[{"abstract":[{"lang":"eng","text":"The problem of electing a leader from among n contenders is one of the fundamental questions in distributed computing. In its simplest formulation, the task is as follows: given n processors, all participants must eventually return a win or lose indication, such that a single contender may win. Despite a considerable amount of work on leader election, the following question is still open: can we elect a leader in an asynchronous fault-prone system faster than just running a Θ(log n)-time tournament, against a strong adaptive adversary? In this paper, we answer this question in the affirmative, improving on a decades-old upper bound. We introduce two new algorithmic ideas to reduce the time complexity of electing a leader to O(log∗ n), using O(n2) point-to-point messages. A non-trivial application of our algorithm is a new upper bound for the tight renaming problem, assigning n items to the n participants in expected O(log2 n) time and O(n2) messages. We complement our results with lower bound of Ω(n2) messages for solving these two problems, closing the question of their message complexity."}],"publication_status":"published","month":"07","language":[{"iso":"eng"}],"date_published":"2015-07-21T00:00:00Z","publisher":"ACM","article_processing_charge":"No","volume":"2015-July","title":"How to elect a leader faster than a tournament","date_updated":"2023-02-23T13:18:55Z","extern":"1","oa_version":"None","citation":{"short":"D.-A. Alistarh, R. Gelashvili, A. Vladu, in:, ACM, 2015, pp. 365–374.","mla":"Alistarh, Dan-Adrian, et al. <i>How to Elect a Leader Faster than a Tournament</i>. Vol. 2015–July, ACM, 2015, pp. 365–74, doi:<a href=\"https://doi.org/10.1145/2767386.2767420\">10.1145/2767386.2767420</a>.","apa":"Alistarh, D.-A., Gelashvili, R., &#38; Vladu, A. (2015). How to elect a leader faster than a tournament (Vol. 2015–July, pp. 365–374). Presented at the PODC: Principles of Distributed Computing, ACM. <a href=\"https://doi.org/10.1145/2767386.2767420\">https://doi.org/10.1145/2767386.2767420</a>","chicago":"Alistarh, Dan-Adrian, Rati Gelashvili, and Adrian Vladu. “How to Elect a Leader Faster than a Tournament,” 2015–July:365–74. ACM, 2015. <a href=\"https://doi.org/10.1145/2767386.2767420\">https://doi.org/10.1145/2767386.2767420</a>.","ista":"Alistarh D-A, Gelashvili R, Vladu A. 2015. How to elect a leader faster than a tournament. PODC: Principles of Distributed Computing vol. 2015–July, 365–374.","ama":"Alistarh D-A, Gelashvili R, Vladu A. How to elect a leader faster than a tournament. In: Vol 2015-July. ACM; 2015:365-374. doi:<a href=\"https://doi.org/10.1145/2767386.2767420\">10.1145/2767386.2767420</a>","ieee":"D.-A. Alistarh, R. Gelashvili, and A. Vladu, “How to elect a leader faster than a tournament,” presented at the PODC: Principles of Distributed Computing, 2015, vol. 2015–July, pp. 365–374."},"author":[{"id":"4A899BFC-F248-11E8-B48F-1D18A9856A87","full_name":"Alistarh, Dan-Adrian","last_name":"Alistarh","first_name":"Dan-Adrian","orcid":"0000-0003-3650-940X"},{"full_name":"Gelashvili, Rati","last_name":"Gelashvili","first_name":"Rati"},{"full_name":"Vladu, Adrian","first_name":"Adrian","last_name":"Vladu"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publist_id":"6875","conference":{"name":"PODC: Principles of Distributed Computing"},"date_created":"2018-12-11T11:48:28Z","oa":1,"_id":"783","type":"conference","acknowledgement":"Support is gratefully acknowledged from the National Science Foundation under grants CCF-1217921, CCF-1301926,\r\nand  IIS-1447786,  the  Department  of  Energy  under  grant\r\nER26116/DE-SC0008923,  and the  Oracle  and Intel  corporations.\r\nThe authors would like to thank Prof.  Nir Shavit for ad-\r\nvice and encouragement during this work,  and the anonymous reviewers for their very useful suggestions.","day":"21","year":"2015","status":"public","doi":"10.1145/2767386.2767420","page":"365 - 374","main_file_link":[{"url":"https://arxiv.org/abs/1411.1001","open_access":"1"}]},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"orcid":"0000-0003-3650-940X","last_name":"Alistarh","first_name":"Dan-Adrian","full_name":"Alistarh, Dan-Adrian","id":"4A899BFC-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Ballani, Hitesh","last_name":"Ballani","first_name":"Hitesh"},{"full_name":"Costa, Paolo","last_name":"Costa","first_name":"Paolo"},{"first_name":"Adam","last_name":"Funnell","full_name":"Funnell, Adam"},{"last_name":"Benjamin","first_name":"Joshua","full_name":"Benjamin, Joshua"},{"last_name":"Watts","first_name":"Philip","full_name":"Watts, Philip"},{"full_name":"Thomsen, Benn","first_name":"Benn","last_name":"Thomsen"}],"citation":{"short":"D.-A. Alistarh, H. Ballani, P. Costa, A. Funnell, J. Benjamin, P. Watts, B. Thomsen, in:, ACM, 2015, pp. 367–368.","mla":"Alistarh, Dan-Adrian, et al. <i>A High-Radix, Low-Latency Optical Switch for Data Centers</i>. ACM, 2015, pp. 367–68, doi:<a href=\"https://doi.org/10.1145/2785956.2790035\">10.1145/2785956.2790035</a>.","apa":"Alistarh, D.-A., Ballani, H., Costa, P., Funnell, A., Benjamin, J., Watts, P., &#38; Thomsen, B. (2015). A high-radix, low-latency optical switch for data centers (pp. 367–368). Presented at the SIGCOMM: Special Interest Group on Data Communication, London, United Kindgdom: ACM. <a href=\"https://doi.org/10.1145/2785956.2790035\">https://doi.org/10.1145/2785956.2790035</a>","ama":"Alistarh D-A, Ballani H, Costa P, et al. A high-radix, low-latency optical switch for data centers. In: ACM; 2015:367-368. doi:<a href=\"https://doi.org/10.1145/2785956.2790035\">10.1145/2785956.2790035</a>","ista":"Alistarh D-A, Ballani H, Costa P, Funnell A, Benjamin J, Watts P, Thomsen B. 2015. A high-radix, low-latency optical switch for data centers. SIGCOMM: Special Interest Group on Data Communication, 367–368.","chicago":"Alistarh, Dan-Adrian, Hitesh Ballani, Paolo Costa, Adam Funnell, Joshua Benjamin, Philip Watts, and Benn Thomsen. “A High-Radix, Low-Latency Optical Switch for Data Centers,” 367–68. ACM, 2015. <a href=\"https://doi.org/10.1145/2785956.2790035\">https://doi.org/10.1145/2785956.2790035</a>.","ieee":"D.-A. Alistarh <i>et al.</i>, “A high-radix, low-latency optical switch for data centers,” presented at the SIGCOMM: Special Interest Group on Data Communication, London, United Kindgdom, 2015, pp. 367–368."},"oa_version":"None","date_updated":"2023-02-23T13:18:57Z","extern":"1","quality_controlled":"1","title":"A high-radix, low-latency optical switch for data centers","publisher":"ACM","language":[{"iso":"eng"}],"date_published":"2015-01-01T00:00:00Z","abstract":[{"lang":"eng","text":"We demonstrate an optical switch design that can scale up to a thousand ports with high per-port bandwidth (25 Gbps+) and low switching latency (40 ns). Our design uses a broadcast and select architecture, based on a passive star coupler and fast tunable transceivers. In addition we employ time division multiplexing to achieve very low switching latency. Our demo shows the feasibility of the switch data plane using a small testbed, comprising two transmitters and a receiver, connected through a star coupler."}],"publication_status":"published","month":"01","page":"367 - 368","publication_identifier":{"isbn":["978-1-4503-3542-3"]},"doi":"10.1145/2785956.2790035","status":"public","year":"2015","day":"01","_id":"784","type":"conference","date_created":"2018-12-11T11:48:29Z","conference":{"location":"London, United Kindgdom","name":"SIGCOMM: Special Interest Group on Data Communication","end_date":"2015-08-21","start_date":"2015-08-17"},"publist_id":"6872"},{"month":"12","publication_status":"published","abstract":[{"text":"Glycoinositolphosphoceramides (GIPCs) are complex sphingolipids present at the plasma membrane of various eukaryotes with the important exception of mammals. In fungi, these glycosphingolipids commonly contain an alpha-mannose residue (Man) linked at position 2 of the inositol. However, several pathogenic fungi additionally synthesize zwitterionic GIPCs carrying an alpha-glucosamine residue (GlcN) at this position. In the human pathogen Aspergillus fumigatus, the GlcNalpha1,2IPC core (where IPC is inositolphosphoceramide) is elongated to Manalpha1,3Manalpha1,6GlcNalpha1,2IPC, which is the most abundant GIPC synthesized by this fungus. In this study, we identified an A. fumigatus N-acetylglucosaminyltransferase, named GntA, and demonstrate its involvement in the initiation of zwitterionic GIPC biosynthesis. Targeted deletion of the gene encoding GntA in A. fumigatus resulted in complete absence of zwitterionic GIPC; a phenotype that could be reverted by episomal expression of GntA in the mutant. The N-acetylhexosaminyltransferase activity of GntA was substantiated by production of N-acetylhexosamine-IPC in the yeast Saccharomyces cerevisiae upon GntA expression. Using an in vitro assay, GntA was furthermore shown to use UDP-N-acetylglucosamine as donor substrate to generate a glycolipid product resistant to saponification and to digestion by phosphatidylinositol-phospholipase C as expected for GlcNAcalpha1,2IPC. Finally, as the enzymes involved in mannosylation of IPC, GntA was localized to the Golgi apparatus, the site of IPC synthesis.","lang":"eng"}],"issue":"12","pmid":1,"publisher":"Oxford University Press","date_published":"2015-12-01T00:00:00Z","language":[{"iso":"eng"}],"volume":25,"title":"Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis","quality_controlled":"1","department":[{"_id":"CaHe"}],"date_updated":"2021-01-12T08:16:33Z","citation":{"ama":"Engel J, Schmalhorst PS, Kruger A, Muller C, Buettner F, Routier F. Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis. <i>Glycobiology</i>. 2015;25(12):1423-1430. doi:<a href=\"https://doi.org/10.1093/glycob/cwv059\">10.1093/glycob/cwv059</a>","ista":"Engel J, Schmalhorst PS, Kruger A, Muller C, Buettner F, Routier F. 2015. Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis. Glycobiology. 25(12), 1423–1430.","chicago":"Engel, Jakob, Philipp S Schmalhorst, Anke Kruger, Christina Muller, Falk Buettner, and Françoise Routier. “Characterization of an N-Acetylglucosaminyltransferase Involved in Aspergillus Fumigatus Zwitterionic Glycoinositolphosphoceramide Biosynthesis.” <i>Glycobiology</i>. Oxford University Press, 2015. <a href=\"https://doi.org/10.1093/glycob/cwv059\">https://doi.org/10.1093/glycob/cwv059</a>.","apa":"Engel, J., Schmalhorst, P. S., Kruger, A., Muller, C., Buettner, F., &#38; Routier, F. (2015). Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis. <i>Glycobiology</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/glycob/cwv059\">https://doi.org/10.1093/glycob/cwv059</a>","ieee":"J. Engel, P. S. Schmalhorst, A. Kruger, C. Muller, F. Buettner, and F. Routier, “Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis,” <i>Glycobiology</i>, vol. 25, no. 12. Oxford University Press, pp. 1423–1430, 2015.","short":"J. Engel, P.S. Schmalhorst, A. Kruger, C. Muller, F. Buettner, F. Routier, Glycobiology 25 (2015) 1423–1430.","mla":"Engel, Jakob, et al. “Characterization of an N-Acetylglucosaminyltransferase Involved in Aspergillus Fumigatus Zwitterionic Glycoinositolphosphoceramide Biosynthesis.” <i>Glycobiology</i>, vol. 25, no. 12, Oxford University Press, 2015, pp. 1423–30, doi:<a href=\"https://doi.org/10.1093/glycob/cwv059\">10.1093/glycob/cwv059</a>."},"oa_version":"None","author":[{"first_name":"Jakob","last_name":"Engel","full_name":"Engel, Jakob"},{"last_name":"Schmalhorst","first_name":"Philipp S","orcid":"0000-0002-5795-0133","id":"309D50DA-F248-11E8-B48F-1D18A9856A87","full_name":"Schmalhorst, Philipp S"},{"first_name":"Anke","last_name":"Kruger","full_name":"Kruger, Anke"},{"full_name":"Muller, Christina","last_name":"Muller","first_name":"Christina"},{"full_name":"Buettner, Falk","first_name":"Falk","last_name":"Buettner"},{"last_name":"Routier","first_name":"Françoise","full_name":"Routier, Françoise"}],"external_id":{"pmid":["26306635"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":1,"publist_id":"6851","intvolume":"        25","publication":"Glycobiology","date_created":"2018-12-11T11:48:35Z","type":"journal_article","_id":"802","page":"1423 - 1430","doi":"10.1093/glycob/cwv059","status":"public","day":"01","year":"2015"},{"volume":517,"title":"Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution","publisher":"Nature Publishing Group","date_published":"2015-01-22T00:00:00Z","issue":"7535","publication_status":"published","month":"01","abstract":[{"lang":"eng","text":"Human immunodeficiency virus type 1 (HIV-1) assembly proceeds in two stages. First, the 55 kilodalton viral Gag polyprotein assembles into a hexameric protein lattice at the plasma membrane of the infected cell, inducing budding and release of an immature particle. Second, Gag is cleaved by the viral protease, leading to internal rearrangement of the virus into the mature, infectious form. Immature and mature HIV-1 particles are heterogeneous in size and morphology, preventing high-resolution analysis of their protein arrangement in situ by conventional structural biology methods. Here we apply cryo-electron tomography and sub-tomogram averaging methods to resolve the structure of the capsid lattice within intact immature HIV-1 particles at subnanometre resolution, allowing unambiguous positioning of all α-helices. The resulting model reveals tertiary and quaternary structural interactions that mediate HIV-1 assembly. Strikingly, these interactions differ from those predicted by the current model based on in vitro-assembled arrays of Gag-derived proteins from Mason-Pfizer monkey virus. To validate this difference, we solve the structure of the capsid lattice within intact immature Mason-Pfizer monkey virus particles. Comparison with the immature HIV-1 structure reveals that retroviral capsid proteins, while having conserved tertiary structures, adopt different quaternary arrangements during virus assembly. The approach demonstrated here should be applicable to determine structures of other proteins at subnanometre resolution within heterogeneous environments."}],"author":[{"last_name":"Schur","first_name":"Florian","orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Florian Schur"},{"full_name":"Hagen, Wim J","first_name":"Wim","last_name":"Hagen"},{"first_name":"Michaela","last_name":"Rumlová","full_name":"Rumlová, Michaela"},{"first_name":"Tomáš","last_name":"Ruml","full_name":"Ruml, Tomáš"},{"last_name":"Müller","first_name":"B","full_name":"Müller B"},{"first_name":"Hans","last_name":"Kraüsslich","full_name":"Kraüsslich, Hans Georg"},{"full_name":"Briggs, John A","last_name":"Briggs","first_name":"John"}],"citation":{"short":"F.K. Schur, W. Hagen, M. Rumlová, T. Ruml, B. Müller, H. Kraüsslich, J. Briggs, Nature 517 (2015) 505–508.","mla":"Schur, Florian KM, et al. “Structure of the Immature HIV-1 Capsid in Intact Virus Particles at 8.8 Å Resolution.” <i>Nature</i>, vol. 517, no. 7535, Nature Publishing Group, 2015, pp. 505–08, doi:<a href=\"https://doi.org/10.1038/nature13838\">10.1038/nature13838</a>.","ieee":"F. K. Schur <i>et al.</i>, “Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution,” <i>Nature</i>, vol. 517, no. 7535. Nature Publishing Group, pp. 505–508, 2015.","apa":"Schur, F. K., Hagen, W., Rumlová, M., Ruml, T., Müller, B., Kraüsslich, H., &#38; Briggs, J. (2015). Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution. <i>Nature</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nature13838\">https://doi.org/10.1038/nature13838</a>","ista":"Schur FK, Hagen W, Rumlová M, Ruml T, Müller B, Kraüsslich H, Briggs J. 2015. Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution. Nature. 517(7535), 505–508.","chicago":"Schur, Florian KM, Wim Hagen, Michaela Rumlová, Tomáš Ruml, B Müller, Hans Kraüsslich, and John Briggs. “Structure of the Immature HIV-1 Capsid in Intact Virus Particles at 8.8 Å Resolution.” <i>Nature</i>. Nature Publishing Group, 2015. <a href=\"https://doi.org/10.1038/nature13838\">https://doi.org/10.1038/nature13838</a>.","ama":"Schur FK, Hagen W, Rumlová M, et al. Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution. <i>Nature</i>. 2015;517(7535):505-508. doi:<a href=\"https://doi.org/10.1038/nature13838\">10.1038/nature13838</a>"},"extern":1,"quality_controlled":0,"date_updated":"2021-01-12T08:17:08Z","publication":"Nature","publist_id":"6836","intvolume":"       517","doi":"10.1038/nature13838","page":"505 - 508","year":"2015","day":"22","status":"public","acknowledgement":"This study was supported by Deutsche Forschungsgemeinschaft grants BR 3635/2-1 to J.A.G.B., KR 906/7-1 to H.-G.K. and by Grant Agency of the Czech Republic 14-15326S to M.R. The Briggs laboratory acknowledges financial support from the European Molecular Biology Laboratory and from the Chica und Heinz Schaller Stiftung. We thank B. Glass, M. Anders and S. Mattei for preparation of samples, and R. Hadravova, K. H. Bui, F. Thommen, M. Schorb, S. Dodonova, S. Glatt, P. Ulbrich and T. Bharat for technical support and/or discussion. This study was technically supported by the European Molecular Biology Laboratory IT services unit.","_id":"814","type":"journal_article","date_created":"2018-12-11T11:48:39Z"},{"publist_id":"6837","intvolume":"        89","publication":"Journal of Virology","status":"public","doi":"10.1128/JVI.01502-15","day":"22","year":"2015","page":"10294 - 10302","date_created":"2018-12-11T11:48:39Z","_id":"815","type":"journal_article","pmid":1,"publisher":"ASM","language":[{"iso":"eng"}],"date_published":"2015-09-22T00:00:00Z","volume":89,"title":"The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly","publication_status":"published","month":"09","abstract":[{"text":"The polyprotein Gag is the primary structural component of retroviruses. Gag consists of independently folded domains connected by flexible linkers. Interactions between the conserved capsid (CA) domains of Gag mediate formation of hexameric protein lattices that drive assembly of immature virus particles. Proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retroviruses from an immature form into an infectious form. Within the assembled Gag lattices of HIV-1 and Mason- Pfizer monkey virus (M-PMV), the C-terminal domain of CA adopts similar quaternary arrangements, while the N-terminal domain of CA is packed in very different manners. Here, we have used cryo-electron tomography and subtomogram averaging to study in vitro-assembled, immature virus-like Rous sarcoma virus (RSV) Gag particles and have determined the structure of CA and the surrounding regions to a resolution of ~8 Å. We found that the C-terminal domain of RSV CA is arranged similarly to HIV-1 and M-PMV, whereas the N-terminal domain of CA adopts a novel arrangement in which the upstream p10 domain folds back into the CA lattice. In this position the cleavage site between CA and p10 appears to be inaccessible to PR. Below CA, an extended density is consistent with the presence of a six-helix bundle formed by the spacer-peptide region. We have also assessed the affect of lattice assembly on proteolytic processing by exogenous PR. The cleavage between p10 and CA is indeed inhibited in the assembled lattice, a finding consistent with structural regulation of proteolytic maturation.\r\n","lang":"eng"}],"issue":"20","author":[{"full_name":"Schur, Florian","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","last_name":"Schur","first_name":"Florian"},{"full_name":"Dick, Robert","last_name":"Dick","first_name":"Robert"},{"first_name":"Wim","last_name":"Hagen","full_name":"Hagen, Wim"},{"first_name":"Volker","last_name":"Vogt","full_name":"Vogt, Volker"},{"first_name":"John","last_name":"Briggs","full_name":"Briggs, John"}],"external_id":{"pmid":["26223638"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","quality_controlled":"1","date_updated":"2021-01-12T08:17:09Z","citation":{"short":"F.K. Schur, R. Dick, W. Hagen, V. Vogt, J. Briggs, Journal of Virology 89 (2015) 10294–10302.","mla":"Schur, Florian KM, et al. “The Structure of Immature Virus like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the P10 Domain in Assembly.” <i>Journal of Virology</i>, vol. 89, no. 20, ASM, 2015, pp. 10294–302, doi:<a href=\"https://doi.org/10.1128/JVI.01502-15\">10.1128/JVI.01502-15</a>.","ieee":"F. K. Schur, R. Dick, W. Hagen, V. Vogt, and J. Briggs, “The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly,” <i>Journal of Virology</i>, vol. 89, no. 20. ASM, pp. 10294–10302, 2015.","ama":"Schur FK, Dick R, Hagen W, Vogt V, Briggs J. The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. <i>Journal of Virology</i>. 2015;89(20):10294-10302. doi:<a href=\"https://doi.org/10.1128/JVI.01502-15\">10.1128/JVI.01502-15</a>","ista":"Schur FK, Dick R, Hagen W, Vogt V, Briggs J. 2015. The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. Journal of Virology. 89(20), 10294–10302.","chicago":"Schur, Florian KM, Robert Dick, Wim Hagen, Volker Vogt, and John Briggs. “The Structure of Immature Virus like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the P10 Domain in Assembly.” <i>Journal of Virology</i>. ASM, 2015. <a href=\"https://doi.org/10.1128/JVI.01502-15\">https://doi.org/10.1128/JVI.01502-15</a>.","apa":"Schur, F. K., Dick, R., Hagen, W., Vogt, V., &#38; Briggs, J. (2015). The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. <i>Journal of Virology</i>. ASM. <a href=\"https://doi.org/10.1128/JVI.01502-15\">https://doi.org/10.1128/JVI.01502-15</a>"},"oa_version":"None"},{"article_number":"1511.03501","publication_status":"submitted","month":"11","abstract":[{"text":"We study conditions under which a finite simplicial complex $K$ can be mapped to $\\mathbb R^d$ without higher-multiplicity intersections. An almost $r$-embedding is a map $f: K\\to \\mathbb R^d$ such that the images of any $r$\r\npairwise disjoint simplices of $K$ do not have a common point. We show that if $r$ is not a prime power and $d\\geq 2r+1$, then there is a counterexample to the topological Tverberg conjecture, i.e., there is an almost $r$-embedding of\r\nthe $(d+1)(r-1)$-simplex in $\\mathbb R^d$. This improves on previous constructions of counterexamples (for $d\\geq 3r$) based on a series of papers by M. \\\"Ozaydin, M. Gromov, P. Blagojevi\\'c, F. Frick, G. Ziegler, and the second and fourth present authors. The counterexamples are obtained by proving the following algebraic criterion in codimension 2: If $r\\ge3$ and if $K$ is a finite $2(r-1)$-complex then there exists an almost $r$-embedding $K\\to \\mathbb R^{2r}$ if and only if there exists a general position PL map $f:K\\to \\mathbb R^{2r}$ such that the algebraic intersection number of the $f$-images of any $r$ pairwise disjoint simplices of $K$ is zero. This result can be restated in terms of cohomological obstructions or equivariant maps, and extends an analogous codimension 3 criterion by the second and fourth authors. As another application we classify ornaments $f:S^3 \\sqcup S^3\\sqcup S^3\\to \\mathbb R^5$ up to ornament\r\nconcordance. It follows from work of M. Freedman, V. Krushkal and P. Teichner that the analogous criterion for $r=2$ is false. We prove a lemma on singular higher-dimensional Borromean rings, yielding an elementary proof of the counterexample.","lang":"eng"}],"title":"Eliminating higher-multiplicity intersections, III. Codimension 2","article_processing_charge":"No","date_published":"2015-11-15T00:00:00Z","language":[{"iso":"eng"}],"citation":{"ieee":"S. Avvakumov, I. Mabillard, A. Skopenkov, and U. Wagner, “Eliminating higher-multiplicity intersections, III. Codimension 2,” <i>arXiv</i>. .","ama":"Avvakumov S, Mabillard I, Skopenkov A, Wagner U. Eliminating higher-multiplicity intersections, III. Codimension 2. <i>arXiv</i>.","ista":"Avvakumov S, Mabillard I, Skopenkov A, Wagner U. Eliminating higher-multiplicity intersections, III. Codimension 2. arXiv, 1511.03501.","chicago":"Avvakumov, Sergey, Isaac Mabillard, A. Skopenkov, and Uli Wagner. “Eliminating Higher-Multiplicity Intersections, III. Codimension 2.” <i>ArXiv</i>, n.d.","apa":"Avvakumov, S., Mabillard, I., Skopenkov, A., &#38; Wagner, U. (n.d.). Eliminating higher-multiplicity intersections, III. Codimension 2. <i>arXiv</i>.","mla":"Avvakumov, Sergey, et al. “Eliminating Higher-Multiplicity Intersections, III. Codimension 2.” <i>ArXiv</i>, 1511.03501.","short":"S. Avvakumov, I. Mabillard, A. Skopenkov, U. Wagner, ArXiv (n.d.)."},"oa_version":"Preprint","department":[{"_id":"UlWa"}],"date_updated":"2023-09-07T13:12:17Z","external_id":{"arxiv":["1511.03501"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"last_name":"Avvakumov","first_name":"Sergey","full_name":"Avvakumov, Sergey","id":"3827DAC8-F248-11E8-B48F-1D18A9856A87"},{"id":"32BF9DAA-F248-11E8-B48F-1D18A9856A87","full_name":"Mabillard, Isaac","last_name":"Mabillard","first_name":"Isaac"},{"full_name":"Skopenkov, A.","last_name":"Skopenkov","first_name":"A."},{"last_name":"Wagner","first_name":"Uli","orcid":"0000-0002-1494-0568","id":"36690CA2-F248-11E8-B48F-1D18A9856A87","full_name":"Wagner, Uli"}],"related_material":{"record":[{"status":"public","id":"9308","relation":"later_version"},{"relation":"later_version","id":"10220","status":"public"},{"relation":"dissertation_contains","id":"8156","status":"public"}]},"publication":"arXiv","arxiv":1,"type":"preprint","_id":"8183","date_created":"2020-07-30T10:45:19Z","oa":1,"day":"15","status":"public","year":"2015","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1511.03501"}],"acknowledgement":"We would like to thank A. Klyachko, V. Krushkal, S. Melikhov, M. Tancer, P. Teichner and anonymous referees for helpful discussions."},{"doi":"10.1016/j.jaci.2014.12.1263","status":"public","day":"01","year":"2015","publication_identifier":{"issn":["0091-6749"]},"date_created":"2020-08-10T11:54:09Z","type":"journal_article","_id":"8242","article_type":"original","intvolume":"       135","publication":"Journal of Allergy and Clinical Immunology","author":[{"first_name":"Lukas","last_name":"Einhorn","full_name":"Einhorn, Lukas"},{"last_name":"Fazekas","first_name":"Judit","orcid":"0000-0002-8777-3502","id":"36432834-F248-11E8-B48F-1D18A9856A87","full_name":"Fazekas, Judit"},{"full_name":"Muhr, Martina","first_name":"Martina","last_name":"Muhr"},{"full_name":"Schoos, Alexandra","last_name":"Schoos","first_name":"Alexandra"},{"full_name":"Oida, Kumiko","first_name":"Kumiko","last_name":"Oida"},{"last_name":"Singer","first_name":"Josef","full_name":"Singer, Josef"},{"full_name":"Panakova, Lucia","last_name":"Panakova","first_name":"Lucia"},{"full_name":"Manzano-Szalai, Krisztina","last_name":"Manzano-Szalai","first_name":"Krisztina"},{"full_name":"Jensen-Jarolim, Erika","last_name":"Jensen-Jarolim","first_name":"Erika"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:17:42Z","extern":"1","quality_controlled":"1","citation":{"ieee":"L. Einhorn <i>et al.</i>, “Generation of recombinant FcεRIα of dog, cat and horse for component-resolved allergy diagnosis in veterinary patients,” <i>Journal of Allergy and Clinical Immunology</i>, vol. 135, no. 2. Elsevier, 2015.","apa":"Einhorn, L., Singer, J., Muhr, M., Schoos, A., Oida, K., Singer, J., … Jensen-Jarolim, E. (2015). Generation of recombinant FcεRIα of dog, cat and horse for component-resolved allergy diagnosis in veterinary patients. <i>Journal of Allergy and Clinical Immunology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jaci.2014.12.1263\">https://doi.org/10.1016/j.jaci.2014.12.1263</a>","chicago":"Einhorn, Lukas, Judit Singer, Martina Muhr, Alexandra Schoos, Kumiko Oida, Josef Singer, Lucia Panakova, Krisztina Manzano-Szalai, and Erika Jensen-Jarolim. “Generation of Recombinant FcεRIα of Dog, Cat and Horse for Component-Resolved Allergy Diagnosis in Veterinary Patients.” <i>Journal of Allergy and Clinical Immunology</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.jaci.2014.12.1263\">https://doi.org/10.1016/j.jaci.2014.12.1263</a>.","ama":"Einhorn L, Singer J, Muhr M, et al. Generation of recombinant FcεRIα of dog, cat and horse for component-resolved allergy diagnosis in veterinary patients. <i>Journal of Allergy and Clinical Immunology</i>. 2015;135(2). doi:<a href=\"https://doi.org/10.1016/j.jaci.2014.12.1263\">10.1016/j.jaci.2014.12.1263</a>","ista":"Einhorn L, Singer J, Muhr M, Schoos A, Oida K, Singer J, Panakova L, Manzano-Szalai K, Jensen-Jarolim E. 2015. Generation of recombinant FcεRIα of dog, cat and horse for component-resolved allergy diagnosis in veterinary patients. Journal of Allergy and Clinical Immunology. 135(2), AB101.","short":"L. Einhorn, J. Singer, M. Muhr, A. Schoos, K. Oida, J. Singer, L. Panakova, K. Manzano-Szalai, E. Jensen-Jarolim, Journal of Allergy and Clinical Immunology 135 (2015).","mla":"Einhorn, Lukas, et al. “Generation of Recombinant FcεRIα of Dog, Cat and Horse for Component-Resolved Allergy Diagnosis in Veterinary Patients.” <i>Journal of Allergy and Clinical Immunology</i>, vol. 135, no. 2, AB101, Elsevier, 2015, doi:<a href=\"https://doi.org/10.1016/j.jaci.2014.12.1263\">10.1016/j.jaci.2014.12.1263</a>."},"oa_version":"None","language":[{"iso":"eng"}],"publisher":"Elsevier","date_published":"2015-02-01T00:00:00Z","article_processing_charge":"No","title":"Generation of recombinant FcεRIα of dog, cat and horse for component-resolved allergy diagnosis in veterinary patients","volume":135,"month":"02","publication_status":"published","issue":"2","article_number":"AB101"},{"acknowledgement":"European Research Council with a Starting Independent Research grant: ERC-2007-Stg-207362-HCPO, Czech Science Foundation: GA13-39982S\nWe thank Matyas Fendrych for critical reading and comments. The protocol was developed based on previously published work of De Rybel et al. (2010) and Laskowski et al. (2008). ","day":"20","year":"2015","status":"public","doi":"10.21769/BioProtoc.1446","date_created":"2018-12-11T11:48:44Z","type":"journal_article","_id":"832","publist_id":"6816","intvolume":"         5","publication":"Bio-protocol","author":[{"orcid":"0000-0001-5227-5741","last_name":"Marhavy","first_name":"Peter","full_name":"Peter Marhavy","id":"3F45B078-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Eva","last_name":"Benková","orcid":"0000-0002-8510-9739","id":"38F4F166-F248-11E8-B48F-1D18A9856A87","full_name":"Eva Benková"}],"quality_controlled":0,"extern":1,"date_updated":"2021-01-12T08:18:07Z","citation":{"ieee":"P. Marhavý and E. Benková, “Real time analysis of lateral root organogenesis in arabidopsis,” <i>Bio-protocol</i>, vol. 5, no. 8. Bio-protocol LLC, 2015.","apa":"Marhavý, P., &#38; Benková, E. (2015). Real time analysis of lateral root organogenesis in arabidopsis. <i>Bio-Protocol</i>. Bio-protocol LLC. <a href=\"https://doi.org/10.21769/BioProtoc.1446\">https://doi.org/10.21769/BioProtoc.1446</a>","ista":"Marhavý P, Benková E. 2015. Real time analysis of lateral root organogenesis in arabidopsis. Bio-protocol. 5(8).","chicago":"Marhavý, Peter, and Eva Benková. “Real Time Analysis of Lateral Root Organogenesis in Arabidopsis.” <i>Bio-Protocol</i>. Bio-protocol LLC, 2015. <a href=\"https://doi.org/10.21769/BioProtoc.1446\">https://doi.org/10.21769/BioProtoc.1446</a>.","ama":"Marhavý P, Benková E. Real time analysis of lateral root organogenesis in arabidopsis. <i>Bio-protocol</i>. 2015;5(8). doi:<a href=\"https://doi.org/10.21769/BioProtoc.1446\">10.21769/BioProtoc.1446</a>","short":"P. Marhavý, E. Benková, Bio-Protocol 5 (2015).","mla":"Marhavý, Peter, and Eva Benková. “Real Time Analysis of Lateral Root Organogenesis in Arabidopsis.” <i>Bio-Protocol</i>, vol. 5, no. 8, Bio-protocol LLC, 2015, doi:<a href=\"https://doi.org/10.21769/BioProtoc.1446\">10.21769/BioProtoc.1446</a>."},"publisher":"Bio-protocol LLC","date_published":"2015-04-20T00:00:00Z","title":"Real time analysis of lateral root organogenesis in arabidopsis","volume":5,"month":"04","publication_status":"published","abstract":[{"lang":"eng","text":"Plants maintain capacity to form new organs such as leaves, flowers, lateral shoots and roots throughout their postembryonic lifetime. Lateral roots (LRs) originate from a few pericycle cells that acquire attributes of founder cells (FCs), undergo series of anticlinal divisions, and give rise to a few short initial cells. After initiation, coordinated cell division and differentiation occur, giving rise to lateral root primordia (LRP). Primordia continue to grow, emerge through the cortex and epidermal layers of the primary root, and finally a new apical meristem is established taking over the responsibility for growth of mature lateral roots [for detailed description of the individual stages of lateral root organogenesis see Malamy and Benfey (1997)]. To examine this highly dynamic developmental process and to investigate a role of various hormonal, genetic and environmental factors in the regulation of lateral root organogenesis, the real time imaging based analyses represent extremely powerful tools (Laskowski et al., 2008; De Smet et al., 2012; Marhavy et al., 2013 and 2014). Herein, we describe a protocol for real time lateral root primordia (LRP) analysis, which enables the monitoring of an onset of the specific gene expression and subcellular protein localization during primordia organogenesis, as well as the evaluation of the impact of genetic and environmental perturbations on LRP organogenesis."}],"issue":"8"},{"type":"journal_article","_id":"8456","article_type":"original","date_created":"2020-09-18T10:07:36Z","year":"2015","status":"public","day":"05","doi":"10.1038/ncomms9361","publication_identifier":{"issn":["2041-1723"]},"keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"publication":"Nature Communications","intvolume":"         6","oa_version":"Published Version","citation":{"mla":"Ma, Peixiang, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>, vol. 6, 8361, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>.","short":"P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015).","ista":"Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P. 2015. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6, 8361.","chicago":"Ma, Peixiang, Yi Xue, Nicolas Coquelle, Jens D. Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>.","ama":"Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>","apa":"Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>","ieee":"P. Ma <i>et al.</i>, “Observing the overall rocking motion of a protein in a crystal,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015."},"date_updated":"2021-01-12T08:19:24Z","extern":"1","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"last_name":"Ma","first_name":"Peixiang","full_name":"Ma, Peixiang"},{"full_name":"Xue, Yi","first_name":"Yi","last_name":"Xue"},{"last_name":"Coquelle","first_name":"Nicolas","full_name":"Coquelle, Nicolas"},{"full_name":"Haller, Jens D.","first_name":"Jens D.","last_name":"Haller"},{"full_name":"Yuwen, Tairan","first_name":"Tairan","last_name":"Yuwen"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"first_name":"Oleg","last_name":"Mikhailovskii","full_name":"Mikhailovskii, Oleg"},{"first_name":"Dieter","last_name":"Willbold","full_name":"Willbold, Dieter"},{"full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe","last_name":"Colletier"},{"last_name":"Skrynnikov","first_name":"Nikolai R.","full_name":"Skrynnikov, Nikolai R."},{"orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"article_number":"8361","abstract":[{"text":"The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall ‘rocking’ motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments.","lang":"eng"}],"month":"10","publication_status":"published","article_processing_charge":"No","volume":6,"title":"Observing the overall rocking motion of a protein in a crystal","date_published":"2015-10-05T00:00:00Z","publisher":"Springer Nature","language":[{"iso":"eng"}]},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Peixiang","last_name":"Ma","full_name":"Ma, Peixiang"},{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"}],"oa_version":"None","citation":{"short":"P. Ma, P. Schanda, EMagRes 4 (2015) 699–708.","mla":"Ma, Peixiang, and Paul Schanda. “Conformational Exchange Processes in Biological Systems: Detection by Solid-State NMR.” <i>EMagRes</i>, vol. 4, no. 3, Wiley, 2015, pp. 699–708, doi:<a href=\"https://doi.org/10.1002/9780470034590.emrstm1418\">10.1002/9780470034590.emrstm1418</a>.","ista":"Ma P, Schanda P. 2015. Conformational exchange processes in biological systems: Detection by solid-state NMR. eMagRes. 4(3), 699–708.","ama":"Ma P, Schanda P. Conformational exchange processes in biological systems: Detection by solid-state NMR. <i>eMagRes</i>. 2015;4(3):699-708. doi:<a href=\"https://doi.org/10.1002/9780470034590.emrstm1418\">10.1002/9780470034590.emrstm1418</a>","chicago":"Ma, Peixiang, and Paul Schanda. “Conformational Exchange Processes in Biological Systems: Detection by Solid-State NMR.” <i>EMagRes</i>. Wiley, 2015. <a href=\"https://doi.org/10.1002/9780470034590.emrstm1418\">https://doi.org/10.1002/9780470034590.emrstm1418</a>.","apa":"Ma, P., &#38; Schanda, P. (2015). Conformational exchange processes in biological systems: Detection by solid-state NMR. <i>EMagRes</i>. Wiley. <a href=\"https://doi.org/10.1002/9780470034590.emrstm1418\">https://doi.org/10.1002/9780470034590.emrstm1418</a>","ieee":"P. Ma and P. Schanda, “Conformational exchange processes in biological systems: Detection by solid-state NMR,” <i>eMagRes</i>, vol. 4, no. 3. Wiley, pp. 699–708, 2015."},"extern":"1","quality_controlled":"1","date_updated":"2021-01-12T08:19:24Z","title":"Conformational exchange processes in biological systems: Detection by solid-state NMR","volume":4,"article_processing_charge":"No","date_published":"2015-09-10T00:00:00Z","publisher":"Wiley","language":[{"iso":"eng"}],"issue":"3","publication_status":"published","month":"09","abstract":[{"text":"We review recent advances in methodologies to study microseconds‐to‐milliseconds exchange processes in biological molecules using magic‐angle spinning solid‐state nuclear magnetic resonance (MAS ssNMR) spectroscopy. The particularities of MAS ssNMR, as compared to solution‐state NMR, are elucidated using numerical simulations and experimental data. These simulations reveal the potential of MAS NMR to provide detailed insight into short‐lived conformations of biological molecules. Recent studies of conformational exchange dynamics in microcrystalline ubiquitin are discussed.","lang":"eng"}],"publication_identifier":{"isbn":["9780470034590","9780470058213"]},"page":"699-708","doi":"10.1002/9780470034590.emrstm1418","day":"10","year":"2015","status":"public","article_type":"original","type":"journal_article","_id":"8457","date_created":"2020-09-18T10:07:45Z","publication":"eMagRes","intvolume":"         4"},{"_id":"848","type":"journal_article","date_created":"2018-12-11T11:48:49Z","doi":"10.1093/molbev/msu318","year":"2015","page":"542 - 554","status":"public","day":"01","publication":"Molecular Biology and Evolution","intvolume":"        32","publist_id":"6804","citation":{"apa":"Usmanova, D., Ferretti, L., Povolotskaya, I., Vlasov, P., &#38; Kondrashov, F. (2015). A model of substitution trajectories in sequence space and long-term protein evolution. <i>Molecular Biology and Evolution</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/molbev/msu318\">https://doi.org/10.1093/molbev/msu318</a>","chicago":"Usmanova, Dinara, Luca Ferretti, Inna Povolotskaya, Peter Vlasov, and Fyodor Kondrashov. “A Model of Substitution Trajectories in Sequence Space and Long-Term Protein Evolution.” <i>Molecular Biology and Evolution</i>. Oxford University Press, 2015. <a href=\"https://doi.org/10.1093/molbev/msu318\">https://doi.org/10.1093/molbev/msu318</a>.","ista":"Usmanova D, Ferretti L, Povolotskaya I, Vlasov P, Kondrashov F. 2015. A model of substitution trajectories in sequence space and long-term protein evolution. Molecular Biology and Evolution. 32(2), 542–554.","ama":"Usmanova D, Ferretti L, Povolotskaya I, Vlasov P, Kondrashov F. A model of substitution trajectories in sequence space and long-term protein evolution. <i>Molecular Biology and Evolution</i>. 2015;32(2):542-554. doi:<a href=\"https://doi.org/10.1093/molbev/msu318\">10.1093/molbev/msu318</a>","ieee":"D. Usmanova, L. Ferretti, I. Povolotskaya, P. Vlasov, and F. Kondrashov, “A model of substitution trajectories in sequence space and long-term protein evolution,” <i>Molecular Biology and Evolution</i>, vol. 32, no. 2. Oxford University Press, pp. 542–554, 2015.","short":"D. Usmanova, L. Ferretti, I. Povolotskaya, P. Vlasov, F. Kondrashov, Molecular Biology and Evolution 32 (2015) 542–554.","mla":"Usmanova, Dinara, et al. “A Model of Substitution Trajectories in Sequence Space and Long-Term Protein Evolution.” <i>Molecular Biology and Evolution</i>, vol. 32, no. 2, Oxford University Press, 2015, pp. 542–54, doi:<a href=\"https://doi.org/10.1093/molbev/msu318\">10.1093/molbev/msu318</a>."},"oa_version":"None","date_updated":"2021-01-12T08:19:33Z","quality_controlled":"1","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Dinara","last_name":"Usmanova","full_name":"Usmanova, Dinara"},{"full_name":"Ferretti, Luca","first_name":"Luca","last_name":"Ferretti"},{"first_name":"Inna","last_name":"Povolotskaya","full_name":"Povolotskaya, Inna"},{"first_name":"Peter","last_name":"Vlasov","full_name":"Vlasov, Peter"},{"id":"44FDEF62-F248-11E8-B48F-1D18A9856A87","full_name":"Kondrashov, Fyodor","first_name":"Fyodor","last_name":"Kondrashov","orcid":"0000-0001-8243-4694"}],"issue":"2","abstract":[{"lang":"eng","text":"The nature of factors governing the tempo and mode of protein evolution is a fundamental issue in evolutionary biology. Specifically, whether or not interactions between different sites, or epistasis, are important in directing the course of evolution became one of the central questions. Several recent reports have scrutinized patterns of long-term protein evolution claiming them to be compatible only with an epistatic fitness landscape. However, these claims have not yet been substantiated with a formal model of protein evolution. Here, we formulate a simple covarion-like model of protein evolution focusing on the rate at which the fitness impact of amino acids at a site changes with time. We then apply the model to the data on convergent and divergent protein evolution to test whether or not the incorporation of epistatic interactions is necessary to explain the data. We find that convergent evolution cannot be explained without the incorporation of epistasis and the rate at which an amino acid state switches from being acceptable at a site to being deleterious is faster than the rate of amino acid substitution. Specifically, for proteins that have persisted in modern prokaryotic organisms since the last universal common ancestor for one amino acid substitution approximately ten amino acid states switch from being accessible to being deleterious, or vice versa. Thus, molecular evolution can only be perceived in the context of rapid turnover of which amino acids are available for evolution."}],"month":"02","publication_status":"published","volume":32,"title":"A model of substitution trajectories in sequence space and long-term protein evolution","date_published":"2015-02-01T00:00:00Z","publisher":"Oxford University Press","language":[{"iso":"eng"}]},{"publisher":"American Mathematical Society","language":[{"iso":"eng"}],"date_published":"2015-12-21T00:00:00Z","volume":144,"title":"A note on micro-instability for Hamiltonian systems close to integrable","article_processing_charge":"No","month":"12","publication_status":"published","abstract":[{"text":"In this note, we consider the dynamics associated to a perturbation of an integrable Hamiltonian system in action-angle coordinates in any number of degrees of freedom and we prove the following result of ``micro-diffusion'': under generic assumptions on $ h$ and $ f$, there exists an orbit of the system for which the drift of its action variables is at least of order $ \\sqrt {\\varepsilon }$, after a time of order $ \\sqrt {\\varepsilon }^{-1}$. The assumptions, which are essentially minimal, are that there exists a resonant point for $ h$ and that the corresponding averaged perturbation is non-constant. The conclusions, although very weak when compared to usual instability phenomena, are also essentially optimal within this setting.","lang":"eng"}],"issue":"4","author":[{"full_name":"Bounemoura, Abed","first_name":"Abed","last_name":"Bounemoura"},{"full_name":"Kaloshin, Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","orcid":"0000-0002-6051-2628","first_name":"Vadim","last_name":"Kaloshin"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","extern":"1","date_updated":"2021-01-12T08:19:40Z","citation":{"short":"A. Bounemoura, V. Kaloshin, Proceedings of the American Mathematical Society 144 (2015) 1553–1560.","mla":"Bounemoura, Abed, and Vadim Kaloshin. “A Note on Micro-Instability for Hamiltonian Systems Close to Integrable.” <i>Proceedings of the American Mathematical Society</i>, vol. 144, no. 4, American Mathematical Society, 2015, pp. 1553–60, doi:<a href=\"https://doi.org/10.1090/proc/12796\">10.1090/proc/12796</a>.","apa":"Bounemoura, A., &#38; Kaloshin, V. (2015). A note on micro-instability for Hamiltonian systems close to integrable. <i>Proceedings of the American Mathematical Society</i>. American Mathematical Society. <a href=\"https://doi.org/10.1090/proc/12796\">https://doi.org/10.1090/proc/12796</a>","ama":"Bounemoura A, Kaloshin V. A note on micro-instability for Hamiltonian systems close to integrable. <i>Proceedings of the American Mathematical Society</i>. 2015;144(4):1553-1560. doi:<a href=\"https://doi.org/10.1090/proc/12796\">10.1090/proc/12796</a>","chicago":"Bounemoura, Abed, and Vadim Kaloshin. “A Note on Micro-Instability for Hamiltonian Systems Close to Integrable.” <i>Proceedings of the American Mathematical Society</i>. American Mathematical Society, 2015. <a href=\"https://doi.org/10.1090/proc/12796\">https://doi.org/10.1090/proc/12796</a>.","ista":"Bounemoura A, Kaloshin V. 2015. A note on micro-instability for Hamiltonian systems close to integrable. Proceedings of the American Mathematical Society. 144(4), 1553–1560.","ieee":"A. Bounemoura and V. Kaloshin, “A note on micro-instability for Hamiltonian systems close to integrable,” <i>Proceedings of the American Mathematical Society</i>, vol. 144, no. 4. American Mathematical Society, pp. 1553–1560, 2015."},"oa_version":"None","intvolume":"       144","publication":"Proceedings of the American Mathematical Society","day":"21","status":"public","year":"2015","doi":"10.1090/proc/12796","page":"1553-1560","publication_identifier":{"issn":["0002-9939","1088-6826"]},"date_created":"2020-09-18T10:46:14Z","article_type":"letter_note","type":"journal_article","_id":"8495"},{"page":"2699-2720","day":"30","publication_identifier":{"issn":["0951-7715","1361-6544"]},"doi":"10.1088/0951-7715/28/8/2699","year":"2015","status":"public","article_type":"original","_id":"8498","type":"journal_article","date_created":"2020-09-18T10:46:43Z","publication":"Nonlinearity","intvolume":"        28","keyword":["Mathematical Physics","General Physics and Astronomy","Applied Mathematics","Statistical and Nonlinear Physics"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Kaloshin, Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","orcid":"0000-0002-6051-2628","last_name":"Kaloshin","first_name":"Vadim"},{"full_name":"Zhang, K","first_name":"K","last_name":"Zhang"}],"oa_version":"None","citation":{"apa":"Kaloshin, V., &#38; Zhang, K. (2015). Arnold diffusion for smooth convex systems of two and a half degrees of freedom. <i>Nonlinearity</i>. IOP Publishing. <a href=\"https://doi.org/10.1088/0951-7715/28/8/2699\">https://doi.org/10.1088/0951-7715/28/8/2699</a>","ista":"Kaloshin V, Zhang K. 2015. Arnold diffusion for smooth convex systems of two and a half degrees of freedom. Nonlinearity. 28(8), 2699–2720.","chicago":"Kaloshin, Vadim, and K Zhang. “Arnold Diffusion for Smooth Convex Systems of Two and a Half Degrees of Freedom.” <i>Nonlinearity</i>. IOP Publishing, 2015. <a href=\"https://doi.org/10.1088/0951-7715/28/8/2699\">https://doi.org/10.1088/0951-7715/28/8/2699</a>.","ama":"Kaloshin V, Zhang K. Arnold diffusion for smooth convex systems of two and a half degrees of freedom. <i>Nonlinearity</i>. 2015;28(8):2699-2720. doi:<a href=\"https://doi.org/10.1088/0951-7715/28/8/2699\">10.1088/0951-7715/28/8/2699</a>","ieee":"V. Kaloshin and K. Zhang, “Arnold diffusion for smooth convex systems of two and a half degrees of freedom,” <i>Nonlinearity</i>, vol. 28, no. 8. IOP Publishing, pp. 2699–2720, 2015.","short":"V. Kaloshin, K. Zhang, Nonlinearity 28 (2015) 2699–2720.","mla":"Kaloshin, Vadim, and K. Zhang. “Arnold Diffusion for Smooth Convex Systems of Two and a Half Degrees of Freedom.” <i>Nonlinearity</i>, vol. 28, no. 8, IOP Publishing, 2015, pp. 2699–720, doi:<a href=\"https://doi.org/10.1088/0951-7715/28/8/2699\">10.1088/0951-7715/28/8/2699</a>."},"extern":"1","quality_controlled":"1","date_updated":"2021-01-12T08:19:41Z","title":"Arnold diffusion for smooth convex systems of two and a half degrees of freedom","volume":28,"article_processing_charge":"No","publisher":"IOP Publishing","date_published":"2015-06-30T00:00:00Z","language":[{"iso":"eng"}],"issue":"8","publication_status":"published","month":"06","abstract":[{"text":"In the present note we announce a proof of a strong form of Arnold diffusion for smooth convex Hamiltonian systems. Let ${\\mathbb T}^2$  be a 2-dimensional torus and B2 be the unit ball around the origin in ${\\mathbb R}^2$ . Fix ρ > 0. Our main result says that for a 'generic' time-periodic perturbation of an integrable system of two degrees of freedom $H_0(p)+\\varepsilon H_1(\\theta,p,t),\\quad \\ \\theta\\in {\\mathbb T}^2,\\ p\\in B^2,\\ t\\in {\\mathbb T}={\\mathbb R}/{\\mathbb Z}$ , with a strictly convex H0, there exists a ρ-dense orbit (θε, pε, t)(t) in ${\\mathbb T}^2 \\times B^2 \\times {\\mathbb T}$ , namely, a ρ-neighborhood of the orbit contains ${\\mathbb T}^2 \\times B^2 \\times {\\mathbb T}$ .\r\n\r\nOur proof is a combination of geometric and variational methods. The fundamental elements of the construction are the usage of crumpled normally hyperbolic invariant cylinders from [9], flower and simple normally hyperbolic invariant manifolds from [36] as well as their kissing property at a strong double resonance. This allows us to build a 'connected' net of three-dimensional normally hyperbolic invariant manifolds. To construct diffusing orbits along this net we employ a version of the Mather variational method [41] equipped with weak KAM theory [28], proposed by Bernard in [7].","lang":"eng"}]},{"publication":"Journal of the European Mathematical Society","intvolume":"        17","doi":"10.4171/jems/499","page":"71-149","publication_identifier":{"issn":["1435-9855"]},"year":"2015","status":"public","day":"05","article_type":"original","type":"journal_article","_id":"8499","date_created":"2020-09-18T10:46:50Z","volume":17,"title":"Growth of Sobolev norms in the cubic defocusing nonlinear Schrödinger equation","article_processing_charge":"No","date_published":"2015-02-05T00:00:00Z","language":[{"iso":"eng"}],"publisher":"European Mathematical Society Publishing House","issue":"1","month":"02","publication_status":"published","abstract":[{"lang":"eng","text":"We consider the cubic defocusing nonlinear Schrödinger equation in the two dimensional torus. Fix s>1. Recently Colliander, Keel, Staffilani, Tao and Takaoka proved the existence of solutions with s-Sobolev norm growing in time.\r\n\r\nWe establish the existence of solutions with polynomial time estimates. More exactly, there is c>0 such that for any K≫1 we find a solution u and a time T such that ∥u(T)∥Hs≥K∥u(0)∥Hs. Moreover, the time T satisfies the polynomial bound 0<T<Kc."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Marcel","last_name":"Guardia","full_name":"Guardia, Marcel"},{"last_name":"Kaloshin","first_name":"Vadim","orcid":"0000-0002-6051-2628","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","full_name":"Kaloshin, Vadim"}],"oa_version":"None","citation":{"mla":"Guardia, Marcel, and Vadim Kaloshin. “Growth of Sobolev Norms in the Cubic Defocusing Nonlinear Schrödinger Equation.” <i>Journal of the European Mathematical Society</i>, vol. 17, no. 1, European Mathematical Society Publishing House, 2015, pp. 71–149, doi:<a href=\"https://doi.org/10.4171/jems/499\">10.4171/jems/499</a>.","short":"M. Guardia, V. Kaloshin, Journal of the European Mathematical Society 17 (2015) 71–149.","ieee":"M. Guardia and V. Kaloshin, “Growth of Sobolev norms in the cubic defocusing nonlinear Schrödinger equation,” <i>Journal of the European Mathematical Society</i>, vol. 17, no. 1. European Mathematical Society Publishing House, pp. 71–149, 2015.","chicago":"Guardia, Marcel, and Vadim Kaloshin. “Growth of Sobolev Norms in the Cubic Defocusing Nonlinear Schrödinger Equation.” <i>Journal of the European Mathematical Society</i>. European Mathematical Society Publishing House, 2015. <a href=\"https://doi.org/10.4171/jems/499\">https://doi.org/10.4171/jems/499</a>.","ista":"Guardia M, Kaloshin V. 2015. Growth of Sobolev norms in the cubic defocusing nonlinear Schrödinger equation. Journal of the European Mathematical Society. 17(1), 71–149.","ama":"Guardia M, Kaloshin V. Growth of Sobolev norms in the cubic defocusing nonlinear Schrödinger equation. <i>Journal of the European Mathematical Society</i>. 2015;17(1):71-149. doi:<a href=\"https://doi.org/10.4171/jems/499\">10.4171/jems/499</a>","apa":"Guardia, M., &#38; Kaloshin, V. (2015). Growth of Sobolev norms in the cubic defocusing nonlinear Schrödinger equation. <i>Journal of the European Mathematical Society</i>. European Mathematical Society Publishing House. <a href=\"https://doi.org/10.4171/jems/499\">https://doi.org/10.4171/jems/499</a>"},"extern":"1","quality_controlled":"1","date_updated":"2021-01-12T08:19:41Z"},{"publist_id":"6783","intvolume":"       112","publication":"PNAS","date_created":"2018-12-11T11:48:55Z","_id":"866","type":"journal_article","acknowledgement":"We thank Isabel Wang and Vivian Cheung from the Life Sciences Institute, University of Michigan, for assistance with high- throughput sequencing experiments and valuable discussions. We also thank J. Evan Sadler (Washington University) and Sriram Krishnaswamy (Children’s Hospital of Philadelphia) for helpful discussions. We thank Jeff Weitz (McMaster University), Jim Fredenburgh (McMaster University), and Steve Weiss (University of Michigan) for critical review of the manuscript. C.A.K. was awarded the Judith Graham Pool Fellowship from National Hemophilia Foundation. This work was supported by the National Institutes of Health (R01 HL039693), the National Heart, Lung, and Blood Institute (P01- HL057346), Ministerio de Economía y Competitividad Grants BFU2012- 31329 and Sev-2012-0208, and European Research Council Starting Grant 335980_EinME. D.G. is an investigator of the Howard Hughes Medical In- stitute, and F.A.K. is a Howard Hughes Medical Institute International Early Career Scientist.\n","status":"public","year":"2015","day":"28","page":"9328 - 9333","doi":"10.1073/pnas.1511328112","month":"07","publication_status":"published","abstract":[{"text":"Proteases play important roles in many biologic processes and are key mediators of cancer, inflammation, and thrombosis. However, comprehensive and quantitative techniques to define the substrate specificity profile of proteases are lacking. The metalloprotease ADAMTS13 regulates blood coagulation by cleaving von Willebrand factor (VWF), reducing its procoagulant activity. A mutagenized substrate phage display library based on a 73-amino acid fragment of VWF was constructed, and the ADAMTS13-dependent change in library complexity was evaluated over reaction time points, using high-throughput sequencing. Reaction rate constants (kcat/KM) were calculated for nearly every possible single amino acid substitution within this fragment. This massively parallel enzyme kinetics analysis detailed the specificity of ADAMTS13 and demonstrated the critical importance of the P1-P1' substrate residues while defining exosite binding domains. These data provided empirical evidence for the propensity for epistasis within VWF and showed strong correlation to conservation across orthologs, highlighting evolutionary selective pressures for VWF.","lang":"eng"}],"issue":"30","publisher":"National Academy of Sciences","date_published":"2015-07-28T00:00:00Z","title":"Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13","volume":112,"extern":1,"quality_controlled":0,"date_updated":"2021-01-12T08:20:26Z","citation":{"mla":"Kretz, Colin, et al. “Massively Parallel Enzyme Kinetics Reveals the Substrate Recognition Landscape of the Metalloprotease ADAMTS13.” <i>PNAS</i>, vol. 112, no. 30, National Academy of Sciences, 2015, pp. 9328–33, doi:<a href=\"https://doi.org/10.1073/pnas.1511328112\">10.1073/pnas.1511328112</a>.","short":"C. Kretz, M. Dai, O. Soylemez, A. Yee, K. Desch, D. Siemieniak, K. Tomberg, F. Kondrashov, F. Meng, D. Ginsburg, PNAS 112 (2015) 9328–9333.","ieee":"C. Kretz <i>et al.</i>, “Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13,” <i>PNAS</i>, vol. 112, no. 30. National Academy of Sciences, pp. 9328–9333, 2015.","apa":"Kretz, C., Dai, M., Soylemez, O., Yee, A., Desch, K., Siemieniak, D., … Ginsburg, D. (2015). Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13. <i>PNAS</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1511328112\">https://doi.org/10.1073/pnas.1511328112</a>","ista":"Kretz C, Dai M, Soylemez O, Yee A, Desch K, Siemieniak D, Tomberg K, Kondrashov F, Meng F, Ginsburg D. 2015. Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13. PNAS. 112(30), 9328–9333.","ama":"Kretz C, Dai M, Soylemez O, et al. Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13. <i>PNAS</i>. 2015;112(30):9328-9333. doi:<a href=\"https://doi.org/10.1073/pnas.1511328112\">10.1073/pnas.1511328112</a>","chicago":"Kretz, Colin, Manhong Dai, Onuralp Soylemez, Andrew Yee, Karl Desch, David Siemieniak, Kärt Tomberg, Fyodor Kondrashov, Fan Meng, and David Ginsburg. “Massively Parallel Enzyme Kinetics Reveals the Substrate Recognition Landscape of the Metalloprotease ADAMTS13.” <i>PNAS</i>. National Academy of Sciences, 2015. <a href=\"https://doi.org/10.1073/pnas.1511328112\">https://doi.org/10.1073/pnas.1511328112</a>."},"author":[{"full_name":"Kretz, Colin A","first_name":"Colin","last_name":"Kretz"},{"full_name":"Dai, Manhong","first_name":"Manhong","last_name":"Dai"},{"last_name":"Soylemez","first_name":"Onuralp","full_name":"Soylemez, Onuralp"},{"first_name":"Andrew","last_name":"Yee","full_name":"Yee, Andrew"},{"full_name":"Desch, Karl C","first_name":"Karl","last_name":"Desch"},{"full_name":"Siemieniak, David R","last_name":"Siemieniak","first_name":"David"},{"last_name":"Tomberg","first_name":"Kärt","full_name":"Tomberg, Kärt"},{"orcid":"0000-0001-8243-4694","first_name":"Fyodor","last_name":"Kondrashov","full_name":"Fyodor Kondrashov","id":"44FDEF62-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Meng","first_name":"Fan","full_name":"Meng, Fan"},{"last_name":"Ginsburg","first_name":"David","full_name":"Ginsburg, David B"}]},{"quality_controlled":0,"extern":1,"date_updated":"2021-01-12T08:21:16Z","citation":{"short":"D. Kondrashov, F. Kondrashov, Trends in Genetics 31 (2015) 24–33.","mla":"Kondrashov, Dmitry, and Fyodor Kondrashov. “Topological Features of Rugged Fitness Landscapes in Sequence Space.” <i>Trends in Genetics</i>, vol. 31, no. 1, Elsevier, 2015, pp. 24–33, doi:<a href=\"https://doi.org/10.1016/j.tig.2014.09.009\">10.1016/j.tig.2014.09.009</a>.","ieee":"D. Kondrashov and F. Kondrashov, “Topological features of rugged fitness landscapes in sequence space,” <i>Trends in Genetics</i>, vol. 31, no. 1. Elsevier, pp. 24–33, 2015.","apa":"Kondrashov, D., &#38; Kondrashov, F. (2015). Topological features of rugged fitness landscapes in sequence space. <i>Trends in Genetics</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.tig.2014.09.009\">https://doi.org/10.1016/j.tig.2014.09.009</a>","chicago":"Kondrashov, Dmitry, and Fyodor Kondrashov. “Topological Features of Rugged Fitness Landscapes in Sequence Space.” <i>Trends in Genetics</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.tig.2014.09.009\">https://doi.org/10.1016/j.tig.2014.09.009</a>.","ama":"Kondrashov D, Kondrashov F. Topological features of rugged fitness landscapes in sequence space. <i>Trends in Genetics</i>. 2015;31(1):24-33. doi:<a href=\"https://doi.org/10.1016/j.tig.2014.09.009\">10.1016/j.tig.2014.09.009</a>","ista":"Kondrashov D, Kondrashov F. 2015. Topological features of rugged fitness landscapes in sequence space. Trends in Genetics. 31(1), 24–33."},"author":[{"full_name":"Kondrashov, Dmitry A","last_name":"Kondrashov","first_name":"Dmitry"},{"orcid":"0000-0001-8243-4694","first_name":"Fyodor","last_name":"Kondrashov","full_name":"Fyodor Kondrashov","id":"44FDEF62-F248-11E8-B48F-1D18A9856A87"}],"publication_status":"published","month":"01","abstract":[{"lang":"eng","text":"The factors that determine the tempo and mode of protein evolution continue to be a central question in molecular evolution. Traditionally, studies of protein evolution focused on the rates of amino acid substitutions. More recently, with the availability of sequence data and advanced experimental techniques, the focus of attention has shifted toward the study of evolutionary trajectories and the overall layout of protein fitness landscapes. In this review we describe the effect of epistasis on the topology of evolutionary pathways that are likely to be found in fitness landscapes and develop a simple theory to connect the number of maladapted genotypes to the topology of fitness landscapes with epistatic interactions. Finally, we review recent studies that have probed the extent of epistatic interactions and have begun to chart the fitness landscapes in protein sequence space."}],"issue":"1","date_published":"2015-01-01T00:00:00Z","publisher":"Elsevier","volume":31,"title":"Topological features of rugged fitness landscapes in sequence space","date_created":"2018-12-11T11:49:01Z","_id":"886","type":"journal_article","acknowledgement":"This work has been supported by a grant from the HHMI International Early Career Scientist Program (#55007424), the Spanish Ministry of Economy and Competitiveness (grant #BFU2012-31329) as part of the EMBO YIP program, two grants from the Spanish Ministry of Economy and Competitiveness, Centro de Excelencia Severo Ochoa 2013–2017 (#Sev-2012-0208) and BES-2013-064004 funded by the European Regional Development Fund (ERDF), the European Union, and the European Research Council under grant agreement no 335980_EinME.","doi":"10.1016/j.tig.2014.09.009","page":"24 - 33","day":"01","year":"2015","status":"public","publist_id":"6764","intvolume":"        31","publication":"Trends in Genetics"},{"pubrep_id":"470","status":"public","date_created":"2018-12-11T11:53:02Z","type":"journal_article","_id":"1615","language":[{"iso":"eng"}],"volume":13,"has_accepted_license":"1","month":"10","issue":"3","file":[{"file_name":"IST-2016-470-v1+1_1-s2.0-S2211124715010220-main.pdf","content_type":"application/pdf","date_updated":"2020-07-14T12:45:07Z","date_created":"2018-12-12T10:13:23Z","creator":"system","file_id":"5005","checksum":"44d30fbb543774b076b4938bd36af9d7","file_size":2314406,"access_level":"open_access","relation":"main_file"}],"author":[{"full_name":"Hammer, Matthieu","last_name":"Hammer","first_name":"Matthieu"},{"full_name":"Krueger Burg, Dilja","first_name":"Dilja","last_name":"Krueger Burg"},{"full_name":"Tuffy, Liam","first_name":"Liam","last_name":"Tuffy"},{"full_name":"Cooper, Benjamin","last_name":"Cooper","first_name":"Benjamin"},{"full_name":"Taschenberger, Holger","first_name":"Holger","last_name":"Taschenberger"},{"first_name":"Sarit","last_name":"Goswami","full_name":"Goswami, Sarit","id":"3A578F32-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Ehrenreich, Hannelore","last_name":"Ehrenreich","first_name":"Hannelore"},{"first_name":"Peter M","last_name":"Jonas","orcid":"0000-0001-5001-4804","id":"353C1B58-F248-11E8-B48F-1D18A9856A87","full_name":"Jonas, Peter M"},{"full_name":"Varoqueaux, Frederique","first_name":"Frederique","last_name":"Varoqueaux"},{"full_name":"Rhee, Jeong","last_name":"Rhee","first_name":"Jeong"},{"full_name":"Brose, Nils","first_name":"Nils","last_name":"Brose"}],"quality_controlled":"1","oa_version":"Published Version","intvolume":"        13","publist_id":"5551","publication":"Cell Reports","scopus_import":1,"acknowledgement":"This work was supported by the Max Planck Society (N.B. and H.E.), the European Commission (EU-AIMS FP7-115300, N.B. and H.E.; Marie Curie IRG, D.K.-B.), the German Research Foundation (CNMPB, N.B., H.E., and F.V.), the Alexander von Humboldt-Foundation (D.K.-B.), and the Austrian Fond zur Förderung der Wissenschaftlichen Forschung (P 24909-B24, P.J.). M.H. was a student of the doctoral program Molecular Physiology of the Brain. Dr. J.-M. Fritschy generously provided the GABAARγ2 antibody. We thank F. Benseler, I. Thanhäuser, D. Schwerdtfeger, A. Ronnenberg, and D. Winkler for valuable advice and excellent technical support. We are grateful to the staff at the animal facility of the Max Planck Institute of Experimental Medicine for mouse husbandry.","day":"20","doi":"10.1016/j.celrep.2015.09.011","year":"2015","page":"516 - 523","oa":1,"file_date_updated":"2020-07-14T12:45:07Z","date_published":"2015-10-20T00:00:00Z","publisher":"Cell Press","title":"Perturbed hippocampal synaptic inhibition and γ-oscillations in a neuroligin-4 knockout mouse model of autism","abstract":[{"lang":"eng","text":"Loss-of-function mutations in the synaptic adhesion protein Neuroligin-4 are among the most common genetic abnormalities associated with autism spectrum disorders, but little is known about the function of Neuroligin-4 and the consequences of its loss. We assessed synaptic and network characteristics in Neuroligin-4 knockout mice, focusing on the hippocampus as a model brain region with a critical role in cognition and memory, and found that Neuroligin-4 deletion causes subtle defects of the protein composition and function of GABAergic synapses in the hippocampal CA3 region. Interestingly, these subtle synaptic changes are accompanied by pronounced perturbations of γ-oscillatory network activity, which has been implicated in cognitive function and is altered in multiple psychiatric and neurodevelopmental disorders. Our data provide important insights into the mechanisms by which Neuroligin-4-dependent GABAergic synapses may contribute to autism phenotypes and indicate new strategies for therapeutic approaches."}],"publication_status":"published","ddc":["570"],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T06:52:01Z","department":[{"_id":"PeJo"}],"citation":{"ama":"Hammer M, Krueger Burg D, Tuffy L, et al. Perturbed hippocampal synaptic inhibition and γ-oscillations in a neuroligin-4 knockout mouse model of autism. <i>Cell Reports</i>. 2015;13(3):516-523. doi:<a href=\"https://doi.org/10.1016/j.celrep.2015.09.011\">10.1016/j.celrep.2015.09.011</a>","ista":"Hammer M, Krueger Burg D, Tuffy L, Cooper B, Taschenberger H, Goswami S, Ehrenreich H, Jonas PM, Varoqueaux F, Rhee J, Brose N. 2015. Perturbed hippocampal synaptic inhibition and γ-oscillations in a neuroligin-4 knockout mouse model of autism. Cell Reports. 13(3), 516–523.","chicago":"Hammer, Matthieu, Dilja Krueger Burg, Liam Tuffy, Benjamin Cooper, Holger Taschenberger, Sarit Goswami, Hannelore Ehrenreich, et al. “Perturbed Hippocampal Synaptic Inhibition and γ-Oscillations in a Neuroligin-4 Knockout Mouse Model of Autism.” <i>Cell Reports</i>. Cell Press, 2015. <a href=\"https://doi.org/10.1016/j.celrep.2015.09.011\">https://doi.org/10.1016/j.celrep.2015.09.011</a>.","apa":"Hammer, M., Krueger Burg, D., Tuffy, L., Cooper, B., Taschenberger, H., Goswami, S., … Brose, N. (2015). Perturbed hippocampal synaptic inhibition and γ-oscillations in a neuroligin-4 knockout mouse model of autism. <i>Cell Reports</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.celrep.2015.09.011\">https://doi.org/10.1016/j.celrep.2015.09.011</a>","ieee":"M. Hammer <i>et al.</i>, “Perturbed hippocampal synaptic inhibition and γ-oscillations in a neuroligin-4 knockout mouse model of autism,” <i>Cell Reports</i>, vol. 13, no. 3. Cell Press, pp. 516–523, 2015.","mla":"Hammer, Matthieu, et al. “Perturbed Hippocampal Synaptic Inhibition and γ-Oscillations in a Neuroligin-4 Knockout Mouse Model of Autism.” <i>Cell Reports</i>, vol. 13, no. 3, Cell Press, 2015, pp. 516–23, doi:<a href=\"https://doi.org/10.1016/j.celrep.2015.09.011\">10.1016/j.celrep.2015.09.011</a>.","short":"M. Hammer, D. Krueger Burg, L. Tuffy, B. Cooper, H. Taschenberger, S. Goswami, H. Ehrenreich, P.M. Jonas, F. Varoqueaux, J. Rhee, N. Brose, Cell Reports 13 (2015) 516–523."}},{"ec_funded":1,"type":"journal_article","_id":"1618","date_created":"2018-12-11T11:53:03Z","status":"public","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4809050/"}],"issue":"27","month":"06","article_processing_charge":"No","volume":54,"language":[{"iso":"eng"}],"oa_version":"Submitted Version","quality_controlled":"1","project":[{"name":"Cytoskeletal force generation and force transduction of migrating leukocytes (EU)","grant_number":"281556","_id":"25A603A2-B435-11E9-9278-68D0E5697425","call_identifier":"FP7"}],"author":[{"last_name":"Veldkamp","first_name":"Christopher","full_name":"Veldkamp, Christopher"},{"full_name":"Kiermaier, Eva","id":"3EB04B78-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6165-5738","first_name":"Eva","last_name":"Kiermaier"},{"full_name":"Gabel Eissens, Skylar","first_name":"Skylar","last_name":"Gabel Eissens"},{"full_name":"Gillitzer, Miranda","last_name":"Gillitzer","first_name":"Miranda"},{"last_name":"Lippner","first_name":"David","full_name":"Lippner, David"},{"full_name":"Disilvio, Frank","first_name":"Frank","last_name":"Disilvio"},{"full_name":"Mueller, Casey","first_name":"Casey","last_name":"Mueller"},{"first_name":"Paeton","last_name":"Wantuch","full_name":"Wantuch, Paeton"},{"full_name":"Chaffee, Gary","first_name":"Gary","last_name":"Chaffee"},{"first_name":"Michael","last_name":"Famiglietti","full_name":"Famiglietti, Michael"},{"last_name":"Zgoba","first_name":"Danielle","full_name":"Zgoba, Danielle"},{"full_name":"Bailey, Asha","last_name":"Bailey","first_name":"Asha"},{"full_name":"Bah, Yaya","first_name":"Yaya","last_name":"Bah"},{"full_name":"Engebretson, Samantha","first_name":"Samantha","last_name":"Engebretson"},{"last_name":"Graupner","first_name":"David","full_name":"Graupner, David"},{"full_name":"Lackner, Emily","last_name":"Lackner","first_name":"Emily"},{"first_name":"Vincent","last_name":"Larosa","full_name":"Larosa, Vincent"},{"first_name":"Tysha","last_name":"Medeiros","full_name":"Medeiros, Tysha"},{"full_name":"Olson, Michael","first_name":"Michael","last_name":"Olson"},{"last_name":"Phillips","first_name":"Andrew","full_name":"Phillips, Andrew"},{"full_name":"Pyles, Harley","last_name":"Pyles","first_name":"Harley"},{"first_name":"Amanda","last_name":"Richard","full_name":"Richard, Amanda"},{"full_name":"Schoeller, Scott","last_name":"Schoeller","first_name":"Scott"},{"full_name":"Touzeau, Boris","last_name":"Touzeau","first_name":"Boris"},{"last_name":"Williams","first_name":"Larry","full_name":"Williams, Larry"},{"full_name":"Sixt, Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179","last_name":"Sixt","first_name":"Michael K"},{"full_name":"Peterson, Francis","first_name":"Francis","last_name":"Peterson"}],"scopus_import":"1","publication":"Biochemistry","intvolume":"        54","publist_id":"5548","oa":1,"year":"2015","page":"4163 - 4166","doi":"10.1021/acs.biochem.5b00560","day":"26","abstract":[{"lang":"eng","text":"CCL19 and CCL21 are chemokines involved in the trafficking of immune cells, particularly within the lymphatic system, through activation of CCR7. Concurrent expression of PSGL-1 and CCR7 in naive T-cells enhances recruitment of these cells to secondary lymphoid organs by CCL19 and CCL21. Here the solution structure of CCL19 is reported. It contains a canonical chemokine domain. Chemical shift mapping shows the N-termini of PSGL-1 and CCR7 have overlapping binding sites for CCL19 and binding is competitive. Implications for the mechanism of PSGL-1's enhancement of resting T-cell recruitment are discussed."}],"publication_status":"published","title":"Solution structure of CCL19 and identification of overlapping CCR7 and PSGL-1 binding sites","date_published":"2015-06-26T00:00:00Z","publisher":"American Chemical Society","pmid":1,"citation":{"mla":"Veldkamp, Christopher, et al. “Solution Structure of CCL19 and Identification of Overlapping CCR7 and PSGL-1 Binding Sites.” <i>Biochemistry</i>, vol. 54, no. 27, American Chemical Society, 2015, pp. 4163–66, doi:<a href=\"https://doi.org/10.1021/acs.biochem.5b00560\">10.1021/acs.biochem.5b00560</a>.","short":"C. Veldkamp, E. Kiermaier, S. Gabel Eissens, M. Gillitzer, D. Lippner, F. Disilvio, C. Mueller, P. Wantuch, G. Chaffee, M. Famiglietti, D. Zgoba, A. Bailey, Y. Bah, S. Engebretson, D. Graupner, E. Lackner, V. Larosa, T. Medeiros, M. Olson, A. Phillips, H. Pyles, A. Richard, S. Schoeller, B. Touzeau, L. Williams, M.K. Sixt, F. Peterson, Biochemistry 54 (2015) 4163–4166.","ieee":"C. Veldkamp <i>et al.</i>, “Solution structure of CCL19 and identification of overlapping CCR7 and PSGL-1 binding sites,” <i>Biochemistry</i>, vol. 54, no. 27. American Chemical Society, pp. 4163–4166, 2015.","apa":"Veldkamp, C., Kiermaier, E., Gabel Eissens, S., Gillitzer, M., Lippner, D., Disilvio, F., … Peterson, F. (2015). Solution structure of CCL19 and identification of overlapping CCR7 and PSGL-1 binding sites. <i>Biochemistry</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.biochem.5b00560\">https://doi.org/10.1021/acs.biochem.5b00560</a>","chicago":"Veldkamp, Christopher, Eva Kiermaier, Skylar Gabel Eissens, Miranda Gillitzer, David Lippner, Frank Disilvio, Casey Mueller, et al. “Solution Structure of CCL19 and Identification of Overlapping CCR7 and PSGL-1 Binding Sites.” <i>Biochemistry</i>. American Chemical Society, 2015. <a href=\"https://doi.org/10.1021/acs.biochem.5b00560\">https://doi.org/10.1021/acs.biochem.5b00560</a>.","ista":"Veldkamp C, Kiermaier E, Gabel Eissens S, Gillitzer M, Lippner D, Disilvio F, Mueller C, Wantuch P, Chaffee G, Famiglietti M, Zgoba D, Bailey A, Bah Y, Engebretson S, Graupner D, Lackner E, Larosa V, Medeiros T, Olson M, Phillips A, Pyles H, Richard A, Schoeller S, Touzeau B, Williams L, Sixt MK, Peterson F. 2015. Solution structure of CCL19 and identification of overlapping CCR7 and PSGL-1 binding sites. Biochemistry. 54(27), 4163–4166.","ama":"Veldkamp C, Kiermaier E, Gabel Eissens S, et al. Solution structure of CCL19 and identification of overlapping CCR7 and PSGL-1 binding sites. <i>Biochemistry</i>. 2015;54(27):4163-4166. doi:<a href=\"https://doi.org/10.1021/acs.biochem.5b00560\">10.1021/acs.biochem.5b00560</a>"},"date_updated":"2023-03-30T11:32:57Z","department":[{"_id":"MiSi"}],"user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["26115234"]}},{"date_created":"2018-12-11T11:53:04Z","_id":"1619","type":"journal_article","status":"public","pubrep_id":"468","ec_funded":1,"project":[{"name":"Revealing the fundamental limits of cell growth","_id":"25EB3A80-B435-11E9-9278-68D0E5697425","grant_number":"RGP0042/2013"},{"call_identifier":"FWF","name":"Revealing the mechanisms underlying drug interactions","grant_number":"P27201-B22","_id":"25E9AF9E-B435-11E9-9278-68D0E5697425"},{"call_identifier":"FP7","_id":"25E83C2C-B435-11E9-9278-68D0E5697425","grant_number":"303507","name":"Optimality principles in responses to antibiotics"}],"quality_controlled":"1","oa_version":"Published Version","author":[{"last_name":"Chevereau","first_name":"Guillaume","id":"424D78A0-F248-11E8-B48F-1D18A9856A87","full_name":"Chevereau, Guillaume"},{"full_name":"Dravecka, Marta","id":"4342E402-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-2519-8004","first_name":"Marta","last_name":"Dravecka"},{"full_name":"Batur, Tugce","first_name":"Tugce","last_name":"Batur"},{"last_name":"Guvenek","first_name":"Aysegul","full_name":"Guvenek, Aysegul"},{"full_name":"Ayhan, Dilay","first_name":"Dilay","last_name":"Ayhan"},{"full_name":"Toprak, Erdal","first_name":"Erdal","last_name":"Toprak"},{"last_name":"Bollenbach","first_name":"Mark Tobias","orcid":"0000-0003-4398-476X","id":"3E6DB97A-F248-11E8-B48F-1D18A9856A87","full_name":"Bollenbach, Mark Tobias"}],"month":"11","has_accepted_license":"1","issue":"11","article_number":"e1002299","file":[{"date_updated":"2020-07-14T12:45:07Z","date_created":"2018-12-12T10:09:00Z","content_type":"application/pdf","file_name":"IST-2016-468-v1+1_journal.pbio.1002299.pdf","relation":"main_file","file_size":1387760,"access_level":"open_access","creator":"system","file_id":"4723","checksum":"0e82e3279f50b15c6c170c042627802b"}],"language":[{"iso":"eng"}],"volume":13,"oa":1,"year":"2015","doi":"10.1371/journal.pbio.1002299","day":"18","related_material":{"record":[{"relation":"research_data","id":"9711","status":"public"},{"status":"public","relation":"research_data","id":"9765"},{"relation":"dissertation_contains","id":"6263","status":"public"}]},"scopus_import":1,"intvolume":"        13","publist_id":"5547","publication":"PLoS Biology","date_updated":"2024-03-25T23:30:14Z","department":[{"_id":"ToBo"}],"citation":{"ieee":"G. Chevereau <i>et al.</i>, “Quantifying the determinants of evolutionary dynamics leading to drug resistance,” <i>PLoS Biology</i>, vol. 13, no. 11. Public Library of Science, 2015.","apa":"Chevereau, G., Lukacisinova, M., Batur, T., Guvenek, A., Ayhan, D., Toprak, E., &#38; Bollenbach, M. T. (2015). Quantifying the determinants of evolutionary dynamics leading to drug resistance. <i>PLoS Biology</i>. Public Library of Science. <a href=\"https://doi.org/10.1371/journal.pbio.1002299\">https://doi.org/10.1371/journal.pbio.1002299</a>","chicago":"Chevereau, Guillaume, Marta Lukacisinova, Tugce Batur, Aysegul Guvenek, Dilay Ayhan, Erdal Toprak, and Mark Tobias Bollenbach. “Quantifying the Determinants of Evolutionary Dynamics Leading to Drug Resistance.” <i>PLoS Biology</i>. Public Library of Science, 2015. <a href=\"https://doi.org/10.1371/journal.pbio.1002299\">https://doi.org/10.1371/journal.pbio.1002299</a>.","ista":"Chevereau G, Lukacisinova M, Batur T, Guvenek A, Ayhan D, Toprak E, Bollenbach MT. 2015. Quantifying the determinants of evolutionary dynamics leading to drug resistance. PLoS Biology. 13(11), e1002299.","ama":"Chevereau G, Lukacisinova M, Batur T, et al. Quantifying the determinants of evolutionary dynamics leading to drug resistance. <i>PLoS Biology</i>. 2015;13(11). doi:<a href=\"https://doi.org/10.1371/journal.pbio.1002299\">10.1371/journal.pbio.1002299</a>","short":"G. Chevereau, M. Lukacisinova, T. Batur, A. Guvenek, D. Ayhan, E. Toprak, M.T. Bollenbach, PLoS Biology 13 (2015).","mla":"Chevereau, Guillaume, et al. “Quantifying the Determinants of Evolutionary Dynamics Leading to Drug Resistance.” <i>PLoS Biology</i>, vol. 13, no. 11, e1002299, Public Library of Science, 2015, doi:<a href=\"https://doi.org/10.1371/journal.pbio.1002299\">10.1371/journal.pbio.1002299</a>."},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"text":"The emergence of drug resistant pathogens is a serious public health problem. It is a long-standing goal to predict rates of resistance evolution and design optimal treatment strategies accordingly. To this end, it is crucial to reveal the underlying causes of drug-specific differences in the evolutionary dynamics leading to resistance. However, it remains largely unknown why the rates of resistance evolution via spontaneous mutations and the diversity of mutational paths vary substantially between drugs. Here we comprehensively quantify the distribution of fitness effects (DFE) of mutations, a key determinant of evolutionary dynamics, in the presence of eight antibiotics representing the main modes of action. Using precise high-throughput fitness measurements for genome-wide Escherichia coli gene deletion strains, we find that the width of the DFE varies dramatically between antibiotics and, contrary to conventional wisdom, for some drugs the DFE width is lower than in the absence of stress. We show that this previously underappreciated divergence in DFE width among antibiotics is largely caused by their distinct drug-specific dose-response characteristics. Unlike the DFE, the magnitude of the changes in tolerated drug concentration resulting from genome-wide mutations is similar for most drugs but exceptionally small for the antibiotic nitrofurantoin, i.e., mutations generally have considerably smaller resistance effects for nitrofurantoin than for other drugs. A population genetics model predicts that resistance evolution for drugs with this property is severely limited and confined to reproducible mutational paths. We tested this prediction in laboratory evolution experiments using the “morbidostat”, a device for evolving bacteria in well-controlled drug environments. Nitrofurantoin resistance indeed evolved extremely slowly via reproducible mutations—an almost paradoxical behavior since this drug causes DNA damage and increases the mutation rate. Overall, we identified novel quantitative characteristics of the evolutionary landscape that provide the conceptual foundation for predicting the dynamics of drug resistance evolution.","lang":"eng"}],"publication_status":"published","ddc":["570"],"date_published":"2015-11-18T00:00:00Z","file_date_updated":"2020-07-14T12:45:07Z","publisher":"Public Library of Science","title":"Quantifying the determinants of evolutionary dynamics leading to drug resistance"},{"date_published":"2015-11-25T00:00:00Z","publisher":"BioMed Central","file_date_updated":"2020-07-14T12:45:07Z","title":"Single-cell screening of photosynthetic growth and lactate production by cyanobacteria","abstract":[{"text":"Background\r\nPhotosynthetic cyanobacteria are attractive for a range of biotechnological applications including biofuel production. However, due to slow growth, screening of mutant libraries using microtiter plates is not feasible.\r\nResults\r\nWe present a method for high-throughput, single-cell analysis and sorting of genetically engineered l-lactate-producing strains of Synechocystis sp. PCC6803. A microfluidic device is used to encapsulate single cells in picoliter droplets, assay the droplets for l-lactate production, and sort strains with high productivity. We demonstrate the separation of low- and high-producing reference strains, as well as enrichment of a more productive l-lactate-synthesizing population after UV-induced mutagenesis. The droplet platform also revealed population heterogeneity in photosynthetic growth and lactate production, as well as the presence of metabolically stalled cells.\r\nConclusions\r\nThe workflow will facilitate metabolic engineering and directed evolution studies and will be useful in studies of cyanobacteria biochemistry and physiology.\r\n","lang":"eng"}],"publication_status":"published","ddc":["570"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"date_updated":"2021-01-12T06:52:04Z","department":[{"_id":"ToBo"}],"citation":{"mla":"Hammar, Petter, et al. “Single-Cell Screening of Photosynthetic Growth and Lactate Production by Cyanobacteria.” <i>Biotechnology for Biofuels</i>, vol. 8, no. 1, 193, BioMed Central, 2015, doi:<a href=\"https://doi.org/10.1186/s13068-015-0380-2\">10.1186/s13068-015-0380-2</a>.","short":"P. Hammar, A. Angermayr, S. Sjostrom, J. Van Der Meer, K. Hellingwerf, E. Hudson, H. Joensson, Biotechnology for Biofuels 8 (2015).","ista":"Hammar P, Angermayr A, Sjostrom S, Van Der Meer J, Hellingwerf K, Hudson E, Joensson H. 2015. Single-cell screening of photosynthetic growth and lactate production by cyanobacteria. Biotechnology for Biofuels. 8(1), 193.","ama":"Hammar P, Angermayr A, Sjostrom S, et al. Single-cell screening of photosynthetic growth and lactate production by cyanobacteria. <i>Biotechnology for Biofuels</i>. 2015;8(1). doi:<a href=\"https://doi.org/10.1186/s13068-015-0380-2\">10.1186/s13068-015-0380-2</a>","chicago":"Hammar, Petter, Andreas Angermayr, Staffan Sjostrom, Josefin Van Der Meer, Klaas Hellingwerf, Elton Hudson, and Hakaan Joensson. “Single-Cell Screening of Photosynthetic Growth and Lactate Production by Cyanobacteria.” <i>Biotechnology for Biofuels</i>. BioMed Central, 2015. <a href=\"https://doi.org/10.1186/s13068-015-0380-2\">https://doi.org/10.1186/s13068-015-0380-2</a>.","apa":"Hammar, P., Angermayr, A., Sjostrom, S., Van Der Meer, J., Hellingwerf, K., Hudson, E., &#38; Joensson, H. (2015). Single-cell screening of photosynthetic growth and lactate production by cyanobacteria. <i>Biotechnology for Biofuels</i>. BioMed Central. <a href=\"https://doi.org/10.1186/s13068-015-0380-2\">https://doi.org/10.1186/s13068-015-0380-2</a>","ieee":"P. Hammar <i>et al.</i>, “Single-cell screening of photosynthetic growth and lactate production by cyanobacteria,” <i>Biotechnology for Biofuels</i>, vol. 8, no. 1. BioMed Central, 2015."},"intvolume":"         8","publist_id":"5537","publication":"Biotechnology for Biofuels","scopus_import":1,"year":"2015","day":"25","doi":"10.1186/s13068-015-0380-2","oa":1,"language":[{"iso":"eng"}],"volume":8,"month":"11","has_accepted_license":"1","issue":"1","file":[{"date_updated":"2020-07-14T12:45:07Z","date_created":"2018-12-12T10:10:11Z","content_type":"application/pdf","file_name":"IST-2016-467-v1+1_s13068-015-0380-2.pdf","relation":"main_file","file_size":2914089,"access_level":"open_access","creator":"system","checksum":"172b0b6f4eb2e5c22b7cec1d57dc0107","file_id":"4796"}],"article_number":"193","author":[{"full_name":"Hammar, Petter","first_name":"Petter","last_name":"Hammar"},{"orcid":"0000-0001-8619-2223","last_name":"Angermayr","first_name":"Andreas","full_name":"Angermayr, Andreas","id":"4677C796-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Sjostrom, Staffan","first_name":"Staffan","last_name":"Sjostrom"},{"last_name":"Van Der Meer","first_name":"Josefin","full_name":"Van Der Meer, Josefin"},{"last_name":"Hellingwerf","first_name":"Klaas","full_name":"Hellingwerf, Klaas"},{"full_name":"Hudson, Elton","first_name":"Elton","last_name":"Hudson"},{"full_name":"Joensson, Hakaan","first_name":"Hakaan","last_name":"Joensson"}],"quality_controlled":"1","oa_version":"Published Version","pubrep_id":"467","status":"public","date_created":"2018-12-11T11:53:05Z","_id":"1623","type":"journal_article"}]