Briones, Rodolfo

[["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","22546"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","22551"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Villinger, Saskia"],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:45:10Z"],["dc.date.available","2017-09-07T11:45:10Z"],["dc.date.issued","2010"],["dc.description.abstract","The voltage-dependent anion channel (VDAC), located in the outer mitochondrial membrane, acts as a gatekeeper for the entry and exit of mitochondrial metabolites. Here we reveal functional dynamics of isoform one of VDAC (VDAC1) by a combination of solution NMR spectroscopy, Gaussian network model analysis, and molecular dynamics simulation. Micro-to millisecond dynamics are significantly increased for the N-terminal six beta-strands of VDAC1 in micellar solution, in agreement with increased B-factors observed in the same region in the bicellar crystal structure of VDAC1. Molecular dynamics simulations reveal that a charge on the membrane-facing glutamic acid 73 (E73) accounts for the elevation of N-terminal protein dynamics as well as a thinning of the nearby membrane. Mutation or chemical modification of E73 strongly reduces the micro-to millisecond dynamics in solution. Because E73 is necessary for hexokinase-I-induced VDAC channel closure and inhibition of apoptosis, our results imply that micro- to millisecond dynamics in the N-terminal part of the barrel are essential for VDAC interaction and gating."],["dc.identifier.doi","10.1073/pnas.1012310108"],["dc.identifier.gro","3142815"],["dc.identifier.isi","000285684200039"],["dc.identifier.pmid","21148773"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/261"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Functional dynamics in 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"]]

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[["dc.bibliographiccitation.firstpage","149a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Machtens, Jan-Philipp"],["dc.contributor.author","Lansche, Christine"],["dc.contributor.author","Leinenweber, Ariane"],["dc.contributor.author","Kilian, Petra"],["dc.contributor.author","Begemann, Birgit"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Ewers, David"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Fahlke, Christoph"],["dc.date.accessioned","2021-03-05T08:57:57Z"],["dc.date.available","2021-03-05T08:57:57Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.bpj.2013.11.858"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79947"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0006-3495"],["dc.title","Anion Permeation through Excitatory Amino Acid Transporters"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]