\"https://doi.org/10.1002/anie.201610441\">10.1002/anie.201610441</a>","mla":"Bersch, Beate, et al. “Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.” <i>Angewandte Chemie International Edition</i>, vol. 56, no. 9, Wiley, 2017, pp. 2508–12, doi:<a href=\"https://doi.org/10.1002/anie.201610441\">10.1002/anie.201610441</a>.","ista":"Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. 2017. Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. Angewandte Chemie International Edition. 56(9), 2508–2512.","ieee":"B. Bersch, J. M. Dörr, A. Hessel, J. A. Killian, and P. Schanda, “Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs,” <i>Angewandte Chemie International Edition</i>, vol. 56, no. 9. Wiley, pp. 2508–2512, 2017.","short":"B. Bersch, J.M. Dörr, A. Hessel, J.A. Killian, P. Schanda, Angewandte Chemie International Edition 56 (2017) 2508–2512.","chicago":"Bersch, Beate, Jonas M. Dörr, Audrey Hessel, J. Antoinette Killian, and Paul Schanda. “Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.” <i>Angewandte Chemie International Edition</i>. Wiley, 2017. <a href=\"https://doi.org/10.1002/anie.201610441\">https://doi.org/10.1002/anie.201610441</a>.","apa":"Bersch, B., Dörr, J. M., Hessel, A., Killian, J. A., &#38; Schanda, P. (2017). Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. <i>Angewandte Chemie International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.201610441\">https://doi.org/10.1002/anie.201610441</a>"},"quality_controlled":"1","publication":"Angewandte Chemie International Edition","publisher":"Wiley","status":"public","publication_identifier":{"issn":["1433-7851"]},"date_published":"2017-01-27T00:00:00Z","year":"2017","article_type":"original","abstract":[{"lang":"eng","text":"The structure, dynamics, and function of membrane proteins are intimately linked to the properties of the membrane environment in which the proteins are embedded. For structural and biophysical characterization, membrane proteins generally need to be extracted from the membrane and reconstituted in a suitable membrane‐mimicking environment. Ensuring functional and structural integrity in these environments is often a major concern. The styrene/maleic acid co‐polymer has recently been shown to be able to extract lipid/membrane protein patches directly from native membranes to form nanosize discoidal proteolipid particles, also referred to as native nanodiscs. In this work, we show that high‐resolution solid‐state NMR spectra can be obtained from an integral membrane protein in native nanodiscs, as exemplified by the 2×34 kDa bacterial cation diffusion facilitator CzcD."}],"doi":"10.1002/anie.201610441","title":"Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs","intvolume":"        56"},{"language":[{"iso":"eng"}],"oa_version":"None","article_number":"155102","_id":"9065","issue":"15","day":"01","date_created":"2021-02-02T15:49:21Z","volume":96,"article_processing_charge":"No","publication_status":"published","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1103/physrevb.96.155102","type":"journal_article","doi":"10.1103/physrevb.96.155102","intvolume":"        96","title":"In-plane magnetic anisotropy in strontium iridate Sr2IrO4","year":"2017","date_published":"2017-10-01T00:00:00Z","publication_identifier":{"issn":["2469-9950","2469-9969"]},"abstract":[{"text":"Magnetic anisotropy in strontium iridate (Sr2IrO4) is found to be large because of the strong spin-orbit interactions. In our work, we studied the in-plane magnetic anisotropy of Sr2IrO4 and traced the anisotropic exchange interactions between the isospins in the crystal. The magnetic-field-dependent torque τ(H) showed a prominent transition from the canted antiferromagnetic state to the weak ferromagnetic (WFM) state. A comprehensive analysis was conducted to examine the isotropic and anisotropic regimes and probe the easy magnetization axis along the a b plane. The angle-dependent torque τ(θ) revealed a deviation from the sinusoidal behavior, and small differences in hysteresis were observed around 0° and 90° in the low-magnetic-field regime. This indicates that the orientation of the easy axis of the FM component is along the b axis, where the antiferromagnetic to WFM spin-flop transition occurs. We compared the coefficients of the magnetic susceptibility tensors and captured the anisotropy of the material. The in-plane τ(θ) revealed a tendency toward isotropic behavior for fields with values above the field value of the WFM transition.","lang":"eng"}],"article_type":"original","publisher":"American Physical Society","status":"public","month":"10","author":[{"orcid":"0000-0002-2111-4846","id":"32c21954-2022-11eb-9d5f-af9f93c24e71","last_name":"Nauman","first_name":"Muhammad","full_name":"Nauman, Muhammad"},{"last_name":"Hong","full_name":"Hong, Yunjeong","first_name":"Yunjeong"},{"first_name":"Tayyaba","full_name":"Hussain, Tayyaba","last_name":"Hussain"},{"full_name":"Seo, M. S.","first_name":"M. S.","last_name":"Seo"},{"first_name":"S. Y.","full_name":"Park, S. Y.","last_name":"Park"},{"last_name":"Lee","first_name":"N.","full_name":"Lee, N."},{"last_name":"Choi","first_name":"Y. J.","full_name":"Choi, Y. J."},{"first_name":"Woun","full_name":"Kang, Woun","last_name":"Kang"},{"last_name":"Jo","first_name":"Younjung","full_name":"Jo, Younjung"}],"date_updated":"2021-02-03T12:53:00Z","publication":"Physical Review B","quality_controlled":"1","citation":{"mla":"Nauman, Muhammad, et al. “In-Plane Magnetic Anisotropy in Strontium Iridate Sr2IrO4.” <i>Physical Review B</i>, vol. 96, no. 15, 155102, American Physical Society, 2017, doi:<a href=\"https://doi.org/10.1103/physrevb.96.155102\">10.1103/physrevb.96.155102</a>.","ista":"Nauman M, Hong Y, Hussain T, Seo MS, Park SY, Lee N, Choi YJ, Kang W, Jo Y. 2017. In-plane magnetic anisotropy in strontium iridate Sr2IrO4. Physical Review B. 96(15), 155102.","ama":"Nauman M, Hong Y, Hussain T, et al. In-plane magnetic anisotropy in strontium iridate Sr2IrO4. <i>Physical Review B</i>. 2017;96(15). doi:<a href=\"https://doi.org/10.1103/physrevb.96.155102\">10.1103/physrevb.96.155102</a>","chicago":"Nauman, Muhammad, Yunjeong Hong, Tayyaba Hussain, M. S. Seo, S. Y. Park, N. Lee, Y. J. Choi, Woun Kang, and Younjung Jo. “In-Plane Magnetic Anisotropy in Strontium Iridate Sr2IrO4.” <i>Physical Review B</i>. American Physical Society, 2017. <a href=\"https://doi.org/10.1103/physrevb.96.155102\">https://doi.org/10.1103/physrevb.96.155102</a>.","apa":"Nauman, M., Hong, Y., Hussain, T., Seo, M. S., Park, S. Y., Lee, N., … Jo, Y. (2017). In-plane magnetic anisotropy in strontium iridate Sr2IrO4. <i>Physical Review B</i>. American Physical Society. <a href=\"https://doi.org/10.1103/physrevb.96.155102\">https://doi.org/10.1103/physrevb.96.155102</a>","ieee":"M. Nauman <i>et al.</i>, “In-plane magnetic anisotropy in strontium iridate Sr2IrO4,” <i>Physical Review B</i>, vol. 96, no. 15. American Physical Society, 2017.","short":"M. Nauman, Y. Hong, T. Hussain, M.S. Seo, S.Y. Park, N. Lee, Y.J. Choi, W. Kang, Y. Jo, Physical Review B 96 (2017)."}},{"_id":"909","language":[{"iso":"eng"}],"oa_version":"Submitted Version","scopus_import":"1","date_created":"2018-12-11T11:49:09Z","day":"01","ec_funded":1,"oa":1,"publication_status":"published","volume":124,"project":[{"grant_number":"291734","name":"International IST Postdoc Fellowship Programme","_id":"25681D80-B435-11E9-9278-68D0E5697425","call_identifier":"FP7"}],"fulldoi":"https://doi.org/10.4169/amer.math.monthly.124.7.588","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","department":[{"_id":"HeEd"}],"doi":"10.4169/amer.math.monthly.124.7.588","article_type":"original","external_id":{"arxiv":["1605.07997"],"isi":["000413947300002"]},"publication_identifier":{"issn":["0002-9890"]},"date_published":"2017-01-01T00:00:00Z","status":"public","publisher":"Mathematical Association of America","citation":{"ieee":"A. Akopyan and V. Vysotsky, “On the lengths of curves passing through boundary points of a planar convex shape,” <i>The American Mathematical Monthly</i>, vol. 124, no. 7. Mathematical Association of America, pp. 588–596, 2017.","short":"A. Akopyan, V. Vysotsky, The American Mathematical Monthly 124 (2017) 588–596.","chicago":"Akopyan, Arseniy, and Vladislav Vysotsky. “On the Lengths of Curves Passing through Boundary Points of a Planar Convex Shape.” <i>The American Mathematical Monthly</i>. Mathematical Association of America, 2017. <a href=\"https://doi.org/10.4169/amer.math.monthly.124.7.588\">https://doi.org/10.4169/amer.math.monthly.124.7.588</a>.","apa":"Akopyan, A., &#38; Vysotsky, V. (2017). On the lengths of curves passing through boundary points of a planar convex shape. <i>The American Mathematical Monthly</i>. Mathematical Association of America. <a href=\"https://doi.org/10.4169/amer.math.monthly.124.7.588\">https://doi.org/10.4169/amer.math.monthly.124.7.588</a>","ama":"Akopyan A, Vysotsky V. On the lengths of curves passing through boundary points of a planar convex shape. <i>The American Mathematical Monthly</i>. 2017;124(7):588-596. doi:<a href=\"https://doi.org/10.4169/amer.math.monthly.124.7.588\">10.4169/amer.math.monthly.124.7.588</a>","mla":"Akopyan, Arseniy, and Vladislav Vysotsky. “On the Lengths of Curves Passing through Boundary Points of a Planar Convex Shape.” <i>The American Mathematical Monthly</i>, vol. 124, no. 7, Mathematical Association of America, 2017, pp. 588–96, doi:<a href=\"https://doi.org/10.4169/amer.math.monthly.124.7.588\">10.4169/amer.math.monthly.124.7.588</a>.","ista":"Akopyan A, Vysotsky V. 2017. On the lengths of curves passing through boundary points of a planar convex shape. The American Mathematical Monthly. 124(7), 588–596."},"isi":1,"quality_controlled":"1","author":[{"last_name":"Akopyan","id":"430D2C90-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-2548-617X","full_name":"Akopyan, Arseniy","first_name":"Arseniy"},{"full_name":"Vysotsky, Vladislav","first_name":"Vladislav","last_name":"Vysotsky"}],"page":"588 - 596","issue":"7","article_processing_charge":"No","type":"journal_article","intvolume":"       124","title":"On the lengths of curves passing through boundary points of a planar convex shape","main_file_link":[{"url":"https://arxiv.org/abs/1605.07997","open_access":"1"}],"abstract":[{"lang":"eng","text":"We study the lengths of curves passing through a fixed number of points on the boundary of a convex shape in the plane. We show that, for any convex shape K, there exist four points on the boundary of K such that the length of any curve passing through these points is at least half of the perimeter of K. It is also shown that the same statement does not remain valid with the additional constraint that the points are extreme points of K. Moreover, the factor &amp;#xbd; cannot be achieved with any fixed number of extreme points. We conclude the paper with a few other inequalities related to the perimeter of a convex shape."}],"year":"2017","publist_id":"6534","publication":"The American Mathematical Monthly","arxiv":1,"date_updated":"2025-07-10T12:01:35Z","month":"01"},{"issue":"2","type":"journal_article","article_processing_charge":"No","abstract":[{"lang":"eng","text":"Frequency-independent selection is generally considered as a force that acts to reduce the genetic variation in evolving populations, yet rigorous arguments for this idea are scarce. When selection fluctuates in time, it is unclear whether frequency-independent selection may maintain genetic polymorphism without invoking additional mechanisms. We show that constant frequency-independent selection with arbitrary epistasis on a well-mixed haploid population eliminates genetic variation if we assume linkage equilibrium between alleles. To this end, we introduce the notion of frequency-independent selection at the level of alleles, which is sufficient to prove our claim and contains the notion of frequency-independent selection on haploids. When selection and recombination are weak but of the same order, there may be strong linkage disequilibrium; numerical calculations show that stable equilibria are highly unlikely. Using the example of a diallelic two-locus model, we then demonstrate that frequency-independent selection that fluctuates in time can maintain stable polymorphism if linkage disequilibrium changes its sign periodically. We put our findings in the context of results from the existing literature and point out those scenarios in which the possible role of frequency-independent selection in maintaining genetic variation remains unclear.\r\n"}],"publist_id":"6533","year":"2017","title":"When does frequency-independent selection maintain genetic variation?","intvolume":"       207","has_accepted_license":"1","publication":"Genetics","date_updated":"2025-04-15T08:22:21Z","month":"10","file":[{"date_updated":"2020-07-14T12:48:15Z","file_name":"IST-2018-974-v1+1_manuscript.pdf","file_id":"5264","access_level":"open_access","file_size":494268,"date_created":"2018-12-12T10:17:12Z","content_type":"application/pdf","checksum":"f7c32dabf52e6d9e709d9203761e39fd","creator":"system","relation":"main_file"}],"day":"01","date_created":"2018-12-11T11:49:09Z","ec_funded":1,"ddc":["576"],"_id":"910","corr_author":"1","oa_version":"Submitted Version","language":[{"iso":"eng"}],"scopus_import":"1","pubrep_id":"974","fulldoi":"https://doi.org/10.1534/genetics.117.300129","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","publication_status":"published","oa":1,"project":[{"name":"Speed of Adaptation in Population Genetics and Evolutionary Computation","_id":"25B1EC9E-B435-11E9-9278-68D0E5697425","call_identifier":"FP7","grant_number":"618091"}],"volume":207,"external_id":{"isi":["000412232600019"]},"date_published":"2017-10-01T00:00:00Z","department":[{"_id":"NiBa"}],"doi":"10.1534/genetics.117.300129","file_date_updated":"2020-07-14T12:48:15Z","citation":{"ista":"Novak S, Barton NH. 2017. When does frequency-independent selection maintain genetic variation? Genetics. 207(2), 653–668.","mla":"Novak, Sebastian, and Nicholas H. Barton. “When Does Frequency-Independent Selection Maintain Genetic Variation?” <i>Genetics</i>, vol. 207, no. 2, Genetics Society of America, 2017, pp. 653–68, doi:<a href=\"https://doi.org/10.1534/genetics.117.300129\">10.1534/genetics.117.300129</a>.","ama":"Novak S, Barton NH. When does frequency-independent selection maintain genetic variation? <i>Genetics</i>. 2017;207(2):653-668. doi:<a href=\"https://doi.org/10.1534/genetics.117.300129\">10.1534/genetics.117.300129</a>","apa":"Novak, S., &#38; Barton, N. H. (2017). When does frequency-independent selection maintain genetic variation? <i>Genetics</i>. Genetics Society of America. <a href=\"https://doi.org/10.1534/genetics.117.300129\">https://doi.org/10.1534/genetics.117.300129</a>","chicago":"Novak, Sebastian, and Nicholas H Barton. “When Does Frequency-Independent Selection Maintain Genetic Variation?” <i>Genetics</i>. Genetics Society of America, 2017. <a href=\"https://doi.org/10.1534/genetics.117.300129\">https://doi.org/10.1534/genetics.117.300129</a>.","short":"S. Novak, N.H. Barton, Genetics 207 (2017) 653–668.","ieee":"S. Novak and N. H. Barton, “When does frequency-independent selection maintain genetic variation?,” <i>Genetics</i>, vol. 207, no. 2. Genetics Society of America, pp. 653–668, 2017."},"isi":1,"quality_controlled":"1","page":"653 - 668","author":[{"orcid":"0000-0002-2519-824X","last_name":"Novak","id":"461468AE-F248-11E8-B48F-1D18A9856A87","full_name":"Novak, Sebastian","first_name":"Sebastian"},{"first_name":"Nicholas H","full_name":"Barton, Nicholas H","orcid":"0000-0002-8548-5240","id":"4880FE40-F248-11E8-B48F-1D18A9856A87","last_name":"Barton"}],"status":"public","publisher":"Genetics Society of America"},{"date_published":"2017-09-01T00:00:00Z","publication_identifier":{"eisbn":["190172560X"]},"external_id":{"arxiv":["1705.04258"]},"file_date_updated":"2020-08-10T07:14:33Z","doi":"10.5244/c.31.85","department":[{"_id":"ChLa"}],"page":"85.1-85.12","author":[{"full_name":"Royer, Amélie","first_name":"Amélie","orcid":"0000-0002-8407-0705","last_name":"Royer","id":"3811D890-F248-11E8-B48F-1D18A9856A87"},{"id":"2D157DB6-F248-11E8-B48F-1D18A9856A87","last_name":"Kolesnikov","first_name":"Alexander","full_name":"Kolesnikov, Alexander"},{"orcid":"0000-0001-8622-7887","id":"40C20FD2-F248-11E8-B48F-1D18A9856A87","last_name":"Lampert","first_name":"Christoph","full_name":"Lampert, Christoph"}],"quality_controlled":"1","citation":{"ama":"Royer A, Kolesnikov A, Lampert C. Probabilistic image colorization. In: BMVA Press; 2017:85.1-85.12. doi:<a href=\"https://doi.org/10.5244/c.31.85\">10.5244/c.31.85</a>","ista":"Royer A, Kolesnikov A, Lampert C. 2017. Probabilistic image colorization. BMVC: British Machine Vision Conference, 85.1-85.12.","mla":"Royer, Amélie, et al. <i>Probabilistic Image Colorization</i>. BMVA Press, 2017, p. 85.1-85.12, doi:<a href=\"https://doi.org/10.5244/c.31.85\">10.5244/c.31.85</a>.","short":"A. Royer, A. Kolesnikov, C. Lampert, in:, BMVA Press, 2017, p. 85.1-85.12.","ieee":"A. Royer, A. Kolesnikov, and C. Lampert, “Probabilistic image colorization,” presented at the BMVC: British Machine Vision Conference, London, United Kingdom, 2017, p. 85.1-85.12.","apa":"Royer, A., Kolesnikov, A., &#38; Lampert, C. (2017). Probabilistic image colorization (p. 85.1-85.12). Presented at the BMVC: British Machine Vision Conference, London, United Kingdom: BMVA Press. <a href=\"https://doi.org/10.5244/c.31.85\">https://doi.org/10.5244/c.31.85</a>","chicago":"Royer, Amélie, Alexander Kolesnikov, and Christoph Lampert. “Probabilistic Image Colorization,” 85.1-85.12. BMVA Press, 2017. <a href=\"https://doi.org/10.5244/c.31.85\">https://doi.org/10.5244/c.31.85</a>."},"publisher":"BMVA Press","status":"public","ddc":["000"],"ec_funded":1,"date_created":"2018-12-11T11:49:09Z","day":"01","scopus_import":"1","oa_version":"Published Version","corr_author":"1","language":[{"iso":"eng"}],"_id":"911","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.5244/c.31.85","project":[{"grant_number":"308036","call_identifier":"FP7","name":"Lifelong Learning of Visual Scene Understanding","_id":"2532554C-B435-11E9-9278-68D0E5697425"}],"conference":{"name":"BMVC: British Machine Vision Conference","start_date":"2017-09-04","location":"London, United Kingdom","end_date":"2017-09-07"},"oa":1,"publication_status":"published","publist_id":"6532","year":"2017","abstract":[{"lang":"eng","text":"We develop a probabilistic technique for colorizing grayscale natural images. In light of the intrinsic uncertainty of this task, the proposed probabilistic framework has numerous desirable properties. In particular, our model is able to produce multiple plausible and vivid colorizations for a given grayscale image and is one of the first colorization models to provide a proper stochastic sampling scheme. Moreover, our training procedure is supported by a rigorous theoretical framework that does not require any ad hoc heuristics and allows for efficient modeling and learning of the joint pixel color distribution.We demonstrate strong quantitative and qualitative experimental results on the CIFAR-10 dataset and the challenging ILSVRC 2012 dataset."}],"related_material":{"record":[{"id":"8390","status":"public","relation":"dissertation_contains"}]},"has_accepted_license":"1","title":"Probabilistic image colorization","month":"09","file":[{"content_type":"application/pdf","date_created":"2020-08-10T07:14:33Z","file_size":1625363,"relation":"main_file","success":1,"creator":"dernst","file_name":"2017_BMVC_Royer.pdf","date_updated":"2020-08-10T07:14:33Z","access_level":"open_access","file_id":"8224"}],"date_updated":"2026-04-08T07:26:44Z","arxiv":1,"type":"conference","article_processing_charge":"No"},{"volume":38,"publication_status":"published","oa":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","fulldoi":"https://doi.org/10.1007/s10712-017-9447-x","oa_version":"Published Version","language":[{"iso":"eng"}],"_id":"9137","date_created":"2021-02-15T14:20:07Z","day":"14","publisher":"Springer Nature","status":"public","page":"1283-1305","author":[{"last_name":"Zuidema","full_name":"Zuidema, Paquita","first_name":"Paquita"},{"last_name":"Torri","full_name":"Torri, Giuseppe","first_name":"Giuseppe"},{"first_name":"Caroline J","full_name":"Muller, Caroline J","orcid":"0000-0001-5836-5350","id":"f978ccb0-3f7f-11eb-b193-b0e2bd13182b","last_name":"Muller"},{"last_name":"Chandra","full_name":"Chandra, Arunchandra","first_name":"Arunchandra"}],"citation":{"mla":"Zuidema, Paquita, et al. “A Survey of Precipitation-Induced Atmospheric Cold Pools over Oceans and Their Interactions with the Larger-Scale Environment.” <i>Surveys in Geophysics</i>, vol. 38, no. 6, Springer Nature, 2017, pp. 1283–305, doi:<a href=\"https://doi.org/10.1007/s10712-017-9447-x\">10.1007/s10712-017-9447-x</a>.","ista":"Zuidema P, Torri G, Muller CJ, Chandra A. 2017. A survey of precipitation-induced atmospheric cold pools over oceans and their interactions with the larger-scale environment. Surveys in Geophysics. 38(6), 1283–1305.","ama":"Zuidema P, Torri G, Muller CJ, Chandra A. A survey of precipitation-induced atmospheric cold pools over oceans and their interactions with the larger-scale environment. <i>Surveys in Geophysics</i>. 2017;38(6):1283-1305. doi:<a href=\"https://doi.org/10.1007/s10712-017-9447-x\">10.1007/s10712-017-9447-x</a>","chicago":"Zuidema, Paquita, Giuseppe Torri, Caroline J Muller, and Arunchandra Chandra. “A Survey of Precipitation-Induced Atmospheric Cold Pools over Oceans and Their Interactions with the Larger-Scale Environment.” <i>Surveys in Geophysics</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1007/s10712-017-9447-x\">https://doi.org/10.1007/s10712-017-9447-x</a>.","apa":"Zuidema, P., Torri, G., Muller, C. J., &#38; Chandra, A. (2017). A survey of precipitation-induced atmospheric cold pools over oceans and their interactions with the larger-scale environment. <i>Surveys in Geophysics</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10712-017-9447-x\">https://doi.org/10.1007/s10712-017-9447-x</a>","ieee":"P. Zuidema, G. Torri, C. J. Muller, and A. Chandra, “A survey of precipitation-induced atmospheric cold pools over oceans and their interactions with the larger-scale environment,” <i>Surveys in Geophysics</i>, vol. 38, no. 6. Springer Nature, pp. 1283–1305, 2017.","short":"P. Zuidema, G. Torri, C.J. Muller, A. Chandra, Surveys in Geophysics 38 (2017) 1283–1305."},"quality_controlled":"1","doi":"10.1007/s10712-017-9447-x","keyword":["Geochemistry and Petrology","Geophysics"],"publication_identifier":{"issn":["0169-3298","1573-0956"]},"date_published":"2017-11-14T00:00:00Z","article_type":"original","article_processing_charge":"No","extern":"1","type":"journal_article","issue":"6","date_updated":"2022-01-24T12:41:45Z","month":"11","publication":"Surveys in Geophysics","intvolume":"        38","title":"A survey of precipitation-induced atmospheric cold pools over oceans and their interactions with the larger-scale environment","year":"2017","main_file_link":[{"url":"https://doi.org/10.1007/s10712-017-9447-x","open_access":"1"}],"abstract":[{"lang":"eng","text":"Pools of air cooled by partial rain evaporation span up to several hundreds of kilometers in nature and typically last less than 1 day, ultimately losing their identity to the large-scale flow. These fundamentally differ in character from the radiatively-driven dry pools defining convective aggregation. Advancement in remote sensing and in computer capabilities has promoted exploration of how precipitation-induced cold pool processes modify the convective spectrum and life cycle. This contribution surveys current understanding of such cold pools over the tropical and subtropical oceans. In shallow convection with low rain rates, the cold pools moisten, preserving the near-surface equivalent potential temperature or increasing it if the surface moisture fluxes cannot ventilate beyond the new surface layer; both conditions indicate downdraft origin air from within the boundary layer. When rain rates exceed ∼ 2 mm h−1, convective-scale downdrafts can bring down drier air of lower equivalent potential temperature from above the boundary layer. The resulting density currents facilitate the lifting of locally thermodynamically favorable air and can impose an arc-shaped mesoscale cloud organization. This organization allows clouds capable of reaching 4–5 km within otherwise dry environments. These are more commonly observed in the northern hemisphere trade wind regime, where the flow to the intertropical convergence zone is unimpeded by the equator. Their near-surface air properties share much with those shown from cold pools sampled in the equatorial Indian Ocean. Cold pools are most effective at influencing the mesoscale organization when the atmosphere is moist in the lower free troposphere and dry above, suggesting an optimal range of water vapor paths. Outstanding questions on the relationship between cold pools, their accompanying moisture distribution and cloud cover are detailed further. Near-surface water vapor rings are documented in one model inside but near the cold pool edge; these are not consistent with observations, but do improve with smaller horizontal grid spacings."}]},{"type":"journal_article","extern":"1","article_processing_charge":"No","issue":"6","publication":"Surveys in Geophysics","month":"11","date_updated":"2022-01-24T12:43:13Z","main_file_link":[{"url":"https://doi.org/10.1007/s10712-017-9419-1","open_access":"1"}],"abstract":[{"text":"Convective self-aggregation, the spontaneous organization of initially scattered convection into isolated convective clusters despite spatially homogeneous boundary conditions and forcing, was first recognized and studied in idealized numerical simulations. While there is a rich history of observational work on convective clustering and organization, there have been only a few studies that have analyzed observations to look specifically for processes related to self-aggregation in models. Here we review observational work in both of these categories and motivate the need for more of this work. We acknowledge that self-aggregation may appear to be far-removed from observed convective organization in terms of time scales, initial conditions, initiation processes, and mean state extremes, but we argue that these differences vary greatly across the diverse range of model simulations in the literature and that these comparisons are already offering important insights into real tropical phenomena. Some preliminary new findings are presented, including results showing that a self-aggregation simulation with square geometry has too broad distribution of humidity and is too dry in the driest regions when compared with radiosonde records from Nauru, while an elongated channel simulation has realistic representations of atmospheric humidity and its variability. We discuss recent work increasing our understanding of how organized convection and climate change may interact, and how model discrepancies related to this question are prompting interest in observational comparisons. We also propose possible future directions for observational work related to convective aggregation, including novel satellite approaches and a ground-based observational network.","lang":"eng"}],"year":"2017","title":"Observing convective aggregation","intvolume":"        38","fulldoi":"https://doi.org/10.1007/s10712-017-9419-1","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","oa":1,"publication_status":"published","volume":38,"day":"01","date_created":"2021-02-15T14:20:38Z","_id":"9138","language":[{"iso":"eng"}],"oa_version":"Published Version","quality_controlled":"1","citation":{"ista":"Holloway CE, Wing AA, Bony S, Muller CJ, Masunaga H, L’Ecuyer TS, Turner DD, Zuidema P. 2017. Observing convective aggregation. Surveys in Geophysics. 38(6), 1199–1236.","mla":"Holloway, Christopher E., et al. “Observing Convective Aggregation.” <i>Surveys in Geophysics</i>, vol. 38, no. 6, Springer Nature, 2017, pp. 1199–236, doi:<a href=\"https://doi.org/10.1007/s10712-017-9419-1\">10.1007/s10712-017-9419-1</a>.","ama":"Holloway CE, Wing AA, Bony S, et al. Observing convective aggregation. <i>Surveys in Geophysics</i>. 2017;38(6):1199-1236. doi:<a href=\"https://doi.org/10.1007/s10712-017-9419-1\">10.1007/s10712-017-9419-1</a>","apa":"Holloway, C. E., Wing, A. A., Bony, S., Muller, C. J., Masunaga, H., L’Ecuyer, T. S., … Zuidema, P. (2017). Observing convective aggregation. <i>Surveys in Geophysics</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10712-017-9419-1\">https://doi.org/10.1007/s10712-017-9419-1</a>","chicago":"Holloway, Christopher E., Allison A. Wing, Sandrine Bony, Caroline J Muller, Hirohiko Masunaga, Tristan S. L’Ecuyer, David D. Turner, and Paquita Zuidema. “Observing Convective Aggregation.” <i>Surveys in Geophysics</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1007/s10712-017-9419-1\">https://doi.org/10.1007/s10712-017-9419-1</a>.","short":"C.E. Holloway, A.A. Wing, S. Bony, C.J. Muller, H. Masunaga, T.S. L’Ecuyer, D.D. Turner, P. Zuidema, Surveys in Geophysics 38 (2017) 1199–1236.","ieee":"C. E. Holloway <i>et al.</i>, “Observing convective aggregation,” <i>Surveys in Geophysics</i>, vol. 38, no. 6. Springer Nature, pp. 1199–1236, 2017."},"author":[{"full_name":"Holloway, Christopher E.","first_name":"Christopher E.","last_name":"Holloway"},{"full_name":"Wing, Allison A.","first_name":"Allison A.","last_name":"Wing"},{"first_name":"Sandrine","full_name":"Bony, Sandrine","last_name":"Bony"},{"orcid":"0000-0001-5836-5350","last_name":"Muller","id":"f978ccb0-3f7f-11eb-b193-b0e2bd13182b","full_name":"Muller, Caroline J","first_name":"Caroline J"},{"first_name":"Hirohiko","full_name":"Masunaga, Hirohiko","last_name":"Masunaga"},{"last_name":"L’Ecuyer","full_name":"L’Ecuyer, Tristan S.","first_name":"Tristan S."},{"last_name":"Turner","full_name":"Turner, David D.","first_name":"David D."},{"last_name":"Zuidema","full_name":"Zuidema, Paquita","first_name":"Paquita"}],"page":"1199-1236","status":"public","publisher":"Springer Nature","article_type":"original","date_published":"2017-11-01T00:00:00Z","publication_identifier":{"issn":["0169-3298","1573-0956"]},"keyword":["Geochemistry and Petrology","Geophysics"],"doi":"10.1007/s10712-017-9419-1"}]