Schneider, Robert

[["dc.bibliographiccitation.firstpage","1540"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","1549"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Gattin, Zrinka"],["dc.contributor.author","Demers, Jean-Philippe"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Maier, Elke"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Benz, Roland"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:48:25Z"],["dc.date.available","2017-09-07T11:48:25Z"],["dc.date.issued","2012"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is the major protein in the outer mitochondrial membrane, where it mediates transport of ATP and ADP. Changes in its permeability, induced by voltage or apoptosis-related proteins, have been implicated in apoptotic pathways. The three-dimensional structure of VDAC has recently been determined as a 19-stranded beta-barrel with an in-lying N-terminal helix. However, its gating mechanism is still unclear. Using solid-state NMR spectroscopy, molecular dynamics simulations, and electrophysiology, we show that deletion of the rigid N-terminal helix sharply increases overall motion in VDAC's beta-barrel, resulting in elliptic, semicollapsed barrel shapes. These states quantitatively reproduce conductance and selectivity of the closed VDAC conformation. Mutation of the N-terminal helix leads to a phenotype intermediate to the open and closed states. These data suggest that the N-terminal helix controls entry into elliptic beta-barrel states which underlie VDAC closure. Our results also indicate that beta-barrel channels are intrinsically flexible."],["dc.identifier.doi","10.1016/j.str.2012.06.015"],["dc.identifier.gro","3142466"],["dc.identifier.isi","000308682700013"],["dc.identifier.pmid","22841291"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8596"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.eissn","1878-4186"],["dc.relation.issn","0969-2126"],["dc.title","beta-Barrel Mobility Underlies Closure of the Voltage-Dependent Anion Channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","747"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","754"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Velisetty, Phanindra"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Seeliger, Daniel"],["dc.contributor.author","Wacker, Sören J."],["dc.contributor.author","Karimi-Nejad, Yasmin"],["dc.contributor.author","Vriend, Gert"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Pongs, Olaf"],["dc.contributor.author","Baldus, Marc"],["dc.contributor.author","de Groot, Bert L."],["dc.date.accessioned","2021-03-05T08:58:11Z"],["dc.date.available","2021-03-05T08:58:11Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1016/j.str.2008.01.018"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80037"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0969-2126"],["dc.title","The Molecular Mechanism of Toxin-Induced Conformational Changes in a Potassium Channel: Relation to C-Type Inactivation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1882"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","1885"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Etzkorn, Manuel"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Daebel, Venita"],["dc.contributor.author","Eisfeld, Joerg"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:46:10Z"],["dc.date.available","2017-09-07T11:46:10Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/anie.200906241"],["dc.identifier.gro","3142985"],["dc.identifier.isi","000275388300034"],["dc.identifier.pmid","20140924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/449"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","The Native Conformation of the Human VDAC1 N Terminus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","7"],["dc.bibliographiccitation.journal","Epigenetics & Chromatin"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Talbert, Paul B."],["dc.contributor.author","Ahmad, Kami"],["dc.contributor.author","Almouzni, Genevieve"],["dc.contributor.author","Ausio, Juan"],["dc.contributor.author","Berger, Frederic"],["dc.contributor.author","Bhalla, Prem L."],["dc.contributor.author","Bonner, William M."],["dc.contributor.author","Cande, W. Zacheus"],["dc.contributor.author","Chadwick, Brian P."],["dc.contributor.author","Chan, Simon W. L."],["dc.contributor.author","Cross, George A. M."],["dc.contributor.author","Cui, Liwang"],["dc.contributor.author","Dimitrov, Stefan I."],["dc.contributor.author","Doenecke, Detlef"],["dc.contributor.author","Eirin-Lopez, Jose M."],["dc.contributor.author","Gorovsky, Martin A."],["dc.contributor.author","Hake, Sandra B."],["dc.contributor.author","Hamkalo, Barbara A."],["dc.contributor.author","Holec, Sarah"],["dc.contributor.author","Jacobsen, Steven E."],["dc.contributor.author","Kamieniarz, Kinga"],["dc.contributor.author","Khochbin, Saadi"],["dc.contributor.author","Ladurner, Andreas G."],["dc.contributor.author","Landsman, David"],["dc.contributor.author","Latham, John A."],["dc.contributor.author","Loppin, Benjamin"],["dc.contributor.author","Malik, Harmit S."],["dc.contributor.author","Marzluff, William F."],["dc.contributor.author","Pehrson, John R."],["dc.contributor.author","Postberg, Jan"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Singh, Mohan B."],["dc.contributor.author","Smith, M. Mitchell"],["dc.contributor.author","Thompson, Eric"],["dc.contributor.author","Torres-Padilla, Maria-Elena"],["dc.contributor.author","Tremethick, David John"],["dc.contributor.author","Turner, Bryan M."],["dc.contributor.author","Waterborg, Jakob Harm"],["dc.contributor.author","Wollmann, Heike"],["dc.contributor.author","Yelagandula, Ramesh"],["dc.contributor.author","Zhu, Bing"],["dc.contributor.author","Henikoff, Steven"],["dc.date.accessioned","2018-11-07T09:10:11Z"],["dc.date.available","2018-11-07T09:10:11Z"],["dc.date.issued","2012"],["dc.description.abstract","Histone variants are non-allelic protein isoforms that play key roles in diversifying chromatin structure. The known number of such variants has greatly increased in recent years, but the lack of naming conventions for them has led to a variety of naming styles, multiple synonyms and misleading homographs that obscure variant relationships and complicate database searches. We propose here a unified nomenclature for variants of all five classes of histones that uses consistent but flexible naming conventions to produce names that are informative and readily searchable. The nomenclature builds on historical usage and incorporates phylogenetic relationships, which are strong predictors of structure and function. A key feature is the consistent use of punctuation to represent phylogenetic divergence, making explicit the relationships among variant subtypes that have previously been implicit or unclear. We recommend that by default new histone variants be named with organism-specific paralog-number suffixes that lack phylogenetic implication, while letter suffixes be reserved for structurally distinct clades of variants. For clarity and searchability, we encourage the use of descriptors that are separate from the phylogeny-based variant name to indicate developmental and other properties of variants that may be independent of structure."],["dc.identifier.doi","10.1186/1756-8935-5-7"],["dc.identifier.isi","000305622000001"],["dc.identifier.pmid","22650316"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26434"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1756-8935"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","A unified phylogeny-based nomenclature for histone variants"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","311"],["dc.bibliographiccitation.issue","3-4"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","320"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Gattin, Zrinka"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Laukat, Yvonne"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Maier, Elke"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Benz, Roland"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:44:27Z"],["dc.date.available","2017-09-07T11:44:27Z"],["dc.date.issued","2015"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles."],["dc.identifier.doi","10.1007/s10858-014-9876-5"],["dc.identifier.gro","3141930"],["dc.identifier.isi","000352711900012"],["dc.identifier.pmid","25399320"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2657"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1573-5001"],["dc.relation.issn","0925-2738"],["dc.title","Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]