[{"doi":"10.1016/j.xpro.2023.102795","acknowledged_ssus":[{"_id":"Bio"},{"_id":"PreCl"}],"language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1016/j.xpro.2023.102795","open_access":"1"}],"oa":1,"external_id":{"pmid":["38165800"]},"quality_controlled":"1","project":[{"grant_number":"24812","_id":"2625A13E-B435-11E9-9278-68D0E5697425","name":"Molecular Mechanisms of Radial Neuronal Migration"}],"month":"01","publication_identifier":{"eissn":["2666-1667"]},"author":[{"first_name":"Andi H","last_name":"Hansen","id":"38853E16-F248-11E8-B48F-1D18A9856A87","full_name":"Hansen, Andi H"},{"full_name":"Hippenmeyer, Simon","id":"37B36620-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-2279-1061","first_name":"Simon","last_name":"Hippenmeyer"}],"related_material":{"link":[{"url":"http://github.com/hippenmeyerlab","relation":"software"}]},"date_created":"2024-01-14T23:00:56Z","date_updated":"2024-01-17T10:32:31Z","volume":5,"acknowledgement":"We thank Florian Pauler for discussion and his expert technical support. This research was supported by the Scientific Service Units (SSU) at IST Austria through resources provided by the Imaging and Optics Facility (IOF) and Preclinical Facility (PCF). A.H.H. was a recipient of a DOC Fellowship (24812) of the Austrian Academy of Sciences.","year":"2024","pmid":1,"publication_status":"epub_ahead","publisher":"Elsevier","department":[{"_id":"SiHi"}],"article_number":"102795","date_published":"2024-01-01T00:00:00Z","publication":"STAR Protocols","citation":{"ama":"Hansen AH, Hippenmeyer S. Time-lapse imaging of cortical projection neuron migration in mice using mosaic analysis with double markers. STAR Protocols. 2024;5(1). doi:10.1016/j.xpro.2023.102795","ieee":"A. H. Hansen and S. Hippenmeyer, “Time-lapse imaging of cortical projection neuron migration in mice using mosaic analysis with double markers,” STAR Protocols, vol. 5, no. 1. Elsevier, 2024.","apa":"Hansen, A. H., & Hippenmeyer, S. (2024). Time-lapse imaging of cortical projection neuron migration in mice using mosaic analysis with double markers. STAR Protocols. Elsevier. https://doi.org/10.1016/j.xpro.2023.102795","ista":"Hansen AH, Hippenmeyer S. 2024. Time-lapse imaging of cortical projection neuron migration in mice using mosaic analysis with double markers. STAR Protocols. 5(1), 102795.","short":"A.H. Hansen, S. Hippenmeyer, STAR Protocols 5 (2024).","mla":"Hansen, Andi H., and Simon Hippenmeyer. “Time-Lapse Imaging of Cortical Projection Neuron Migration in Mice Using Mosaic Analysis with Double Markers.” STAR Protocols, vol. 5, no. 1, 102795, Elsevier, 2024, doi:10.1016/j.xpro.2023.102795.","chicago":"Hansen, Andi H, and Simon Hippenmeyer. “Time-Lapse Imaging of Cortical Projection Neuron Migration in Mice Using Mosaic Analysis with Double Markers.” STAR Protocols. Elsevier, 2024. https://doi.org/10.1016/j.xpro.2023.102795."},"article_type":"review","day":"01","article_processing_charge":"Yes","scopus_import":"1","oa_version":"Published Version","_id":"14794","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Time-lapse imaging of cortical projection neuron migration in mice using mosaic analysis with double markers","status":"public","intvolume":" 5","abstract":[{"lang":"eng","text":"Mosaic analysis with double markers (MADM) technology enables the sparse labeling of genetically defined neurons. We present a protocol for time-lapse imaging of cortical projection neuron migration in mice using MADM. We describe steps for the isolation, culturing, and 4D imaging of neuronal dynamics in MADM-labeled brain tissue. While this protocol is compatible with other single-cell labeling methods, the MADM approach provides a genetic platform for the functional assessment of cell-autonomous candidate gene function and the relative contribution of non-cell-autonomous effects.\r\n\r\nFor complete details on the use and execution of this protocol, please refer to Hansen et al. (2022),1 Contreras et al. (2021),2 and Amberg and Hippenmeyer (2021).3"}],"issue":"1","type":"journal_article"},{"month":"01","publication_identifier":{"eissn":["1097-4172"],"issn":["0092-8674"]},"quality_controlled":"1","project":[{"_id":"261099A6-B435-11E9-9278-68D0E5697425","grant_number":"742985","name":"Tracing Evolution of Auxin Transport and Polarity in Plants","call_identifier":"H2020"},{"_id":"262EF96E-B435-11E9-9278-68D0E5697425","grant_number":"P29988","name":"RNA-directed DNA methylation in plant development","call_identifier":"FWF"}],"oa":1,"tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)"},"external_id":{"pmid":["38128538"]},"language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2023.11.021","file_date_updated":"2024-01-22T13:41:41Z","ec_funded":1,"publication_status":"published","department":[{"_id":"JiFr"}],"publisher":"Elsevier","acknowledgement":"We are grateful to Asuka Shitaku and Eri Koide for generating and sharing the Marchantia PRAF-mCitrine line and Peng-Cheng Wang for sharing the Arabidopsis raf mutant. We are grateful to our team members for discussions and helpful advice. This work was supported by funding from the Netherlands Organization for Scientific Research (NWO): VICI grant 865.14.001 and ENW-KLEIN OCENW.KLEIN.027 grants to D.W.; VENI grant VI.VENI.212.003 to A.K.; the European Research Council AdG DIRNDL (contract number 833867) to D.W.; CoG CATCH to J.S.; StG CELLONGATE (contract 803048) to M.F.; and AdG ETAP (contract 742985) to J.F.; MEXT KAKENHI grant number JP19H05675 to T.K.; JSPS KAKENHI grant number JP20H03275 to R.N.; Takeda Science Foundation to R.N.; and the Austrian Science Fund (FWF, P29988) to J.F.","year":"2024","pmid":1,"date_updated":"2024-01-22T13:43:40Z","date_created":"2024-01-17T12:45:40Z","volume":187,"author":[{"first_name":"Andre","last_name":"Kuhn","full_name":"Kuhn, Andre"},{"first_name":"Mark","last_name":"Roosjen","full_name":"Roosjen, Mark"},{"first_name":"Sumanth","last_name":"Mutte","full_name":"Mutte, Sumanth"},{"first_name":"Shiv Mani","last_name":"Dubey","full_name":"Dubey, Shiv Mani"},{"last_name":"Carrillo Carrasco","first_name":"Vanessa Polet","full_name":"Carrillo Carrasco, Vanessa Polet"},{"first_name":"Sjef","last_name":"Boeren","full_name":"Boeren, Sjef"},{"id":"2DB5D88C-D7B3-11E9-B8FD-7907E6697425","last_name":"Monzer","first_name":"Aline","full_name":"Monzer, Aline"},{"full_name":"Koehorst, Jasper","first_name":"Jasper","last_name":"Koehorst"},{"first_name":"Takayuki","last_name":"Kohchi","full_name":"Kohchi, Takayuki"},{"full_name":"Nishihama, Ryuichi","first_name":"Ryuichi","last_name":"Nishihama"},{"full_name":"Fendrych, Matyas","orcid":"0000-0002-9767-8699","id":"43905548-F248-11E8-B48F-1D18A9856A87","last_name":"Fendrych","first_name":"Matyas"},{"full_name":"Sprakel, Joris","last_name":"Sprakel","first_name":"Joris"},{"id":"4159519E-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8302-7596","first_name":"Jiří","last_name":"Friml","full_name":"Friml, Jiří"},{"full_name":"Weijers, Dolf","last_name":"Weijers","first_name":"Dolf"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"scopus_import":"1","day":"04","article_processing_charge":"Yes (in subscription journal)","has_accepted_license":"1","article_type":"original","page":"130-148.e17","publication":"Cell","citation":{"chicago":"Kuhn, Andre, Mark Roosjen, Sumanth Mutte, Shiv Mani Dubey, Vanessa Polet Carrillo Carrasco, Sjef Boeren, Aline Monzer, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid Auxin Response.” Cell. Elsevier, 2024. https://doi.org/10.1016/j.cell.2023.11.021.","short":"A. Kuhn, M. Roosjen, S. Mutte, S.M. Dubey, V.P. Carrillo Carrasco, S. Boeren, A. Monzer, J. Koehorst, T. Kohchi, R. Nishihama, M. Fendrych, J. Sprakel, J. Friml, D. Weijers, Cell 187 (2024) 130–148.e17.","mla":"Kuhn, Andre, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid Auxin Response.” Cell, vol. 187, no. 1, Elsevier, 2024, p. 130–148.e17, doi:10.1016/j.cell.2023.11.021.","ieee":"A. Kuhn et al., “RAF-like protein kinases mediate a deeply conserved, rapid auxin response,” Cell, vol. 187, no. 1. Elsevier, p. 130–148.e17, 2024.","apa":"Kuhn, A., Roosjen, M., Mutte, S., Dubey, S. M., Carrillo Carrasco, V. P., Boeren, S., … Weijers, D. (2024). RAF-like protein kinases mediate a deeply conserved, rapid auxin response. Cell. Elsevier. https://doi.org/10.1016/j.cell.2023.11.021","ista":"Kuhn A, Roosjen M, Mutte S, Dubey SM, Carrillo Carrasco VP, Boeren S, Monzer A, Koehorst J, Kohchi T, Nishihama R, Fendrych M, Sprakel J, Friml J, Weijers D. 2024. RAF-like protein kinases mediate a deeply conserved, rapid auxin response. Cell. 187(1), 130–148.e17.","ama":"Kuhn A, Roosjen M, Mutte S, et al. RAF-like protein kinases mediate a deeply conserved, rapid auxin response. Cell. 2024;187(1):130-148.e17. doi:10.1016/j.cell.2023.11.021"},"date_published":"2024-01-04T00:00:00Z","type":"journal_article","abstract":[{"lang":"eng","text":"The plant-signaling molecule auxin triggers fast and slow cellular responses across land plants and algae. The nuclear auxin pathway mediates gene expression and controls growth and development in land plants, but this pathway is absent from algal sister groups. Several components of rapid responses have been identified in Arabidopsis, but it is unknown if these are part of a conserved mechanism. We recently identified a fast, proteome-wide phosphorylation response to auxin. Here, we show that this response occurs across 5 land plant and algal species and converges on a core group of shared targets. We found conserved rapid physiological responses to auxin in the same species and identified rapidly accelerated fibrosarcoma (RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation across species. Genetic analysis connects this kinase to both auxin-triggered protein phosphorylation and rapid cellular response, thus identifying an ancient mechanism for fast auxin responses in the green lineage."}],"issue":"1","status":"public","ddc":["580"],"title":"RAF-like protein kinases mediate a deeply conserved, rapid auxin response","intvolume":" 187","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"14826","file":[{"relation":"main_file","file_id":"14874","date_created":"2024-01-22T13:41:41Z","date_updated":"2024-01-22T13:41:41Z","checksum":"06fd236a9ee0b46ccb05f44695bfc34b","success":1,"file_name":"2024_Cell_Kuhn.pdf","access_level":"open_access","file_size":13194060,"content_type":"application/pdf","creator":"dernst"}],"oa_version":"Published Version"},{"publication_status":"published","department":[{"_id":"MaIb"}],"publisher":"American Chemical Society","year":"2024","acknowledgement":"This work was supported by the Technology Innovation Program (20011622, Development of Battery System Applied High-Efficiency Heat Control Polymer and Part Component) funded by the Ministry of Trade, Industry & Energy (MOTIE, Korea). Author acknowledge to Prof. Tsunehiro Takeuchi from Toyota Technological Institute, Nagoya, Japan for the support of computational resources.","date_updated":"2024-01-22T13:47:39Z","date_created":"2024-01-17T12:48:35Z","volume":7,"author":[{"full_name":"Kiran, Gundegowda Kalligowdanadoddi","first_name":"Gundegowda Kalligowdanadoddi","last_name":"Kiran"},{"full_name":"Singh, Saurabh","orcid":"0000-0003-2209-5269","id":"12d625da-9cb3-11ed-9667-af09d37d3f0a","last_name":"Singh","first_name":"Saurabh"},{"full_name":"Mahato, Neelima","first_name":"Neelima","last_name":"Mahato"},{"full_name":"Sreekanth, Thupakula Venkata Madhukar","last_name":"Sreekanth","first_name":"Thupakula Venkata Madhukar"},{"first_name":"Gowra Raghupathy","last_name":"Dillip","full_name":"Dillip, Gowra Raghupathy"},{"full_name":"Yoo, Kisoo","last_name":"Yoo","first_name":"Kisoo"},{"last_name":"Kim","first_name":"Jonghoon","full_name":"Kim, Jonghoon"}],"month":"01","publication_identifier":{"issn":["2574-0962"]},"isi":1,"quality_controlled":"1","external_id":{"isi":["001138342900001"]},"language":[{"iso":"eng"}],"doi":"10.1021/acsaem.3c02519","type":"journal_article","abstract":[{"lang":"eng","text":"Production of hydrogen at large scale requires development of non-noble, inexpensive, and high-performing catalysts for constructing water-splitting devices. Herein, we report the synthesis of Zn-doped NiO heterostructure (ZnNiO) catalysts at room temperature via a coprecipitation method followed by drying (at 80 °C, 6 h) and calcination at an elevated temperature of 400 °C for 5 h under three distinct conditions, namely, air, N2, and vacuum. The vacuum-synthesized catalyst demonstrates a low overpotential of 88 mV at −10 mA cm–2 and a small Tafel slope of 73 mV dec–1 suggesting relatively higher charge transfer kinetics for hydrogen evolution reactions (HER) compared with the specimens synthesized under N2 or O2 atmosphere. It also demonstrates an oxygen evolution (OER) overpotential of 260 mV at 10 mA cm–2 with a low Tafel slope of 63 mV dec–1. In a full-cell water-splitting device, the vacuum-synthesized ZnNiO heterostructure demonstrates a cell voltage of 1.94 V at 50 mA cm–2 and shows remarkable stability over 24 h at a high current density of 100 mA cm–2. It is also demonstrated in this study that Zn-doping, surface, and interface engineering in transition-metal oxides play a crucial role in efficient electrocatalytic water splitting. Also, the results obtained from density functional theory (DFT + U = 0–8 eV), where U is the on-site Coulomb repulsion parameter also known as Hubbard U, based electronic structure calculations confirm that Zn doping constructively modifies the electronic structure, in both the valence band and the conduction band, and found to be suitable in tailoring the carrier’s effective masses of electrons and holes. The decrease in electron’s effective masses together with large differences between the effective masses of electrons and holes is noticed, which is found to be mainly responsible for achieving the best water-splitting performance from a 9% Zn-doped NiO sample prepared under vacuum."}],"issue":"1","title":"Interface engineering modulation combined with electronic structure modification of Zn-doped NiO heterostructure for efficient water-splitting activity","status":"public","intvolume":" 7","_id":"14828","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"None","keyword":["Electrical and Electronic Engineering","Materials Chemistry","Electrochemistry","Energy Engineering and Power Technology","Chemical Engineering (miscellaneous)"],"scopus_import":"1","day":"08","article_processing_charge":"No","article_type":"original","page":"214-229","publication":"ACS Applied Energy Materials","citation":{"short":"G.K. Kiran, S. Singh, N. Mahato, T.V.M. Sreekanth, G.R. Dillip, K. Yoo, J. Kim, ACS Applied Energy Materials 7 (2024) 214–229.","mla":"Kiran, Gundegowda Kalligowdanadoddi, et al. “Interface Engineering Modulation Combined with Electronic Structure Modification of Zn-Doped NiO Heterostructure for Efficient Water-Splitting Activity.” ACS Applied Energy Materials, vol. 7, no. 1, American Chemical Society, 2024, pp. 214–29, doi:10.1021/acsaem.3c02519.","chicago":"Kiran, Gundegowda Kalligowdanadoddi, Saurabh Singh, Neelima Mahato, Thupakula Venkata Madhukar Sreekanth, Gowra Raghupathy Dillip, Kisoo Yoo, and Jonghoon Kim. “Interface Engineering Modulation Combined with Electronic Structure Modification of Zn-Doped NiO Heterostructure for Efficient Water-Splitting Activity.” ACS Applied Energy Materials. American Chemical Society, 2024. https://doi.org/10.1021/acsaem.3c02519.","ama":"Kiran GK, Singh S, Mahato N, et al. Interface engineering modulation combined with electronic structure modification of Zn-doped NiO heterostructure for efficient water-splitting activity. ACS Applied Energy Materials. 2024;7(1):214-229. doi:10.1021/acsaem.3c02519","ieee":"G. K. Kiran et al., “Interface engineering modulation combined with electronic structure modification of Zn-doped NiO heterostructure for efficient water-splitting activity,” ACS Applied Energy Materials, vol. 7, no. 1. American Chemical Society, pp. 214–229, 2024.","apa":"Kiran, G. K., Singh, S., Mahato, N., Sreekanth, T. V. M., Dillip, G. R., Yoo, K., & Kim, J. (2024). Interface engineering modulation combined with electronic structure modification of Zn-doped NiO heterostructure for efficient water-splitting activity. ACS Applied Energy Materials. American Chemical Society. https://doi.org/10.1021/acsaem.3c02519","ista":"Kiran GK, Singh S, Mahato N, Sreekanth TVM, Dillip GR, Yoo K, Kim J. 2024. Interface engineering modulation combined with electronic structure modification of Zn-doped NiO heterostructure for efficient water-splitting activity. ACS Applied Energy Materials. 7(1), 214–229."},"date_published":"2024-01-08T00:00:00Z"},{"date_published":"2024-01-12T00:00:00Z","citation":{"ista":"Radler P, Loose M. 2024. A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. European Journal of Cell Biology. 103(1), 151380.","apa":"Radler, P., & Loose, M. (2024). A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. European Journal of Cell Biology. Elsevier. https://doi.org/10.1016/j.ejcb.2023.151380","ieee":"P. Radler and M. Loose, “A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches,” European Journal of Cell Biology, vol. 103, no. 1. Elsevier, 2024.","ama":"Radler P, Loose M. A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. European Journal of Cell Biology. 2024;103(1). doi:10.1016/j.ejcb.2023.151380","chicago":"Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.” European Journal of Cell Biology. Elsevier, 2024. https://doi.org/10.1016/j.ejcb.2023.151380.","mla":"Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.” European Journal of Cell Biology, vol. 103, no. 1, 151380, Elsevier, 2024, doi:10.1016/j.ejcb.2023.151380.","short":"P. Radler, M. Loose, European Journal of Cell Biology 103 (2024)."},"publication":"European Journal of Cell Biology","article_type":"review","article_processing_charge":"Yes","has_accepted_license":"1","day":"12","scopus_import":"1","keyword":["Cell Biology","General Medicine","Histology","Pathology and Forensic Medicine"],"oa_version":"Published Version","_id":"14834","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":" 103","ddc":["570"],"status":"public","title":"A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches","issue":"1","abstract":[{"text":"Bacteria divide by binary fission. The protein machine responsible for this process is the divisome, a transient assembly of more than 30 proteins in and on the surface of the cytoplasmic membrane. Together, they constrict the cell envelope and remodel the peptidoglycan layer to eventually split the cell into two. For Escherichia coli, most molecular players involved in this process have probably been identified, but obtaining the quantitative information needed for a mechanistic understanding can often not be achieved from experiments in vivo alone. Since the discovery of the Z-ring more than 30 years ago, in vitro reconstitution experiments have been crucial to shed light on molecular processes normally hidden in the complex environment of the living cell. In this review, we summarize how rebuilding the divisome from purified components – or at least parts of it - have been instrumental to obtain the detailed mechanistic understanding of the bacterial cell division machinery that we have today.","lang":"eng"}],"type":"journal_article","doi":"10.1016/j.ejcb.2023.151380","language":[{"iso":"eng"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.ejcb.2023.151380"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa":1,"external_id":{"pmid":["38218128"]},"project":[{"grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","name":"Understanding bacterial cell division by in vitro\r\nreconstitution"}],"quality_controlled":"1","publication_identifier":{"issn":["0171-9335"]},"month":"01","author":[{"full_name":"Radler, Philipp","last_name":"Radler","first_name":"Philipp","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","first_name":"Martin","last_name":"Loose"}],"volume":103,"date_created":"2024-01-18T08:16:43Z","date_updated":"2024-01-23T08:37:13Z","pmid":1,"year":"2024","acknowledgement":"We acknowledge members of the Loose laboratory at ISTA for helpful discussions—in particular M. Kojic for his insightful comments. This work was supported by the Austrian Science Fund (FWF P34607) to M.L.","department":[{"_id":"MaLo"}],"publisher":"Elsevier","publication_status":"epub_ahead","article_number":"151380"},{"intvolume":" 121","status":"public","title":"A structurally precise mechanism links an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"14841","oa_version":"None","type":"journal_article","issue":"3","abstract":[{"lang":"eng","text":"De novo heterozygous variants in KCNC2 encoding the voltage-gated potassium (K+) channel subunit Kv3.2 are a recently described cause of developmental and epileptic encephalopathy (DEE). A de novo variant in KCNC2 c.374G > A (p.Cys125Tyr) was identified via exome sequencing in a patient with DEE. Relative to wild-type Kv3.2, Kv3.2-p.Cys125Tyr induces K+ currents exhibiting a large hyperpolarizing shift in the voltage dependence of activation, accelerated activation, and delayed deactivation consistent with a relative stabilization of the open conformation, along with increased current density. Leveraging the cryogenic electron microscopy (cryo-EM) structure of Kv3.1, molecular dynamic simulations suggest that a strong π-π stacking interaction between the variant Tyr125 and Tyr156 in the α-6 helix of the T1 domain promotes a relative stabilization of the open conformation of the channel, which underlies the observed gain of function. A multicompartment computational model of a Kv3-expressing parvalbumin-positive cerebral cortex fast-spiking γ-aminobutyric acidergic (GABAergic) interneuron (PV-IN) demonstrates how the Kv3.2-Cys125Tyr variant impairs neuronal excitability and dysregulates inhibition in cerebral cortex circuits to explain the resulting epilepsy."}],"article_type":"original","citation":{"ama":"Clatot J, Currin C, Liang Q, et al. A structurally precise mechanism links an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction. Proceedings of the National Academy of Sciences of the United States of America. 2024;121(3). doi:10.1073/pnas.2307776121","ista":"Clatot J, Currin C, Liang Q, Pipatpolkai T, Massey SL, Helbig I, Delemotte L, Vogels TP, Covarrubias M, Goldberg EM. 2024. A structurally precise mechanism links an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction. Proceedings of the National Academy of Sciences of the United States of America. 121(3), e2307776121.","apa":"Clatot, J., Currin, C., Liang, Q., Pipatpolkai, T., Massey, S. L., Helbig, I., … Goldberg, E. M. (2024). A structurally precise mechanism links an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction. Proceedings of the National Academy of Sciences of the United States of America. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2307776121","ieee":"J. Clatot et al., “A structurally precise mechanism links an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction,” Proceedings of the National Academy of Sciences of the United States of America, vol. 121, no. 3. Proceedings of the National Academy of Sciences, 2024.","mla":"Clatot, Jerome, et al. “A Structurally Precise Mechanism Links an Epilepsy-Associated KCNC2 Potassium Channel Mutation to Interneuron Dysfunction.” Proceedings of the National Academy of Sciences of the United States of America, vol. 121, no. 3, e2307776121, Proceedings of the National Academy of Sciences, 2024, doi:10.1073/pnas.2307776121.","short":"J. Clatot, C. Currin, Q. Liang, T. Pipatpolkai, S.L. Massey, I. Helbig, L. Delemotte, T.P. Vogels, M. Covarrubias, E.M. Goldberg, Proceedings of the National Academy of Sciences of the United States of America 121 (2024).","chicago":"Clatot, Jerome, Christopher Currin, Qiansheng Liang, Tanadet Pipatpolkai, Shavonne L. Massey, Ingo Helbig, Lucie Delemotte, Tim P Vogels, Manuel Covarrubias, and Ethan M. Goldberg. “A Structurally Precise Mechanism Links an Epilepsy-Associated KCNC2 Potassium Channel Mutation to Interneuron Dysfunction.” Proceedings of the National Academy of Sciences of the United States of America. Proceedings of the National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2307776121."},"publication":"Proceedings of the National Academy of Sciences of the United States of America","date_published":"2024-01-16T00:00:00Z","scopus_import":"1","article_processing_charge":"No","day":"16","publisher":"Proceedings of the National Academy of Sciences","department":[{"_id":"TiVo"}],"publication_status":"published","pmid":1,"acknowledgement":"This work was supported by an ERC Consolidator Grant (SYNAPSEEK) to T.P.V., the NOMIS Foundation through the NOMIS Fellowships program at IST Austria to C.B.C., a Jefferson Synaptic Biology Center Pilot Project Grant to M.C., NIH NINDS U54 NS108874 (PI, Alfred L. George), and NIH NINDS R01 NS122887 to E.M.G. The computations were enabled by resources provided by the Swedish National Infrastructure for Computing (SNIC) at the PDC Center for High-Performance Computing, KTH Royal Institute of Technology, partially funded by the Swedish Research Council through grant agreement no. 2018-05973. We thank Akshay Sridhar for the fruitful discussion of the project.","year":"2024","volume":121,"date_created":"2024-01-21T23:00:56Z","date_updated":"2024-01-23T10:20:40Z","related_material":{"link":[{"relation":"software","url":"https://github.com/ChrisCurrin/pv-kcnc2 "}]},"author":[{"full_name":"Clatot, Jerome","first_name":"Jerome","last_name":"Clatot"},{"first_name":"Christopher","last_name":"Currin","id":"e8321fc5-3091-11eb-8a53-83f309a11ac9","orcid":"0000-0002-4809-5059","full_name":"Currin, Christopher"},{"last_name":"Liang","first_name":"Qiansheng","full_name":"Liang, Qiansheng"},{"full_name":"Pipatpolkai, Tanadet","last_name":"Pipatpolkai","first_name":"Tanadet"},{"full_name":"Massey, Shavonne L.","first_name":"Shavonne L.","last_name":"Massey"},{"full_name":"Helbig, Ingo","first_name":"Ingo","last_name":"Helbig"},{"full_name":"Delemotte, Lucie","first_name":"Lucie","last_name":"Delemotte"},{"last_name":"Vogels","first_name":"Tim P","orcid":"0000-0003-3295-6181","id":"CB6FF8D2-008F-11EA-8E08-2637E6697425","full_name":"Vogels, Tim P"},{"first_name":"Manuel","last_name":"Covarrubias","full_name":"Covarrubias, Manuel"},{"last_name":"Goldberg","first_name":"Ethan M.","full_name":"Goldberg, Ethan M."}],"article_number":"e2307776121","ec_funded":1,"project":[{"grant_number":"819603","_id":"0aacfa84-070f-11eb-9043-d7eb2c709234","call_identifier":"H2020","name":"Learning the shape of synaptic plasticity rules for neuronal architectures and function through machine learning."}],"quality_controlled":"1","external_id":{"pmid":["38194456"]},"language":[{"iso":"eng"}],"doi":"10.1073/pnas.2307776121","publication_identifier":{"eissn":["1091-6490"]},"month":"01"}]