[{"keyword":["Geometry and Topology","Analysis"],"oa":1,"article_type":"original","title":"Nearly circular domains which are integrable close to the boundary are ellipses","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:11Z","type":"journal_article","abstract":[{"text":"The Birkhoff conjecture says that the boundary of a strictly convex integrable billiard table is necessarily an ellipse. In this article, we consider a stronger notion of integrability, namely integrability close to the boundary, and prove a local version of this conjecture: a small perturbation of an ellipse of small eccentricity which preserves integrability near the boundary, is itself an ellipse. This extends the result in Avila et al. (Ann Math 184:527–558, ADK16), where integrability was assumed on a larger set. In particular, it shows that (local) integrability near the boundary implies global integrability. One of the crucial ideas in the proof consists in analyzing Taylor expansion of the corresponding action-angle coordinates with respect to the eccentricity parameter, deriving and studying higher order conditions for the preservation of integrable rational caustics.","lang":"eng"}],"publication_identifier":{"issn":["1016-443X","1420-8970"]},"date_created":"2020-09-17T10:42:30Z","publication":"Geometric and Functional Analysis","arxiv":1,"oa_version":"Preprint","quality_controlled":"1","language":[{"iso":"eng"}],"month":"03","doi":"10.1007/s00039-018-0440-4","day":"18","publication_status":"published","status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1705.10601","open_access":"1"}],"citation":{"ama":"Huang G, Kaloshin V, Sorrentino A. Nearly circular domains which are integrable close to the boundary are ellipses. <i>Geometric and Functional Analysis</i>. 2018;28(2):334-392. doi:<a href=\"https://doi.org/10.1007/s00039-018-0440-4\">10.1007/s00039-018-0440-4</a>","apa":"Huang, G., Kaloshin, V., &#38; Sorrentino, A. (2018). Nearly circular domains which are integrable close to the boundary are ellipses. <i>Geometric and Functional Analysis</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00039-018-0440-4\">https://doi.org/10.1007/s00039-018-0440-4</a>","ieee":"G. Huang, V. Kaloshin, and A. Sorrentino, “Nearly circular domains which are integrable close to the boundary are ellipses,” <i>Geometric and Functional Analysis</i>, vol. 28, no. 2. Springer Nature, pp. 334–392, 2018.","ista":"Huang G, Kaloshin V, Sorrentino A. 2018. Nearly circular domains which are integrable close to the boundary are ellipses. Geometric and Functional Analysis. 28(2), 334–392.","short":"G. Huang, V. Kaloshin, A. Sorrentino, Geometric and Functional Analysis 28 (2018) 334–392.","mla":"Huang, Guan, et al. “Nearly Circular Domains Which Are Integrable Close to the Boundary Are Ellipses.” <i>Geometric and Functional Analysis</i>, vol. 28, no. 2, Springer Nature, 2018, pp. 334–92, doi:<a href=\"https://doi.org/10.1007/s00039-018-0440-4\">10.1007/s00039-018-0440-4</a>.","chicago":"Huang, Guan, Vadim Kaloshin, and Alfonso Sorrentino. “Nearly Circular Domains Which Are Integrable Close to the Boundary Are Ellipses.” <i>Geometric and Functional Analysis</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1007/s00039-018-0440-4\">https://doi.org/10.1007/s00039-018-0440-4</a>."},"author":[{"full_name":"Huang, Guan","last_name":"Huang","first_name":"Guan"},{"first_name":"Vadim","orcid":"0000-0002-6051-2628","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","full_name":"Kaloshin, Vadim","last_name":"Kaloshin"},{"first_name":"Alfonso","full_name":"Sorrentino, Alfonso","last_name":"Sorrentino"}],"_id":"8422","extern":"1","external_id":{"arxiv":["1705.10601"]},"issue":"2","volume":28,"intvolume":"        28","article_processing_charge":"No","page":"334-392","date_published":"2018-03-18T00:00:00Z","year":"2018","publisher":"Springer Nature"},{"publisher":"Springer Nature","year":"2018","date_published":"2018-02-05T00:00:00Z","page":"54-59","article_processing_charge":"No","intvolume":"        23","volume":23,"external_id":{"arxiv":["1801.00952"]},"_id":"8426","extern":"1","author":[{"last_name":"Buhovsky","full_name":"Buhovsky, Lev","first_name":"Lev"},{"first_name":"Vadim","orcid":"0000-0002-6051-2628","last_name":"Kaloshin","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","full_name":"Kaloshin, Vadim"}],"citation":{"chicago":"Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same Marvizi-Melrose Invariants.” <i>Regular and Chaotic Dynamics</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1134/s1560354718010057\">https://doi.org/10.1134/s1560354718010057</a>.","mla":"Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same Marvizi-Melrose Invariants.” <i>Regular and Chaotic Dynamics</i>, vol. 23, Springer Nature, 2018, pp. 54–59, doi:<a href=\"https://doi.org/10.1134/s1560354718010057\">10.1134/s1560354718010057</a>.","short":"L. Buhovsky, V. Kaloshin, Regular and Chaotic Dynamics 23 (2018) 54–59.","ista":"Buhovsky L, Kaloshin V. 2018. Nonisometric domains with the same Marvizi-Melrose invariants. Regular and Chaotic Dynamics. 23, 54–59.","ieee":"L. Buhovsky and V. Kaloshin, “Nonisometric domains with the same Marvizi-Melrose invariants,” <i>Regular and Chaotic Dynamics</i>, vol. 23. Springer Nature, pp. 54–59, 2018.","apa":"Buhovsky, L., &#38; Kaloshin, V. (2018). Nonisometric domains with the same Marvizi-Melrose invariants. <i>Regular and Chaotic Dynamics</i>. Springer Nature. <a href=\"https://doi.org/10.1134/s1560354718010057\">https://doi.org/10.1134/s1560354718010057</a>","ama":"Buhovsky L, Kaloshin V. Nonisometric domains with the same Marvizi-Melrose invariants. <i>Regular and Chaotic Dynamics</i>. 2018;23:54-59. doi:<a href=\"https://doi.org/10.1134/s1560354718010057\">10.1134/s1560354718010057</a>"},"main_file_link":[{"url":"https://arxiv.org/abs/1801.00952","open_access":"1"}],"status":"public","doi":"10.1134/s1560354718010057","day":"05","publication_status":"published","month":"02","oa_version":"Preprint","quality_controlled":"1","language":[{"iso":"eng"}],"arxiv":1,"publication_identifier":{"issn":["1560-3547","1468-4845"]},"publication":"Regular and Chaotic Dynamics","date_created":"2020-09-17T10:43:21Z","abstract":[{"text":"For any strictly convex planar domain Ω ⊂ R2 with a C∞ boundary one can associate an infinite sequence of spectral invariants introduced by Marvizi–Merlose [5]. These invariants can generically be determined using the spectrum of the Dirichlet problem of the Laplace operator. A natural question asks if this collection is sufficient to determine Ω up to isometry. In this paper we give a counterexample, namely, we present two nonisometric domains Ω and Ω¯ with the same collection of Marvizi–Melrose invariants. Moreover, each domain has countably many periodic orbits {Sn}n≥1 (resp. {S¯n}n⩾1) of period going to infinity such that Sn and S¯n have the same period and perimeter for each n.","lang":"eng"}],"date_updated":"2021-01-12T08:19:11Z","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Nonisometric domains with the same Marvizi-Melrose invariants","article_type":"original","oa":1},{"year":"2018","publisher":"Elsevier","status":"public","citation":{"chicago":"Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>.","mla":"Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>.","short":"K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.","ista":"Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L, Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K, Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.","ieee":"K. Weinhäupl <i>et al.</i>, “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” <i>Cell</i>, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.","ama":"Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. 2018;175(5):1365-1379.e25. doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>","apa":"Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>"},"article_processing_charge":"No","oa_version":"None","language":[{"iso":"eng"}],"page":"1365-1379.e25","quality_controlled":"1","month":"11","date_published":"2018-11-15T00:00:00Z","day":"15","doi":"10.1016/j.cell.2018.10.039","publication_status":"published","volume":175,"date_updated":"2021-01-12T08:19:15Z","type":"journal_article","intvolume":"       175","abstract":[{"text":"The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins in a “nascent chain-like” conformation through a ribosome-free compartment.","lang":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"publication":"Cell","date_created":"2020-09-18T10:04:39Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"author":[{"full_name":"Weinhäupl, Katharina","last_name":"Weinhäupl","first_name":"Katharina"},{"full_name":"Lindau, Caroline","last_name":"Lindau","first_name":"Caroline"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"full_name":"Wang, Yong","last_name":"Wang","first_name":"Yong"},{"first_name":"Conny","last_name":"Schütze","full_name":"Schütze, Conny"},{"last_name":"Jores","full_name":"Jores, Tobias","first_name":"Tobias"},{"full_name":"Melchionda, Laura","last_name":"Melchionda","first_name":"Laura"},{"first_name":"Birgit","last_name":"Schönfisch","full_name":"Schönfisch, Birgit"},{"first_name":"Hubert","full_name":"Kalbacher, Hubert","last_name":"Kalbacher"},{"full_name":"Bersch, Beate","last_name":"Bersch","first_name":"Beate"},{"first_name":"Doron","last_name":"Rapaport","full_name":"Rapaport, Doron"},{"last_name":"Brennich","full_name":"Brennich, Martha","first_name":"Martha"},{"full_name":"Lindorff-Larsen, Kresten","last_name":"Lindorff-Larsen","first_name":"Kresten"},{"first_name":"Nils","last_name":"Wiedemann","full_name":"Wiedemann, Nils"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"article_type":"original","_id":"8436","issue":"5","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space"},{"citation":{"chicago":"Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.” <i>Science Advances</i>. American Association for the Advancement of Science, 2018. <a href=\"https://doi.org/10.1126/sciadv.aau4196\">https://doi.org/10.1126/sciadv.aau4196</a>.","mla":"Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.” <i>Science Advances</i>, vol. 4, no. 9, eaau4196, American Association for the Advancement of Science, 2018, doi:<a href=\"https://doi.org/10.1126/sciadv.aau4196\">10.1126/sciadv.aau4196</a>.","short":"G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn, P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).","ista":"Mas G, Guan J-Y, Crublet E, Debled EC, Moriscot C, Gans P, Schoehn G, Macek P, Schanda P, Boisbouvier J. 2018. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 4(9), eaau4196.","ieee":"G. Mas <i>et al.</i>, “Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle,” <i>Science Advances</i>, vol. 4, no. 9. American Association for the Advancement of Science, 2018.","apa":"Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., … Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.aau4196\">https://doi.org/10.1126/sciadv.aau4196</a>","ama":"Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. <i>Science Advances</i>. 2018;4(9). doi:<a href=\"https://doi.org/10.1126/sciadv.aau4196\">10.1126/sciadv.aau4196</a>"},"publisher":"American Association for the Advancement of Science","status":"public","article_number":"eaau4196","year":"2018","day":"19","doi":"10.1126/sciadv.aau4196","publication_status":"published","month":"09","date_published":"2018-09-19T00:00:00Z","quality_controlled":"1","language":[{"iso":"eng"}],"oa_version":"None","article_processing_charge":"No","publication_identifier":{"issn":["2375-2548"]},"date_created":"2020-09-18T10:04:51Z","publication":"Science Advances","intvolume":"         4","abstract":[{"lang":"eng","text":"Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota, and archaea, facilitating the folding of proteins, preventing protein aggregation, and thus participating in maintaining protein homeostasis in the cell. During their functional cycle, they bind unfolded client proteins inside their double ring structure and promote protein folding by closing the ring chamber in an adenosine 5′-triphosphate (ATP)–dependent manner. Although the static structures of fully open and closed forms of chaperonins were solved by x-ray crystallography or electron microscopy, elucidating the mechanisms of such ATP-driven molecular events requires studying the proteins at the structural level under working conditions. We introduce an approach that combines site-specific nuclear magnetic resonance observation of very large proteins, enabled by advanced isotope labeling methods, with an in situ ATP regeneration system. Using this method, we provide functional insight into the 1-MDa large hsp60 chaperonin while processing client proteins and reveal how nucleotide binding, hydrolysis, and release control switching between closed and open states. While the open conformation stabilizes the unfolded state of client proteins, the internalization of the client protein inside the chaperonin cavity speeds up its functional cycle. This approach opens new perspectives to study structures and mechanisms of various ATP-driven biological machineries in the heat of action."}],"date_updated":"2022-08-26T09:11:06Z","type":"journal_article","volume":4,"issue":"9","_id":"8437","extern":"1","title":"Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","article_type":"original","author":[{"last_name":"Mas","full_name":"Mas, Guillaume","first_name":"Guillaume"},{"first_name":"Jia-Ying","full_name":"Guan, Jia-Ying","last_name":"Guan"},{"first_name":"Elodie","full_name":"Crublet, Elodie","last_name":"Crublet"},{"first_name":"Elisa Colas","last_name":"Debled","full_name":"Debled, Elisa Colas"},{"first_name":"Christine","last_name":"Moriscot","full_name":"Moriscot, Christine"},{"first_name":"Pierre","full_name":"Gans, Pierre","last_name":"Gans"},{"full_name":"Schoehn, Guy","last_name":"Schoehn","first_name":"Guy"},{"first_name":"Pavel","full_name":"Macek, Pavel","last_name":"Macek"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Boisbouvier","full_name":"Boisbouvier, Jerome","first_name":"Jerome"}]},{"volume":25,"date_updated":"2021-01-12T08:19:16Z","type":"journal_article","intvolume":"        25","publication_identifier":{"issn":["1545-9993","1545-9985"]},"date_created":"2020-09-18T10:04:59Z","publication":"Nature Structural & Molecular Biology","author":[{"last_name":"Kurauskas","full_name":"Kurauskas, Vilius","first_name":"Vilius"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"first_name":"François","last_name":"Dehez","full_name":"Dehez, François"},{"last_name":"Chipot","full_name":"Chipot, Christophe","first_name":"Christophe"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"keyword":["Molecular Biology","Structural Biology"],"article_type":"letter_note","_id":"8438","extern":"1","issue":"9","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Dynamics and interactions of AAC3 in DPC are not functionally relevant","year":"2018","publisher":"Springer Nature","status":"public","citation":{"ama":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>","apa":"Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>","ieee":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics and interactions of AAC3 in DPC are not functionally relevant,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.","ista":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural &#38; Molecular Biology. 25(9), 745–747.","mla":"Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9, Springer Nature, 2018, pp. 745–47, doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>.","chicago":"Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>.","short":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural &#38; Molecular Biology 25 (2018) 745–747."},"article_processing_charge":"No","page":"745-747","language":[{"iso":"eng"}],"oa_version":"None","quality_controlled":"1","month":"09","date_published":"2018-09-03T00:00:00Z","doi":"10.1038/s41594-018-0127-4","day":"03","publication_status":"published"},{"year":"2018","status":"public","publisher":"American Chemical Society","citation":{"ista":"Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 13(8), 2106–2113.","short":"C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi, A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.","mla":"Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>, vol. 13, no. 8, American Chemical Society, 2018, pp. 2106–13, doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>.","chicago":"Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>.","apa":"Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>","ama":"Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. 2018;13(8):2106-2113. doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>","ieee":"C. Laguri <i>et al.</i>, “Solid state NMR studies of intact lipopolysaccharide endotoxin,” <i>ACS Chemical Biology</i>, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018."},"article_processing_charge":"No","quality_controlled":"1","language":[{"iso":"eng"}],"page":"2106-2113","oa_version":"None","month":"07","date_published":"2018-07-02T00:00:00Z","publication_status":"published","doi":"10.1021/acschembio.8b00271","day":"02","volume":13,"type":"journal_article","date_updated":"2021-01-12T08:19:16Z","intvolume":"        13","abstract":[{"text":"Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly hampers their structural study in an environment similar to the bacterial surface. We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long O-antigen polysaccharides assembled in solution as vesicles or elongated micelles. Solid-state NMR with magic-angle spinning permitted the identification of NMR signals arising from regions with different flexibilities in the LPS, from the lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa LPS, for which we could confirm that a specific oligosaccharide is involved in the antibiotic binding. The possibility to study LPS alone and bound to a ligand when it is assembled in membrane-like structures opens great prospects for the investigation of proteins and antibiotics that specifically target such an important molecule at the surface of Gram-negative bacteria.","lang":"eng"}],"date_created":"2020-09-18T10:05:09Z","publication":"ACS Chemical Biology","publication_identifier":{"issn":["1554-8929","1554-8937"]},"author":[{"last_name":"Laguri","full_name":"Laguri, Cedric","first_name":"Cedric"},{"first_name":"Alba","full_name":"Silipo, Alba","last_name":"Silipo"},{"full_name":"Martorana, Alessandra M.","last_name":"Martorana","first_name":"Alessandra M."},{"first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda"},{"first_name":"Roberta","last_name":"Marchetti","full_name":"Marchetti, Roberta"},{"last_name":"Polissi","full_name":"Polissi, Alessandra","first_name":"Alessandra"},{"first_name":"Antonio","full_name":"Molinaro, Antonio","last_name":"Molinaro"},{"first_name":"Jean-Pierre","full_name":"Simorre, Jean-Pierre","last_name":"Simorre"}],"keyword":["Molecular Medicine","Biochemistry","General Medicine"],"article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Solid state NMR studies of intact lipopolysaccharide endotoxin","extern":"1","_id":"8439","issue":"8"},{"page":"8379-8393","quality_controlled":"1","language":[{"iso":"eng"}],"oa_version":"None","article_processing_charge":"No","day":"01","doi":"10.1074/jbc.ra118.002251","publication_status":"published","month":"06","date_published":"2018-06-01T00:00:00Z","year":"2018","citation":{"apa":"Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>","ama":"Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393. doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>","ieee":"K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018.","ista":"Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 293(22), 8379–8393.","short":"K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.","mla":"Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>.","chicago":"Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2018. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>."},"publisher":"American Society for Biochemistry & Molecular Biology","status":"public","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"author":[{"first_name":"Katharina","last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina"},{"first_name":"Martha","last_name":"Brennich","full_name":"Brennich, Martha"},{"first_name":"Uli","last_name":"Kazmaier","full_name":"Kazmaier, Uli"},{"last_name":"Lelievre","full_name":"Lelievre, Joel","first_name":"Joel"},{"full_name":"Ballell, Lluis","last_name":"Ballell","first_name":"Lluis"},{"first_name":"Alfred","last_name":"Goldberg","full_name":"Goldberg, Alfred"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"},{"first_name":"Hugo","last_name":"Fraga","full_name":"Fraga, Hugo"}],"_id":"8440","issue":"22","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","article_type":"original","date_updated":"2021-01-12T08:19:17Z","type":"journal_article","volume":293,"publication_identifier":{"issn":["0021-9258","1083-351X"]},"date_created":"2020-09-18T10:05:18Z","publication":"Journal of Biological Chemistry","intvolume":"       293","abstract":[{"text":"Mycobacterium tuberculosis can remain dormant in the host, an ability that explains the failure of many current tuberculosis treatments. Recently, the natural products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein substrates, such as proteins containing phosphorylated arginine residues, to the ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain. Cyclomarin binding to this domain specifically blocked these N-terminal dynamics. On the basis of these results, we propose a mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics, which modulates the chaperone enzymatic activity leading eventually to cell death.","lang":"eng"}]},{"year":"2018","status":"public","publisher":"Springer Nature","citation":{"chicago":"Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda, and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1007/s10858-018-0191-4\">https://doi.org/10.1007/s10858-018-0191-4</a>.","short":"A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter, Journal of Biomolecular NMR 71 (2018) 53–67.","mla":"Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.” <i>Journal of Biomolecular NMR</i>, vol. 71, no. 1, Springer Nature, 2018, pp. 53–67, doi:<a href=\"https://doi.org/10.1007/s10858-018-0191-4\">10.1007/s10858-018-0191-4</a>.","ista":"Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. 2018. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. Journal of Biomolecular NMR. 71(1), 53–67.","ieee":"A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter, “Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals,” <i>Journal of Biomolecular NMR</i>, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.","ama":"Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. <i>Journal of Biomolecular NMR</i>. 2018;71(1):53-67. doi:<a href=\"https://doi.org/10.1007/s10858-018-0191-4\">10.1007/s10858-018-0191-4</a>","apa":"Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., &#38; Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10858-018-0191-4\">https://doi.org/10.1007/s10858-018-0191-4</a>"},"article_processing_charge":"No","oa_version":"Published Version","quality_controlled":"1","language":[{"iso":"eng"}],"page":"53-67","month":"05","date_published":"2018-05-30T00:00:00Z","publication_status":"published","day":"30","doi":"10.1007/s10858-018-0191-4","volume":71,"type":"journal_article","date_updated":"2021-01-12T08:19:17Z","abstract":[{"lang":"eng","text":"Solid-state near-rotary-resonance measurements of the spin–lattice relaxation rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular dynamics in the microsecond time scale. The small difference between the spin-lock (SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions, at the same time it brings up some methodological challenges. In this work, several issues affecting correct measurements and analysis of 15N R1ρ data are considered in detail. Among them are signal amplitude as a function of the difference between SL and MAS frequencies, “dead time” in the initial part of the relaxation decay caused by transient spin-dynamic oscillations, measurements under HORROR condition and proper treatment of the multi-exponential relaxation decays. The multiple 15N R1ρ measurements at different SL fields and temperatures have been conducted in 1D mode (i.e. without site-specific resolution) for a set of four different microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin) to study the overall protein rocking in a crystal. While the amplitude of this motion varies very significantly, its correlation time for all four sample is practically the same, 30–50 μs. The amplitude of the rocking motion correlates with the packing density of a protein crystal. It has been suggested that the rocking motion is not diffusive but likely a jump-like dynamic process."}],"intvolume":"        71","date_created":"2020-09-18T10:05:28Z","publication":"Journal of Biomolecular NMR","publication_identifier":{"issn":["0925-2738","1573-5001"]},"author":[{"first_name":"Alexey","full_name":"Krushelnitsky, Alexey","last_name":"Krushelnitsky"},{"first_name":"Diego","last_name":"Gauto","full_name":"Gauto, Diego"},{"first_name":"Diana C.","last_name":"Rodriguez Camargo","full_name":"Rodriguez Camargo, Diana C."},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"},{"first_name":"Kay","full_name":"Saalwächter, Kay","last_name":"Saalwächter"}],"article_type":"original","title":"Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","issue":"1","_id":"8441","extern":"1"},{"keyword":["General Chemistry"],"author":[{"first_name":"Christophe","full_name":"Chipot, Christophe","last_name":"Chipot"},{"last_name":"Dehez","full_name":"Dehez, François","first_name":"François"},{"first_name":"Jason R.","full_name":"Schnell, Jason R.","last_name":"Schnell"},{"first_name":"Nicole","last_name":"Zitzmann","full_name":"Zitzmann, Nicole"},{"full_name":"Pebay-Peyroula, Eva","last_name":"Pebay-Peyroula","first_name":"Eva"},{"full_name":"Catoire, Laurent J.","last_name":"Catoire","first_name":"Laurent J."},{"full_name":"Miroux, Bruno","last_name":"Miroux","first_name":"Bruno"},{"first_name":"Edmund R. S.","full_name":"Kunji, Edmund R. S.","last_name":"Kunji"},{"last_name":"Veglia","full_name":"Veglia, Gianluigi","first_name":"Gianluigi"},{"first_name":"Timothy A.","full_name":"Cross, Timothy A.","last_name":"Cross"},{"last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul"}],"title":"Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","_id":"8442","issue":"7","article_type":"original","type":"journal_article","date_updated":"2021-01-12T08:19:18Z","volume":118,"publication":"Chemical Reviews","date_created":"2020-09-18T10:05:35Z","publication_identifier":{"issn":["0009-2665","1520-6890"]},"abstract":[{"lang":"eng","text":"Membrane proteins perform a host of vital cellular functions. Deciphering the molecular mechanisms whereby they fulfill these functions requires detailed biophysical and structural investigations. Detergents have proven pivotal to extract the protein from its native surroundings. Yet, they provide a milieu that departs significantly from that of the biological membrane, to the extent that the structure, the dynamics, and the interactions of membrane proteins in detergents may considerably vary, as compared to the native environment. Understanding the impact of detergents on membrane proteins is, therefore, crucial to assess the biological relevance of results obtained in detergents. Here, we review the strengths and weaknesses of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR studies of membrane proteins. While this class of detergents is often successful for membrane protein solubilization, a growing list of examples points to destabilizing and denaturing properties, in particular for α-helical membrane proteins. Our comprehensive analysis stresses the importance of stringent controls when working with this class of detergents and when analyzing the structure and dynamics of membrane proteins in alkyl phosphocholine detergents."}],"intvolume":"       118","quality_controlled":"1","language":[{"iso":"eng"}],"oa_version":"None","page":"3559-3607","article_processing_charge":"No","publication_status":"published","doi":"10.1021/acs.chemrev.7b00570","day":"28","month":"02","date_published":"2018-02-28T00:00:00Z","year":"2018","citation":{"chicago":"Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann, Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>.","mla":"Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>, vol. 118, no. 7, American Chemical Society, 2018, pp. 3559–607, doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>.","short":"C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire, B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118 (2018) 3559–3607.","ista":"Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ, Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.","ieee":"C. Chipot <i>et al.</i>, “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” <i>Chemical Reviews</i>, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018.","apa":"Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>","ama":"Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. 2018;118(7):3559-3607. doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>"},"status":"public","publisher":"American Chemical Society"},{"volume":9,"date_updated":"2021-01-12T08:19:18Z","type":"journal_article","abstract":[{"text":"Characterizing the structure of membrane proteins (MPs) generally requires extraction from their native environment, most commonly with detergents. Yet, the physicochemical properties of detergent micelles and lipid bilayers differ markedly and could alter the structural organization of MPs, albeit without general rules. Dodecylphosphocholine (DPC) is the most widely used detergent for MP structure determination by NMR, but the physiological relevance of several prominent structures has been questioned, though indirectly, by other biophysical techniques, e.g., functional/thermostability assay (TSA) and molecular dynamics (MD) simulations. Here, we resolve unambiguously this controversy by probing the functional relevance of three different mitochondrial carriers (MCs) in DPC at the atomic level, using an exhaustive set of solution-NMR experiments, complemented by functional/TSA and MD data. Our results provide atomic-level insight into the structure, substrate interaction and dynamics of the detergent–membrane protein complexes and demonstrates cogently that, while high-resolution NMR signals can be obtained for MCs in DPC, they systematically correspond to nonfunctional states.","lang":"eng"}],"intvolume":"         9","publication_identifier":{"issn":["1948-7185"]},"date_created":"2020-09-18T10:05:45Z","publication":"The Journal of Physical Chemistry Letters","keyword":["General Materials Science"],"author":[{"first_name":"Vilius","last_name":"Kurauskas","full_name":"Kurauskas, Vilius"},{"first_name":"Audrey","last_name":"Hessel","full_name":"Hessel, Audrey"},{"first_name":"Peixiang","full_name":"Ma, Peixiang","last_name":"Ma"},{"first_name":"Paola","last_name":"Lunetti","full_name":"Lunetti, Paola"},{"first_name":"Katharina","full_name":"Weinhäupl, Katharina","last_name":"Weinhäupl"},{"first_name":"Lionel","full_name":"Imbert, Lionel","last_name":"Imbert"},{"first_name":"Bernhard","full_name":"Brutscher, Bernhard","last_name":"Brutscher"},{"first_name":"Martin S.","last_name":"King","full_name":"King, Martin S."},{"first_name":"Rémy","last_name":"Sounier","full_name":"Sounier, Rémy"},{"first_name":"Vincenza","full_name":"Dolce, Vincenza","last_name":"Dolce"},{"last_name":"Kunji","full_name":"Kunji, Edmund R. S.","first_name":"Edmund R. S."},{"last_name":"Capobianco","full_name":"Capobianco, Loredana","first_name":"Loredana"},{"last_name":"Chipot","full_name":"Chipot, Christophe","first_name":"Christophe"},{"first_name":"François","full_name":"Dehez, François","last_name":"Dehez"},{"last_name":"Bersch","full_name":"Bersch, Beate","first_name":"Beate"},{"last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul"}],"article_type":"original","_id":"8443","issue":"5","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine","year":"2018","publisher":"American Chemical Society","status":"public","citation":{"ama":"Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. <i>The Journal of Physical Chemistry Letters</i>. 2018;9(5):933-938. doi:<a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">10.1021/acs.jpclett.8b00269</a>","apa":"Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L., … Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. <i>The Journal of Physical Chemistry Letters</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">https://doi.org/10.1021/acs.jpclett.8b00269</a>","ieee":"V. Kurauskas <i>et al.</i>, “How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine,” <i>The Journal of Physical Chemistry Letters</i>, vol. 9, no. 5. American Chemical Society, pp. 933–938, 2018.","ista":"Kurauskas V, Hessel A, Ma P, Lunetti P, Weinhäupl K, Imbert L, Brutscher B, King MS, Sounier R, Dolce V, Kunji ERS, Capobianco L, Chipot C, Dehez F, Bersch B, Schanda P. 2018. How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry Letters. 9(5), 933–938.","short":"V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher, M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez, B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.","mla":"Kurauskas, Vilius, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.” <i>The Journal of Physical Chemistry Letters</i>, vol. 9, no. 5, American Chemical Society, 2018, pp. 933–38, doi:<a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">10.1021/acs.jpclett.8b00269</a>.","chicago":"Kurauskas, Vilius, Audrey Hessel, Peixiang Ma, Paola Lunetti, Katharina Weinhäupl, Lionel Imbert, Bernhard Brutscher, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.” <i>The Journal of Physical Chemistry Letters</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">https://doi.org/10.1021/acs.jpclett.8b00269</a>."},"article_processing_charge":"No","language":[{"iso":"eng"}],"page":"933-938","oa_version":"None","quality_controlled":"1","month":"02","date_published":"2018-02-03T00:00:00Z","day":"03","doi":"10.1021/acs.jpclett.8b00269","publication_status":"published"},{"intvolume":"     11014","publist_id":"7969","volume":11014,"external_id":{"isi":["000851042300031"]},"_id":"85","alternative_title":["LNCS"],"author":[{"first_name":"Eran","last_name":"Gilad","full_name":"Gilad, Eran"},{"first_name":"Trevor A","full_name":"Brown, Trevor A","id":"3569F0A0-F248-11E8-B48F-1D18A9856A87","last_name":"Brown"},{"last_name":"Oskin","full_name":"Oskin, Mark","first_name":"Mark"},{"first_name":"Yoav","full_name":"Etsion, Yoav","last_name":"Etsion"}],"isi":1,"publisher":"Springer","project":[{"_id":"26450934-B435-11E9-9278-68D0E5697425","name":"NSERC Postdoctoral fellowship"}],"ddc":["000"],"year":"2018","date_published":"2018-08-01T00:00:00Z","article_processing_charge":"No","page":"465 - 479","abstract":[{"text":"Concurrent accesses to shared data structures must be synchronized to avoid data races. Coarse-grained synchronization, which locks the entire data structure, is easy to implement but does not scale. Fine-grained synchronization can scale well, but can be hard to reason about. Hand-over-hand locking, in which operations are pipelined as they traverse the data structure, combines fine-grained synchronization with ease of use. However, the traditional implementation suffers from inherent overheads. This paper introduces snapshot-based synchronization (SBS), a novel hand-over-hand locking mechanism. SBS decouples the synchronization state from the data, significantly improving cache utilization. Further, it relies on guarantees provided by pipelining to minimize synchronization that requires cross-thread communication. Snapshot-based synchronization thus scales much better than traditional hand-over-hand locking, while maintaining the same ease of use.","lang":"eng"}],"publication_identifier":{"issn":["0302-9743"]},"date_created":"2018-12-11T11:44:33Z","file_date_updated":"2020-07-14T12:48:14Z","date_updated":"2026-04-16T09:53:41Z","type":"conference","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","title":"Snapshot based synchronization: A fast replacement for Hand-over-Hand locking","conference":{"end_date":"2018-08-31","location":"Turin, Italy","start_date":"2018-08-27","name":"Euro-Par: European Conference on Parallel Processing"},"has_accepted_license":"1","oa":1,"status":"public","file":[{"access_level":"open_access","content_type":"application/pdf","checksum":"13a3f250be8878405e791b53c19722ad","relation":"main_file","date_created":"2019-02-12T07:40:40Z","file_id":"5954","file_name":"2018_Brown.pdf","date_updated":"2020-07-14T12:48:14Z","creator":"dernst","file_size":665372}],"citation":{"apa":"Gilad, E., Brown, T. A., Oskin, M., &#38; Etsion, Y. (2018). Snapshot based synchronization: A fast replacement for Hand-over-Hand locking (Vol. 11014, pp. 465–479). Presented at the Euro-Par: European Conference on Parallel Processing, Turin, Italy: Springer. <a href=\"https://doi.org/10.1007/978-3-319-96983-1_33\">https://doi.org/10.1007/978-3-319-96983-1_33</a>","ama":"Gilad E, Brown TA, Oskin M, Etsion Y. Snapshot based synchronization: A fast replacement for Hand-over-Hand locking. In: Vol 11014. Springer; 2018:465-479. doi:<a href=\"https://doi.org/10.1007/978-3-319-96983-1_33\">10.1007/978-3-319-96983-1_33</a>","ieee":"E. Gilad, T. A. Brown, M. Oskin, and Y. Etsion, “Snapshot based synchronization: A fast replacement for Hand-over-Hand locking,” presented at the Euro-Par: European Conference on Parallel Processing, Turin, Italy, 2018, vol. 11014, pp. 465–479.","ista":"Gilad E, Brown TA, Oskin M, Etsion Y. 2018. Snapshot based synchronization: A fast replacement for Hand-over-Hand locking. Euro-Par: European Conference on Parallel Processing, LNCS, vol. 11014, 465–479.","chicago":"Gilad, Eran, Trevor A Brown, Mark Oskin, and Yoav Etsion. “Snapshot Based Synchronization: A Fast Replacement for Hand-over-Hand Locking,” 11014:465–79. Springer, 2018. <a href=\"https://doi.org/10.1007/978-3-319-96983-1_33\">https://doi.org/10.1007/978-3-319-96983-1_33</a>.","short":"E. Gilad, T.A. Brown, M. Oskin, Y. Etsion, in:, Springer, 2018, pp. 465–479.","mla":"Gilad, Eran, et al. <i>Snapshot Based Synchronization: A Fast Replacement for Hand-over-Hand Locking</i>. Vol. 11014, Springer, 2018, pp. 465–79, doi:<a href=\"https://doi.org/10.1007/978-3-319-96983-1_33\">10.1007/978-3-319-96983-1_33</a>."},"scopus_import":"1","acknowledgement":"Trevor Brown was supported in part by the ISF (grants 2005/17 & 1749/14) and by a NSERC post-doctoral fellowship.","month":"08","day":"01","doi":"10.1007/978-3-319-96983-1_33","department":[{"_id":"DaAl"}],"publication_status":"published","language":[{"iso":"eng"}],"quality_controlled":"1","oa_version":"Preprint"},{"oa_version":"Preprint","language":[{"iso":"eng"}],"article_processing_charge":"No","ec_funded":1,"doi":"10.1101/494088","day":"13","publication_status":"submitted","department":[{"_id":"SiHi"}],"month":"12","date_published":"2018-12-13T00:00:00Z","year":"2018","acknowledgement":"We thank I. Andrew and S.E. Bae for excellent technical assistance, F. Gage for plasmids, and K. Nave (Nex-Cre) for mouse colonies. We thank members of the Marín and Rico laboratories for stimulating discussions and ideas. Our research on this topic is supported by grants from the European Research Council (ERC-2017-AdG 787355 to O.M and ERC2016-CoG 725780 to S.H.) and Wellcome Trust (103714MA) to O.M. L.L. was the recipient of an EMBO long-term postdoctoral fellowship, R.B. received support from FWF Lise-Meitner program (M 2416) and F.K.W. was supported by an EMBO postdoctoral fellowship and is currently a Marie Skłodowska-Curie Fellow from the European Commission under the H2020 Programme.","citation":{"ieee":"A. Llorca <i>et al.</i>, “Heterogeneous progenitor cell behaviors underlie the assembly of neocortical cytoarchitecture,” <i>bioRxiv</i>. Cold Spring Harbor Laboratory.","ama":"Llorca A, Ciceri G, Beattie RJ, et al. Heterogeneous progenitor cell behaviors underlie the assembly of neocortical cytoarchitecture. <i>bioRxiv</i>. doi:<a href=\"https://doi.org/10.1101/494088\">10.1101/494088</a>","apa":"Llorca, A., Ciceri, G., Beattie, R. J., Wong, F. K., Diana, G., Serafeimidou, E., … Marín, O. (n.d.). Heterogeneous progenitor cell behaviors underlie the assembly of neocortical cytoarchitecture. <i>bioRxiv</i>. Cold Spring Harbor Laboratory. <a href=\"https://doi.org/10.1101/494088\">https://doi.org/10.1101/494088</a>","mla":"Llorca, Alfredo, et al. “Heterogeneous Progenitor Cell Behaviors Underlie the Assembly of Neocortical Cytoarchitecture.” <i>BioRxiv</i>, Cold Spring Harbor Laboratory, doi:<a href=\"https://doi.org/10.1101/494088\">10.1101/494088</a>.","chicago":"Llorca, Alfredo, Gabriele Ciceri, Robert J Beattie, Fong K. Wong, Giovanni Diana, Eleni Serafeimidou, Marian Fernández-Otero, et al. “Heterogeneous Progenitor Cell Behaviors Underlie the Assembly of Neocortical Cytoarchitecture.” <i>BioRxiv</i>. Cold Spring Harbor Laboratory, n.d. <a href=\"https://doi.org/10.1101/494088\">https://doi.org/10.1101/494088</a>.","short":"A. Llorca, G. Ciceri, R.J. Beattie, F.K. Wong, G. Diana, E. Serafeimidou, M. Fernández-Otero, C. Streicher, S.J. Arnold, M. Meyer, S. Hippenmeyer, M. Maravall, O. Marín, BioRxiv (n.d.).","ista":"Llorca A, Ciceri G, Beattie RJ, Wong FK, Diana G, Serafeimidou E, Fernández-Otero M, Streicher C, Arnold SJ, Meyer M, Hippenmeyer S, Maravall M, Marín O. Heterogeneous progenitor cell behaviors underlie the assembly of neocortical cytoarchitecture. bioRxiv, <a href=\"https://doi.org/10.1101/494088\">10.1101/494088</a>."},"publisher":"Cold Spring Harbor Laboratory","status":"public","project":[{"grant_number":"725780","name":"Principles of Neural Stem Cell Lineage Progression in Cerebral Cortex Development","call_identifier":"H2020","_id":"260018B0-B435-11E9-9278-68D0E5697425"},{"_id":"264E56E2-B435-11E9-9278-68D0E5697425","name":"Molecular Mechanisms Regulating Gliogenesis in the Neocortex","call_identifier":"FWF","grant_number":"M02416"}],"main_file_link":[{"url":"https://doi.org/10.1101/494088","open_access":"1"}],"oa":1,"author":[{"first_name":"Alfredo","full_name":"Llorca, Alfredo","last_name":"Llorca"},{"first_name":"Gabriele","full_name":"Ciceri, Gabriele","last_name":"Ciceri"},{"orcid":"0000-0002-8483-8753","first_name":"Robert J","full_name":"Beattie, Robert J","id":"2E26DF60-F248-11E8-B48F-1D18A9856A87","last_name":"Beattie"},{"full_name":"Wong, Fong K.","last_name":"Wong","first_name":"Fong K."},{"first_name":"Giovanni","last_name":"Diana","full_name":"Diana, Giovanni"},{"last_name":"Serafeimidou","full_name":"Serafeimidou, Eleni","first_name":"Eleni"},{"full_name":"Fernández-Otero, Marian","last_name":"Fernández-Otero","first_name":"Marian"},{"first_name":"Carmen","last_name":"Streicher","full_name":"Streicher, Carmen","id":"36BCB99C-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Sebastian J.","last_name":"Arnold","full_name":"Arnold, Sebastian J."},{"first_name":"Martin","full_name":"Meyer, Martin","last_name":"Meyer"},{"orcid":"0000-0003-2279-1061","first_name":"Simon","last_name":"Hippenmeyer","full_name":"Hippenmeyer, Simon","id":"37B36620-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Miguel","full_name":"Maravall, Miguel","last_name":"Maravall"},{"full_name":"Marín, Oscar","last_name":"Marín","first_name":"Oscar"}],"_id":"8547","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Heterogeneous progenitor cell behaviors underlie the assembly of neocortical cytoarchitecture","date_updated":"2024-10-22T10:46:39Z","type":"preprint","date_created":"2020-09-21T12:01:50Z","publication":"bioRxiv","abstract":[{"text":"The cerebral cortex contains multiple hierarchically organized areas with distinctive cytoarchitectonical patterns, but the cellular mechanisms underlying the emergence of this diversity remain unclear. Here, we have quantitatively investigated the neuronal output of individual progenitor cells in the ventricular zone of the developing mouse neocortex using a combination of methods that together circumvent the biases and limitations of individual approaches. We found that individual cortical progenitor cells show a high degree of stochasticity and generate pyramidal cell lineages that adopt a wide range of laminar configurations. Mathematical modelling these lineage data suggests that a small number of progenitor cell populations, each generating pyramidal cells following different stochastic developmental programs, suffice to generate the heterogenous complement of pyramidal cell lineages that collectively build the complex cytoarchitecture of the neocortex.","lang":"eng"}]},{"date_created":"2018-12-11T11:44:33Z","publication":"Principles of Modeling","abstract":[{"lang":"eng","text":"Responsiveness—the requirement that every request to a system be eventually handled—is one of the fundamental liveness properties of a reactive system. Average response time is a quantitative measure for the responsiveness requirement used commonly in performance evaluation. We show how average response time can be computed on state-transition graphs, on Markov chains, and on game graphs. In all three cases, we give polynomial-time algorithms."}],"date_updated":"2025-04-15T06:26:15Z","type":"book_chapter","file_date_updated":"2020-07-14T12:48:14Z","title":"Computing average response time","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","has_accepted_license":"1","oa":1,"citation":{"ieee":"K. Chatterjee, T. A. Henzinger, and J. Otop, “Computing average response time,” in <i>Principles of Modeling</i>, vol. 10760, M. Lohstroh, P. Derler, and M. Sirjani, Eds. Springer, 2018, pp. 143–161.","ama":"Chatterjee K, Henzinger TA, Otop J. Computing average response time. In: Lohstroh M, Derler P, Sirjani M, eds. <i>Principles of Modeling</i>. Vol 10760. Springer; 2018:143-161. doi:<a href=\"https://doi.org/10.1007/978-3-319-95246-8_9\">10.1007/978-3-319-95246-8_9</a>","apa":"Chatterjee, K., Henzinger, T. A., &#38; Otop, J. (2018). Computing average response time. In M. Lohstroh, P. Derler, &#38; M. Sirjani (Eds.), <i>Principles of Modeling</i> (Vol. 10760, pp. 143–161). Springer. <a href=\"https://doi.org/10.1007/978-3-319-95246-8_9\">https://doi.org/10.1007/978-3-319-95246-8_9</a>","mla":"Chatterjee, Krishnendu, et al. “Computing Average Response Time.” <i>Principles of Modeling</i>, edited by Marten Lohstroh et al., vol. 10760, Springer, 2018, pp. 143–61, doi:<a href=\"https://doi.org/10.1007/978-3-319-95246-8_9\">10.1007/978-3-319-95246-8_9</a>.","short":"K. Chatterjee, T.A. Henzinger, J. Otop, in:, M. Lohstroh, P. Derler, M. Sirjani (Eds.), Principles of Modeling, Springer, 2018, pp. 143–161.","chicago":"Chatterjee, Krishnendu, Thomas A Henzinger, and Jan Otop. “Computing Average Response Time.” In <i>Principles of Modeling</i>, edited by Marten Lohstroh, Patricia Derler, and Marjan Sirjani, 10760:143–61. Springer, 2018. <a href=\"https://doi.org/10.1007/978-3-319-95246-8_9\">https://doi.org/10.1007/978-3-319-95246-8_9</a>.","ista":"Chatterjee K, Henzinger TA, Otop J. 2018.Computing average response time. In: Principles of Modeling. LNCS, vol. 10760, 143–161."},"file":[{"content_type":"application/pdf","checksum":"9995c6ce6957333baf616fc4f20be597","relation":"main_file","access_level":"open_access","date_updated":"2020-07-14T12:48:14Z","creator":"dernst","file_size":516307,"date_created":"2019-11-19T08:22:18Z","file_id":"7053","file_name":"2018_PrinciplesModeling_Chatterjee.pdf"}],"status":"public","scopus_import":1,"acknowledgement":"This research was supported in part by the Austrian Science Fund (FWF) under grants S11402-N23, S11407-N23 (RiSE/SHiNE) and Z211-N23 (Wittgenstein Award), ERC Start grant (279307: Graph Games), Vienna Science and Technology Fund (WWTF) through project ICT15-003 and by the National Science Centre (NCN), Poland under grant 2014/15/D/ST6/04543.","day":"20","ec_funded":1,"doi":"10.1007/978-3-319-95246-8_9","publication_status":"published","department":[{"_id":"KrCh"},{"_id":"ToHe"}],"month":"07","language":[{"iso":"eng"}],"quality_controlled":"1","oa_version":"Submitted Version","publist_id":"7968","intvolume":"     10760","volume":10760,"_id":"86","alternative_title":["LNCS"],"author":[{"first_name":"Krishnendu","orcid":"0000-0002-4561-241X","last_name":"Chatterjee","id":"2E5DCA20-F248-11E8-B48F-1D18A9856A87","full_name":"Chatterjee, Krishnendu"},{"orcid":"0000−0002−2985−7724","first_name":"Thomas A","full_name":"Henzinger, Thomas A","id":"40876CD8-F248-11E8-B48F-1D18A9856A87","last_name":"Henzinger"},{"last_name":"Otop","full_name":"Otop, Jan","id":"2FC5DA74-F248-11E8-B48F-1D18A9856A87","first_name":"Jan"}],"ddc":["000"],"publisher":"Springer","project":[{"_id":"25832EC2-B435-11E9-9278-68D0E5697425","grant_number":"S 11407_N23","name":"Rigorous Systems Engineering","call_identifier":"FWF"},{"_id":"25863FF4-B435-11E9-9278-68D0E5697425","call_identifier":"FWF","name":"Game Theory","grant_number":"S11407"},{"name":"Formal methods for the design and analysis of complex systems","call_identifier":"FWF","grant_number":"Z211","_id":"25F42A32-B435-11E9-9278-68D0E5697425"},{"grant_number":"279307","name":"Quantitative Graph Games: Theory and Applications","call_identifier":"FP7","_id":"2581B60A-B435-11E9-9278-68D0E5697425"},{"_id":"25892FC0-B435-11E9-9278-68D0E5697425","name":"Efficient Algorithms for Computer Aided Verification","grant_number":"ICT15-003"}],"year":"2018","date_published":"2018-07-20T00:00:00Z","editor":[{"first_name":"Marten","last_name":"Lohstroh","full_name":"Lohstroh, Marten"},{"full_name":"Derler, Patricia","last_name":"Derler","first_name":"Patricia"},{"first_name":"Marjan","last_name":"Sirjani","full_name":"Sirjani, Marjan"}],"page":"143 - 161"},{"volume":8,"intvolume":"         8","author":[{"first_name":"Carola","last_name":"Gregor","full_name":"Gregor, Carola"},{"last_name":"Sidenstein","full_name":"Sidenstein, Sven C.","first_name":"Sven C."},{"full_name":"Andresen, Martin","last_name":"Andresen","first_name":"Martin"},{"first_name":"Steffen J.","last_name":"Sahl","full_name":"Sahl, Steffen J."},{"full_name":"Danzl, Johann G","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","last_name":"Danzl","orcid":"0000-0001-8559-3973","first_name":"Johann G"},{"first_name":"Stefan W.","full_name":"Hell, Stefan W.","last_name":"Hell"}],"isi":1,"_id":"8618","external_id":{"pmid":["29426833"],"isi":["000424630400037"]},"year":"2018","article_number":"2724","ddc":["570"],"publisher":"Springer Nature","article_processing_charge":"No","date_published":"2018-02-09T00:00:00Z","pmid":1,"type":"journal_article","date_updated":"2024-10-21T06:02:43Z","file_date_updated":"2020-10-06T16:35:16Z","date_created":"2020-10-06T16:33:37Z","publication":"Scientific Reports","publication_identifier":{"issn":["2045-2322"]},"abstract":[{"lang":"eng","text":"The reversibly switchable fluorescent proteins (RSFPs) commonly used for RESOLFT nanoscopy have been developed from fluorescent proteins of the GFP superfamily. These proteins are bright, but exhibit several drawbacks such as relatively large size, oxygen-dependence, sensitivity to low pH, and limited switching speed. Therefore, RSFPs from other origins with improved properties need to be explored. Here, we report the development of two RSFPs based on the LOV domain of the photoreceptor protein YtvA from Bacillus subtilis. LOV domains obtain their fluorescence by association with the abundant cellular cofactor flavin mononucleotide (FMN). Under illumination with blue and ultraviolet light, they undergo a photocycle, making these proteins inherently photoswitchable. Our first improved variant, rsLOV1, can be used for RESOLFT imaging, whereas rsLOV2 proved useful for STED nanoscopy of living cells with a resolution of down to 50 nm. In addition to their smaller size compared to GFP-related proteins (17 kDa instead of 27 kDa) and their usability at low pH, rsLOV1 and rsLOV2 exhibit faster switching kinetics, switching on and off 3 times faster than rsEGFP2, the fastest-switching RSFP reported to date. Therefore, LOV-domain-based RSFPs have potential for applications where the switching speed of GFP-based proteins is limiting."}],"oa":1,"has_accepted_license":"1","keyword":["Multidisciplinary"],"title":"Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from the bacterial photoreceptor YtvA","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","article_type":"original","scopus_import":"1","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"citation":{"mla":"Gregor, Carola, et al. “Novel Reversibly Switchable Fluorescent Proteins for RESOLFT and STED Nanoscopy Engineered from the Bacterial Photoreceptor YtvA.” <i>Scientific Reports</i>, vol. 8, 2724, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41598-018-19947-1\">10.1038/s41598-018-19947-1</a>.","chicago":"Gregor, Carola, Sven C. Sidenstein, Martin Andresen, Steffen J. Sahl, Johann G Danzl, and Stefan W. Hell. “Novel Reversibly Switchable Fluorescent Proteins for RESOLFT and STED Nanoscopy Engineered from the Bacterial Photoreceptor YtvA.” <i>Scientific Reports</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41598-018-19947-1\">https://doi.org/10.1038/s41598-018-19947-1</a>.","short":"C. Gregor, S.C. Sidenstein, M. Andresen, S.J. Sahl, J.G. Danzl, S.W. Hell, Scientific Reports 8 (2018).","ista":"Gregor C, Sidenstein SC, Andresen M, Sahl SJ, Danzl JG, Hell SW. 2018. Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from the bacterial photoreceptor YtvA. Scientific Reports. 8, 2724.","ieee":"C. Gregor, S. C. Sidenstein, M. Andresen, S. J. Sahl, J. G. Danzl, and S. W. Hell, “Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from the bacterial photoreceptor YtvA,” <i>Scientific Reports</i>, vol. 8. Springer Nature, 2018.","apa":"Gregor, C., Sidenstein, S. C., Andresen, M., Sahl, S. J., Danzl, J. G., &#38; Hell, S. W. (2018). Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from the bacterial photoreceptor YtvA. <i>Scientific Reports</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41598-018-19947-1\">https://doi.org/10.1038/s41598-018-19947-1</a>","ama":"Gregor C, Sidenstein SC, Andresen M, Sahl SJ, Danzl JG, Hell SW. Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from the bacterial photoreceptor YtvA. <i>Scientific Reports</i>. 2018;8. doi:<a href=\"https://doi.org/10.1038/s41598-018-19947-1\">10.1038/s41598-018-19947-1</a>"},"file":[{"creator":"dernst","file_size":2818077,"date_updated":"2020-10-06T16:35:16Z","file_name":"2018_ScientificReports_Gregor.pdf","date_created":"2020-10-06T16:35:16Z","file_id":"8619","checksum":"e642080fcbde9584c63544f587c74f03","relation":"main_file","content_type":"application/pdf","access_level":"open_access","success":1}],"status":"public","oa_version":"Published Version","quality_controlled":"1","language":[{"iso":"eng"}],"publication_status":"published","department":[{"_id":"JoDa"}],"day":"09","doi":"10.1038/s41598-018-19947-1","month":"02"},{"author":[{"first_name":"Herbert","orcid":"0000-0002-9823-6833","last_name":"Edelsbrunner","id":"3FB178DA-F248-11E8-B48F-1D18A9856A87","full_name":"Edelsbrunner, Herbert"},{"orcid":"0000-0002-0659-3201","first_name":"Anton","full_name":"Nikitenko, Anton","id":"3E4FF1BA-F248-11E8-B48F-1D18A9856A87","last_name":"Nikitenko"}],"isi":1,"_id":"87","external_id":{"isi":["000442893500018"],"arxiv":["1705.02870"]},"issue":"5","volume":28,"publist_id":"7967","intvolume":"        28","page":"3215 - 3238","article_processing_charge":"No","date_published":"2018-10-01T00:00:00Z","year":"2018","project":[{"_id":"2561EBF4-B435-11E9-9278-68D0E5697425","grant_number":"I02979-N35","name":"Persistence and stability of geometric complexes","call_identifier":"FWF"}],"publisher":"Institute of Mathematical Statistics","oa":1,"title":"Random inscribed polytopes have similar radius functions as Poisson-Delaunay mosaics","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","article_type":"original","type":"journal_article","date_updated":"2026-04-08T14:19:30Z","publication":"Annals of Applied Probability","date_created":"2018-12-11T11:44:33Z","abstract":[{"lang":"eng","text":"Using the geodesic distance on the n-dimensional sphere, we study the expected radius function of the Delaunay mosaic of a random set of points. Specifically, we consider the partition of the mosaic into intervals of the radius function and determine the expected number of intervals whose radii are less than or equal to a given threshold. We find that the expectations are essentially the same as for the Poisson–Delaunay mosaic in n-dimensional Euclidean space. Assuming the points are not contained in a hemisphere, the Delaunay mosaic is isomorphic to the boundary complex of the convex hull in Rn+1, so we also get the expected number of faces of a random inscribed polytope. As proved in Antonelli et al. [Adv. in Appl. Probab. 9–12 (1977–1980)], an orthant section of the n-sphere is isometric to the standard n-simplex equipped with the Fisher information metric. It follows that the latter space has similar stochastic properties as the n-dimensional Euclidean space. Our results are therefore relevant in information geometry and in population genetics."}],"language":[{"iso":"eng"}],"quality_controlled":"1","oa_version":"Preprint","arxiv":1,"department":[{"_id":"HeEd"}],"publication_status":"published","doi":"10.1214/18-AAP1389","day":"01","related_material":{"record":[{"relation":"dissertation_contains","id":"6287","status":"public"}]},"month":"10","scopus_import":"1","citation":{"apa":"Edelsbrunner, H., &#38; Nikitenko, A. (2018). Random inscribed polytopes have similar radius functions as Poisson-Delaunay mosaics. <i>Annals of Applied Probability</i>. Institute of Mathematical Statistics. <a href=\"https://doi.org/10.1214/18-AAP1389\">https://doi.org/10.1214/18-AAP1389</a>","ama":"Edelsbrunner H, Nikitenko A. Random inscribed polytopes have similar radius functions as Poisson-Delaunay mosaics. <i>Annals of Applied Probability</i>. 2018;28(5):3215-3238. doi:<a href=\"https://doi.org/10.1214/18-AAP1389\">10.1214/18-AAP1389</a>","ieee":"H. Edelsbrunner and A. Nikitenko, “Random inscribed polytopes have similar radius functions as Poisson-Delaunay mosaics,” <i>Annals of Applied Probability</i>, vol. 28, no. 5. Institute of Mathematical Statistics, pp. 3215–3238, 2018.","ista":"Edelsbrunner H, Nikitenko A. 2018. Random inscribed polytopes have similar radius functions as Poisson-Delaunay mosaics. Annals of Applied Probability. 28(5), 3215–3238.","chicago":"Edelsbrunner, Herbert, and Anton Nikitenko. “Random Inscribed Polytopes Have Similar Radius Functions as Poisson-Delaunay Mosaics.” <i>Annals of Applied Probability</i>. Institute of Mathematical Statistics, 2018. <a href=\"https://doi.org/10.1214/18-AAP1389\">https://doi.org/10.1214/18-AAP1389</a>.","mla":"Edelsbrunner, Herbert, and Anton Nikitenko. “Random Inscribed Polytopes Have Similar Radius Functions as Poisson-Delaunay Mosaics.” <i>Annals of Applied Probability</i>, vol. 28, no. 5, Institute of Mathematical Statistics, 2018, pp. 3215–38, doi:<a href=\"https://doi.org/10.1214/18-AAP1389\">10.1214/18-AAP1389</a>.","short":"H. Edelsbrunner, A. Nikitenko, Annals of Applied Probability 28 (2018) 3215–3238."},"status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1705.02870","open_access":"1"}]},{"volume":14,"intvolume":"        14","author":[{"first_name":"Antoine","last_name":"Aubret","full_name":"Aubret, Antoine"},{"orcid":"0000-0002-7253-9465","first_name":"Jérémie A","full_name":"Palacci, Jérémie A","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","last_name":"Palacci"}],"_id":"9053","issue":"47","extern":"1","external_id":{"arxiv":["1909.11121"],"pmid":["30456407"]},"year":"2018","publisher":"Royal Society of Chemistry ","page":"9577-9588","article_processing_charge":"No","pmid":1,"date_published":"2018-12-21T00:00:00Z","date_updated":"2023-02-23T13:47:43Z","type":"journal_article","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"publication":"Soft Matter","date_created":"2021-02-01T13:44:41Z","abstract":[{"lang":"eng","text":"The development of strategies to assemble microscopic machines from dissipative building blocks are essential on the route to novel active materials. We recently demonstrated the hierarchical self-assembly of phoretic microswimmers into self-spinning microgears and their synchronization by diffusiophoretic interactions [Aubret et al., Nat. Phys., 2018]. In this paper, we adopt a pedagogical approach and expose our strategy to control self-assembly and build machines using phoretic phenomena. We notably introduce Highly Inclined Laminated Optical sheets microscopy (HILO) to image and characterize anisotropic and dynamic diffusiophoretic interactions, which cannot be performed by conventional fluorescence microscopy. The dynamics of a (haematite) photocatalytic material immersed in (hydrogen peroxide) fuel under various illumination patterns is first described and quantitatively rationalized by a model of diffusiophoresis, the migration of a colloidal particle in a concentration gradient. It is further exploited to design phototactic microswimmers that direct towards the high intensity of light, as a result of the reorientation of the haematite in a light gradient. We finally show the assembly of self-spinning microgears from colloidal microswimmers and carefully characterize the interactions using HILO techniques. The results are compared with analytical and numerical predictions and agree quantitatively, stressing the important role played by concentration gradients induced by chemical activity to control and design interactions. Because the approach described hereby is generic, this works paves the way for the rational design of machines by controlling phoretic phenomena."}],"oa":1,"keyword":["General Chemistry","Condensed Matter Physics"],"title":"Diffusiophoretic design of self-spinning microgears from colloidal microswimmers","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","article_type":"original","scopus_import":"1","citation":{"ieee":"A. Aubret and J. A. Palacci, “Diffusiophoretic design of self-spinning microgears from colloidal microswimmers,” <i>Soft Matter</i>, vol. 14, no. 47. Royal Society of Chemistry , pp. 9577–9588, 2018.","apa":"Aubret, A., &#38; Palacci, J. A. (2018). Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. <i>Soft Matter</i>. Royal Society of Chemistry . <a href=\"https://doi.org/10.1039/c8sm01760c\">https://doi.org/10.1039/c8sm01760c</a>","ama":"Aubret A, Palacci JA. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. <i>Soft Matter</i>. 2018;14(47):9577-9588. doi:<a href=\"https://doi.org/10.1039/c8sm01760c\">10.1039/c8sm01760c</a>","short":"A. Aubret, J.A. Palacci, Soft Matter 14 (2018) 9577–9588.","mla":"Aubret, Antoine, and Jérémie A. Palacci. “Diffusiophoretic Design of Self-Spinning Microgears from Colloidal Microswimmers.” <i>Soft Matter</i>, vol. 14, no. 47, Royal Society of Chemistry , 2018, pp. 9577–88, doi:<a href=\"https://doi.org/10.1039/c8sm01760c\">10.1039/c8sm01760c</a>.","chicago":"Aubret, Antoine, and Jérémie A Palacci. “Diffusiophoretic Design of Self-Spinning Microgears from Colloidal Microswimmers.” <i>Soft Matter</i>. Royal Society of Chemistry , 2018. <a href=\"https://doi.org/10.1039/c8sm01760c\">https://doi.org/10.1039/c8sm01760c</a>.","ista":"Aubret A, Palacci JA. 2018. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. Soft Matter. 14(47), 9577–9588."},"status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1909.11121","open_access":"1"}],"quality_controlled":"1","language":[{"iso":"eng"}],"oa_version":"Preprint","arxiv":1,"doi":"10.1039/c8sm01760c","day":"21","publication_status":"published","month":"12"},{"language":[{"iso":"eng"}],"oa_version":"Preprint","quality_controlled":"1","arxiv":1,"doi":"10.1038/s41567-018-0227-4","day":"01","publication_status":"published","month":"11","scopus_import":"1","citation":{"ista":"Aubret A, Youssef M, Sacanna S, Palacci JA. 2018. Targeted assembly and synchronization of self-spinning microgears. Nature Physics. 14(11), 1114–1118.","short":"A. Aubret, M. Youssef, S. Sacanna, J.A. Palacci, Nature Physics 14 (2018) 1114–1118.","mla":"Aubret, Antoine, et al. “Targeted Assembly and Synchronization of Self-Spinning Microgears.” <i>Nature Physics</i>, vol. 14, no. 11, Springer Nature, 2018, pp. 1114–18, doi:<a href=\"https://doi.org/10.1038/s41567-018-0227-4\">10.1038/s41567-018-0227-4</a>.","chicago":"Aubret, Antoine, Mena Youssef, Stefano Sacanna, and Jérémie A Palacci. “Targeted Assembly and Synchronization of Self-Spinning Microgears.” <i>Nature Physics</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41567-018-0227-4\">https://doi.org/10.1038/s41567-018-0227-4</a>.","ama":"Aubret A, Youssef M, Sacanna S, Palacci JA. Targeted assembly and synchronization of self-spinning microgears. <i>Nature Physics</i>. 2018;14(11):1114-1118. doi:<a href=\"https://doi.org/10.1038/s41567-018-0227-4\">10.1038/s41567-018-0227-4</a>","apa":"Aubret, A., Youssef, M., Sacanna, S., &#38; Palacci, J. A. (2018). Targeted assembly and synchronization of self-spinning microgears. <i>Nature Physics</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41567-018-0227-4\">https://doi.org/10.1038/s41567-018-0227-4</a>","ieee":"A. Aubret, M. Youssef, S. Sacanna, and J. A. Palacci, “Targeted assembly and synchronization of self-spinning microgears,” <i>Nature Physics</i>, vol. 14, no. 11. Springer Nature, pp. 1114–1118, 2018."},"status":"public","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1810.01033"}],"oa":1,"title":"Targeted assembly and synchronization of self-spinning microgears","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","article_type":"original","date_updated":"2023-02-23T13:48:02Z","type":"journal_article","publication_identifier":{"eissn":["1745-2481"],"issn":["1745-2473"]},"date_created":"2021-02-02T13:52:49Z","publication":"Nature Physics","abstract":[{"lang":"eng","text":"Self-assembly is the autonomous organization of components into patterns or structures: an essential ingredient of biology and a desired route to complex organization1. At equilibrium, the structure is encoded through specific interactions2,3,4,5,6,7,8, at an unfavourable entropic cost for the system. An alternative approach, widely used by nature, uses energy input to bypass the entropy bottleneck and develop features otherwise impossible at equilibrium9. Dissipative building blocks that inject energy locally were made available by recent advances in colloidal science10,11 but have not been used to control self-assembly. Here we show the targeted formation of self-powered microgears from active particles and their autonomous synchronization into dynamical superstructures. We use a photoactive component that consumes fuel, haematite, to devise phototactic microswimmers that form self-spinning microgears following spatiotemporal light patterns. The gears are coupled via their chemical clouds by diffusiophoresis12 and constitute the elementary bricks of synchronized superstructures, which autonomously regulate their dynamics. The results are quantitatively rationalized on the basis of a stochastic description of diffusio-phoretic oscillators dynamically coupled by chemical gradients. Our findings harness non-equilibrium phoretic phenomena to program interactions and direct self-assembly with fidelity and specificity. It lays the groundwork for the autonomous construction of dynamical architectures and functional micro-machinery."}],"page":"1114-1118","article_processing_charge":"No","date_published":"2018-11-01T00:00:00Z","year":"2018","publisher":"Springer Nature","author":[{"full_name":"Aubret, Antoine","last_name":"Aubret","first_name":"Antoine"},{"first_name":"Mena","last_name":"Youssef","full_name":"Youssef, Mena"},{"full_name":"Sacanna, Stefano","last_name":"Sacanna","first_name":"Stefano"},{"first_name":"Jérémie A","orcid":"0000-0002-7253-9465","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","full_name":"Palacci, Jérémie A","last_name":"Palacci"}],"extern":"1","_id":"9062","issue":"11","external_id":{"arxiv":["1810.01033"]},"volume":14,"intvolume":"        14"},{"status":"public","citation":{"apa":"Lee, N., Ko, E., Choi, H. Y., Hong, Y. J., Nauman, M., Kang, W., … Jo, Y. (2018). Antiferromagnet‐based spintronic functionality by controlling isospin domains in a layered perovskite iridate. <i>Advanced Materials</i>. Wiley. <a href=\"https://doi.org/10.1002/adma.201805564\">https://doi.org/10.1002/adma.201805564</a>","ama":"Lee N, Ko E, Choi HY, et al. Antiferromagnet‐based spintronic functionality by controlling isospin domains in a layered perovskite iridate. <i>Advanced Materials</i>. 2018;30(52). doi:<a href=\"https://doi.org/10.1002/adma.201805564\">10.1002/adma.201805564</a>","ieee":"N. Lee <i>et al.</i>, “Antiferromagnet‐based spintronic functionality by controlling isospin domains in a layered perovskite iridate,” <i>Advanced Materials</i>, vol. 30, no. 52. Wiley, 2018.","ista":"Lee N, Ko E, Choi HY, Hong YJ, Nauman M, Kang W, Choi HJ, Choi YJ, Jo Y. 2018. Antiferromagnet‐based spintronic functionality by controlling isospin domains in a layered perovskite iridate. Advanced Materials. 30(52), 1805564.","mla":"Lee, Nara, et al. “Antiferromagnet‐based Spintronic Functionality by Controlling Isospin Domains in a Layered Perovskite Iridate.” <i>Advanced Materials</i>, vol. 30, no. 52, 1805564, Wiley, 2018, doi:<a href=\"https://doi.org/10.1002/adma.201805564\">10.1002/adma.201805564</a>.","short":"N. Lee, E. Ko, H.Y. Choi, Y.J. Hong, M. Nauman, W. Kang, H.J. Choi, Y.J. Choi, Y. Jo, Advanced Materials 30 (2018).","chicago":"Lee, Nara, Eunjung Ko, Hwan Young Choi, Yun Jeong Hong, Muhammad Nauman, Woun Kang, Hyoung Joon Choi, Young Jai Choi, and Younjung Jo. “Antiferromagnet‐based Spintronic Functionality by Controlling Isospin Domains in a Layered Perovskite Iridate.” <i>Advanced Materials</i>. Wiley, 2018. <a href=\"https://doi.org/10.1002/adma.201805564\">https://doi.org/10.1002/adma.201805564</a>."},"month":"10","publication_status":"published","day":"29","doi":"10.1002/adma.201805564","arxiv":1,"quality_controlled":"1","language":[{"iso":"eng"}],"oa_version":"Preprint","abstract":[{"text":"The novel electronic state of the canted antiferromagnetic (AFM) insulator, strontium iridate (Sr2IrO4) has been well described by the spin-orbit-entangled isospin Jeff = 1/2, but the role of isospin in transport phenomena remains poorly understood. In this study, antiferromagnet-based spintronic functionality is demonstrated by combining unique characteristics of the isospin state in Sr2IrO4. Based on magnetic and transport measurements, large and highly anisotropic magnetoresistance (AMR) is obtained by manipulating the antiferromagnetic isospin domains. First-principles calculations suggest that electrons whose isospin directions are strongly coupled to in-plane net magnetic moment encounter the isospin mismatch when moving across antiferromagnetic domain boundaries, which generates a high resistance state. By rotating a magnetic field that aligns in-plane net moments and removes domain boundaries, the macroscopically-ordered isospins govern dynamic transport through the system, which leads to the extremely angle-sensitive AMR. As with this work that establishes a link between isospins and magnetotransport in strongly spin-orbit-coupled AFM Sr2IrO4, the peculiar AMR effect provides a beneficial foundation for fundamental and applied research on AFM spintronics.","lang":"eng"}],"publication":"Advanced Materials","date_created":"2021-02-02T15:50:58Z","publication_identifier":{"issn":["0935-9648","1521-4095"]},"type":"journal_article","date_updated":"2021-02-03T13:58:39Z","article_type":"original","title":"Antiferromagnet‐based spintronic functionality by controlling isospin domains in a layered perovskite iridate","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["Mechanical Engineering","General Materials Science","Mechanics of Materials"],"publisher":"Wiley","year":"2018","article_number":"1805564","date_published":"2018-10-29T00:00:00Z","article_processing_charge":"No","intvolume":"        30","volume":30,"issue":"52","_id":"9066","extern":"1","external_id":{"arxiv":["1811.04562"]},"author":[{"first_name":"Nara","full_name":"Lee, Nara","last_name":"Lee"},{"last_name":"Ko","full_name":"Ko, Eunjung","first_name":"Eunjung"},{"last_name":"Choi","full_name":"Choi, Hwan Young","first_name":"Hwan Young"},{"last_name":"Hong","full_name":"Hong, Yun Jeong","first_name":"Yun Jeong"},{"orcid":"0000-0002-2111-4846","first_name":"Muhammad","full_name":"Nauman, Muhammad","id":"32c21954-2022-11eb-9d5f-af9f93c24e71","last_name":"Nauman"},{"full_name":"Kang, Woun","last_name":"Kang","first_name":"Woun"},{"first_name":"Hyoung Joon","full_name":"Choi, Hyoung Joon","last_name":"Choi"},{"first_name":"Young Jai","last_name":"Choi","full_name":"Choi, Young Jai"},{"full_name":"Jo, Younjung","last_name":"Jo","first_name":"Younjung"}]},{"doi":"10.1016/j.physb.2017.11.032","day":"01","publication_status":"published","date_published":"2018-05-01T00:00:00Z","month":"05","page":"235-238","quality_controlled":"1","oa_version":"None","language":[{"iso":"eng"}],"article_processing_charge":"No","citation":{"short":"T. Hussain, M. Oh, M. Nauman, Y. Jo, G. Han, C. Kim, W. Kang, Physica B: Condensed Matter 536 (2018) 235–238.","chicago":"Hussain, Tayyaba, Myeong-jun Oh, Muhammad Nauman, Younjung Jo, Garam Han, Changyoung Kim, and Woun Kang. “Pressure-Induced Metal–Insulator Transitions in Chalcogenide NiS2-Se.” <i>Physica B: Condensed Matter</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.physb.2017.11.032\">https://doi.org/10.1016/j.physb.2017.11.032</a>.","mla":"Hussain, Tayyaba, et al. “Pressure-Induced Metal–Insulator Transitions in Chalcogenide NiS2-Se.” <i>Physica B: Condensed Matter</i>, vol. 536, Elsevier, 2018, pp. 235–38, doi:<a href=\"https://doi.org/10.1016/j.physb.2017.11.032\">10.1016/j.physb.2017.11.032</a>.","ista":"Hussain T, Oh M, Nauman M, Jo Y, Han G, Kim C, Kang W. 2018. Pressure-induced metal–insulator transitions in chalcogenide NiS2-Se. Physica B: Condensed Matter. 536, 235–238.","ieee":"T. Hussain <i>et al.</i>, “Pressure-induced metal–insulator transitions in chalcogenide NiS2-Se,” <i>Physica B: Condensed Matter</i>, vol. 536. Elsevier, pp. 235–238, 2018.","apa":"Hussain, T., Oh, M., Nauman, M., Jo, Y., Han, G., Kim, C., &#38; Kang, W. (2018). Pressure-induced metal–insulator transitions in chalcogenide NiS2-Se. <i>Physica B: Condensed Matter</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.physb.2017.11.032\">https://doi.org/10.1016/j.physb.2017.11.032</a>","ama":"Hussain T, Oh M, Nauman M, et al. Pressure-induced metal–insulator transitions in chalcogenide NiS2-Se. <i>Physica B: Condensed Matter</i>. 2018;536:235-238. doi:<a href=\"https://doi.org/10.1016/j.physb.2017.11.032\">10.1016/j.physb.2017.11.032</a>"},"publisher":"Elsevier","status":"public","year":"2018","_id":"9068","extern":"1","title":"Pressure-induced metal–insulator transitions in chalcogenide NiS2-Se","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","author":[{"last_name":"Hussain","full_name":"Hussain, Tayyaba","first_name":"Tayyaba"},{"first_name":"Myeong-jun","last_name":"Oh","full_name":"Oh, Myeong-jun"},{"last_name":"Nauman","id":"32c21954-2022-11eb-9d5f-af9f93c24e71","full_name":"Nauman, Muhammad","first_name":"Muhammad","orcid":"0000-0002-2111-4846"},{"first_name":"Younjung","last_name":"Jo","full_name":"Jo, Younjung"},{"full_name":"Han, Garam","last_name":"Han","first_name":"Garam"},{"first_name":"Changyoung","full_name":"Kim, Changyoung","last_name":"Kim"},{"first_name":"Woun","last_name":"Kang","full_name":"Kang, Woun"}],"publication_identifier":{"issn":["0921-4526"]},"publication":"Physica B: Condensed Matter","date_created":"2021-02-02T15:52:43Z","abstract":[{"text":"We report the temperature-dependent resistivity ρ(T) of chalcogenide NiS2-xSex (x = 0.1) using hydrostatic pressure as a control parameter in the temperature range of 4–300 K. The insulating behavior of ρ(T) survives at low temperatures in the pressure regime below 7.5 kbar, whereas a clear insulator-to-metallic transition is observed above 7.5 kbar. Two types of magnetic transitions, from the paramagnetic (PM) to the antiferromagnetic (AFM) state and from the AFM state to the weak ferromagnetic (WF) state, were evaluated and confirmed by magnetization measurement. According to the temperature–pressure phase diagram, the WF phase survives up to 7.5 kbar, and the transition temperature of the WF transition decreases as the pressure increases, whereas the metal–insulator transition temperature increases up to 9.4 kbar. We analyzed the metallic behavior and proposed Fermi-liquid behavior of NiS1.9Se0.1.","lang":"eng"}],"intvolume":"       536","date_updated":"2021-02-04T07:18:57Z","type":"journal_article","volume":536},{"day":"29","ec_funded":1,"doi":"10.1242/jcs.204198","publication_status":"published","department":[{"_id":"JiFr"}],"month":"01","corr_author":"1","oa_version":"Published Version","quality_controlled":"1","language":[{"iso":"eng"}],"file":[{"file_id":"6299","date_created":"2019-04-12T08:46:32Z","file_name":"2017_adamowski_PATELLINS_are.pdf","date_updated":"2020-07-14T12:48:15Z","file_size":14925985,"creator":"dernst","access_level":"open_access","content_type":"application/pdf","relation":"main_file","checksum":"bf156c20a4f117b4b932370d54cbac8c"}],"citation":{"ista":"Tejos R, Rodríguez Furlán C, Adamowski M, Sauer M, Norambuena L, Friml J. 2018. PATELLINS are regulators of auxin mediated PIN1 relocation and plant development in Arabidopsis thaliana. Journal of Cell Science. 131(2), jcs. 204198.","chicago":"Tejos, Ricardo, Cecilia Rodríguez Furlán, Maciek Adamowski, Michael Sauer, Lorena Norambuena, and Jiří Friml. “PATELLINS Are Regulators of Auxin Mediated PIN1 Relocation and Plant Development in Arabidopsis Thaliana.” <i>Journal of Cell Science</i>. Company of Biologists, 2018. <a href=\"https://doi.org/10.1242/jcs.204198\">https://doi.org/10.1242/jcs.204198</a>.","mla":"Tejos, Ricardo, et al. “PATELLINS Are Regulators of Auxin Mediated PIN1 Relocation and Plant Development in Arabidopsis Thaliana.” <i>Journal of Cell Science</i>, vol. 131, no. 2, jcs. 204198, Company of Biologists, 2018, doi:<a href=\"https://doi.org/10.1242/jcs.204198\">10.1242/jcs.204198</a>.","short":"R. Tejos, C. Rodríguez Furlán, M. Adamowski, M. Sauer, L. Norambuena, J. Friml, Journal of Cell Science 131 (2018).","apa":"Tejos, R., Rodríguez Furlán, C., Adamowski, M., Sauer, M., Norambuena, L., &#38; Friml, J. (2018). PATELLINS are regulators of auxin mediated PIN1 relocation and plant development in Arabidopsis thaliana. <i>Journal of Cell Science</i>. Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.204198\">https://doi.org/10.1242/jcs.204198</a>","ama":"Tejos R, Rodríguez Furlán C, Adamowski M, Sauer M, Norambuena L, Friml J. PATELLINS are regulators of auxin mediated PIN1 relocation and plant development in Arabidopsis thaliana. <i>Journal of Cell Science</i>. 2018;131(2). doi:<a href=\"https://doi.org/10.1242/jcs.204198\">10.1242/jcs.204198</a>","ieee":"R. Tejos, C. Rodríguez Furlán, M. Adamowski, M. Sauer, L. Norambuena, and J. Friml, “PATELLINS are regulators of auxin mediated PIN1 relocation and plant development in Arabidopsis thaliana,” <i>Journal of Cell Science</i>, vol. 131, no. 2. Company of Biologists, 2018."},"status":"public","scopus_import":"1","title":"PATELLINS are regulators of auxin mediated PIN1 relocation and plant development in Arabidopsis thaliana","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","has_accepted_license":"1","oa":1,"publication_identifier":{"issn":["0021-9533"]},"publication":"Journal of Cell Science","date_created":"2018-12-11T11:49:10Z","abstract":[{"text":"Coordinated cell polarization in developing tissues is a recurrent theme in multicellular organisms. In plants, a directional distribution of the plant hormone auxin is at the core of many developmental programs. A feedback regulation of auxin on the polarized localization of PIN auxin transporters in individual cells has been proposed as a self-organizing mechanism for coordinated tissue polarization, but the molecular mechanisms linking auxin signalling to PIN-dependent auxin transport remain unknown. We performed a microarray-based approach to find regulators of the auxin-induced PIN relocation in the Arabidopsis thaliana root. We identified a subset of a family of phosphatidylinositol transfer proteins (PITP), the PATELLINs (PATL). Here, we show that PATLs are expressed in partially overlapping cells types in different tissues going through mitosis or initiating differentiation programs. PATLs are plasma membrane-associated proteins accumulated in Arabidopsis embryos, primary roots, lateral root primordia, and developing stomata. Higher order patl mutants display reduced PIN1 repolarization in response to auxin, shorter root apical meristem, and drastic defects in embryo and seedling development. This suggests PATLs redundantly play a crucial role in polarity and patterning in Arabidopsis.","lang":"eng"}],"date_updated":"2025-07-10T12:01:38Z","type":"journal_article","file_date_updated":"2020-07-14T12:48:15Z","date_published":"2018-01-29T00:00:00Z","article_processing_charge":"No","ddc":["581"],"publisher":"Company of Biologists","project":[{"call_identifier":"FP7","name":"Polarity and subcellular dynamics in plants","grant_number":"282300","_id":"25716A02-B435-11E9-9278-68D0E5697425"}],"pubrep_id":"988","article_number":"jcs.204198","year":"2018","_id":"913","external_id":{"isi":["000424842400019"]},"issue":"2","isi":1,"author":[{"first_name":"Ricardo","last_name":"Tejos","full_name":"Tejos, Ricardo"},{"last_name":"Rodríguez Furlán","full_name":"Rodríguez Furlán, Cecilia","first_name":"Cecilia"},{"full_name":"Adamowski, Maciek","id":"45F536D2-F248-11E8-B48F-1D18A9856A87","last_name":"Adamowski","orcid":"0000-0001-6463-5257","first_name":"Maciek"},{"full_name":"Sauer, Michael","last_name":"Sauer","first_name":"Michael"},{"first_name":"Lorena","last_name":"Norambuena","full_name":"Norambuena, Lorena"},{"first_name":"Jirí","orcid":"0000-0002-8302-7596","last_name":"Friml","id":"4159519E-F248-11E8-B48F-1D18A9856A87","full_name":"Friml, Jirí"}],"publist_id":"6530","intvolume":"       131","volume":131}]