Lang, Thorsten

[["dc.bibliographiccitation.firstpage","394"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","404"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Halemani, Nagaraj D."],["dc.contributor.author","Bethani, Ioanna"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lang, Thorsten"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","SNAREs are clustered membrane proteins essential for intracellular fusion steps. During fusion, three to four SNAREs with a Q(a)-, Q(b)-, Q(c)- and R-SNARE-motif form a complex. The core complex represents a Q(a)Q(b)Q(c)R-SNARE-motif bundle, most certainly assembling in steps. However, to date it is unknown which intermediate SNARE complex observed in vitro also exists in vivo. Here we have applied comparative fluorescence recovery after photobleaching (FRAP)-studies as a novel approach for studying in intact cells a SNARE interaction involved in synaptic vesicle fusion [catalyzed by syntaxin 1A (Q(a)), SNAP25 (Q(b)/Q(c)) and synaptobrevin 2 (R)]. We find that the Q(b)-SNARE-motif of SNAP25 interacts reversibly with clustered syntaxin. The interaction requires most of the alpha helical Q(b)-SNARE-motif and depends on its position within the molecule. We conclude that a zippered Q(a)Q(b)-SNARE complex represents a short-lived SNARE intermediate in intact cells, most likely providing an initial molecular platform toward membrane fusion."],["dc.identifier.doi","10.1111/j.1600-0854.2009.01020.x"],["dc.identifier.gro","3142960"],["dc.identifier.isi","000274454500008"],["dc.identifier.pmid","20002656"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/421"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [LA1272/2-3]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","1398-9219"],["dc.title","Structure and Dynamics of a Two-Helix SNARE Complex in Live Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","116"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Physiology"],["dc.bibliographiccitation.lastpage","124"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Fluorescence microscopy is powerful for analyzing the composition and dynamics of cellular elements, but studying precise molecule patterns is precluded due to diffraction limited resolution. This barrier has been lifted now through several superresolution microscopy techniques. They revealed that proteins assemble in defined groups (clusters). A new challenge thus appears for the biologist: to find out whether clusters are molecular machines, stabilizers of defined protein conformations, or simply protein reservoirs."],["dc.identifier.doi","10.1152/physiol.00044.2009"],["dc.identifier.gro","3142947"],["dc.identifier.isi","000278117100006"],["dc.identifier.pmid","20430955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/407"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1548-9213"],["dc.title","Membrane Protein Clusters at Nanoscale Resolution: More Than Pretty Pictures"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","353"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","359"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Aquino, Daniel"],["dc.contributor.author","Schönle, Andreas"],["dc.contributor.author","Geisler, Claudia"],["dc.contributor.author","von Middendorff, Claas"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Okamura, Yosuke"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Egner, Alexander"],["dc.date.accessioned","2017-09-07T11:44:19Z"],["dc.date.available","2017-09-07T11:44:19Z"],["dc.date.issued","2011"],["dc.description.abstract","We demonstrate three-dimensional (3D) super-resolution imaging of stochastically switched fluorophores distributed across whole cells. By evaluating the higher moments of the diffraction spot provided by a 4Pi detection scheme, single markers can be simultaneously localized with < 10 nm precision in three dimensions in a layer of 650 nm thickness at an arbitrarily selected depth in the sample. By splitting the fluorescence light into orthogonal polarization states, our 4Pi setup also facilitates the 3D nanoscopy of multiple fluorophores. Offering a combination of multicolor recording, nanoscale resolution and extended axial depth, our method substantially advances the noninvasive 3D imaging of cells and of other transparent materials."],["dc.identifier.doi","10.1038/NMETH.1583"],["dc.identifier.gro","3142756"],["dc.identifier.isi","000288940300024"],["dc.identifier.pmid","21399636"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/195"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 755]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.title","Two-color nanoscopy of three-dimensional volumes by 4Pi detection of stochastically switched fluorophores"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","4509"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Saka, Sinem K."],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2017-09-07T11:46:11Z"],["dc.date.available","2017-09-07T11:46:11Z"],["dc.date.issued","2014"],["dc.description.abstract","Most proteins have uneven distributions in the plasma membrane. Broadly speaking, this may be caused by mechanisms specific to each protein, or may be a consequence of a general pattern that affects the distribution of all membrane proteins. The latter hypothesis has been difficult to test in the past. Here, we introduce several approaches based on click chemistry, through which we study the distribution of membrane proteins in living cells, as well as in membrane sheets. We found that the plasma membrane proteins form multi-protein assemblies that are long lived (minutes), and in which protein diffusion is restricted. The formation of the assemblies is dependent on cholesterol. They are separated and anchored by the actin cytoskeleton. Specific proteins are preferentially located in different regions of the assemblies, from their cores to their edges. We conclude that the assemblies constitute a basic mesoscale feature of the membrane, which affects the patterning of most membrane proteins, and possibly also their activity."],["dc.identifier.doi","10.1038/ncomms5509"],["dc.identifier.gro","3142092"],["dc.identifier.isi","000340625100012"],["dc.identifier.pmid","25060237"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10970"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4456"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","Multi-protein assemblies underlie the mesoscale organization of the plasma membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1072"],["dc.bibliographiccitation.issue","5841"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1076"],["dc.bibliographiccitation.volume","317"],["dc.contributor.author","Sieber, Jochen J."],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Kutzner, Carsten"],["dc.contributor.author","Gerding-Reimers, Claas"],["dc.contributor.author","Harke, Benjamin"],["dc.contributor.author","Donnert, Gerald"],["dc.contributor.author","Rammner, Burkhard"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Lang, Thorsten"],["dc.date.accessioned","2017-09-07T11:49:26Z"],["dc.date.available","2017-09-07T11:49:26Z"],["dc.date.issued","2007"],["dc.description.abstract","Most plasmalemmal proteins organize in submicrometer-sized clusters whose architecture and dynamics are still enigmatic. With syntaxin 1 as an example, we applied a combination of far-field optical nanoscopy, biochemistry, fluorescence recovery after photobleaching (FRAP) analysis, and simulations to show that clustering can be explained by self-organization based on simple physical principles. On average, the syntaxin clusters exhibit a diameter of 50 to 60 nanometers and contain 75 densely crowded syntaxins that dynamically exchange with freely diffusing molecules. Self-association depends on weak homophilic protein-protein interactions. Simulations suggest that clustering immobilizes and conformationally constrains the molecules. Moreover, a balance between self-association and crowding-induced steric repulsions is sufficient to explain both the size and dynamics of syntaxin clusters and likely of many oligomerizing membrane proteins that form supramolecular structures."],["dc.identifier.doi","10.1126/science.1141727"],["dc.identifier.gro","3143450"],["dc.identifier.isi","000248946700042"],["dc.identifier.pmid","17717182"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/965"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0036-8075"],["dc.title","Anatomy and dynamics of a supramolecular membrane protein cluster"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2701"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","2706"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Brandhorst, Dorothea"],["dc.contributor.author","Zwilling, Daniel"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lippert, Undine"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:53:17Z"],["dc.date.available","2017-09-07T11:53:17Z"],["dc.date.issued","2006"],["dc.description.abstract","Membrane fusion in the secretory pathway is mediated by soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins. Different fusion steps are thought to be effected by independent sets of SNAREs, but it is unclear whether specificity is determined by an intrinsic specificity of SNARE pairing or by upstream factors. Using a newly developed microscopy-based assay, we have investigated the SNARE specificity of homotypic early endosomal fusion.. We show that early endosomes contain multiple sets of SNAREs, including, in addition to the putative early endosomal SNAREs, those involved in exocytosis and in fusion of late endosomes. We demonstrate that fusion is largely mediated by a complex formed by syntaxin 13, syntaxin 6, vti1a, and VAMP4, whereas the exocytic and late endosomal SNAREs play little or no role in the reaction. In contrast, proteoliposomes reconstituted with early endosomal SNAREs promiscuously fuse with liposomes containing exocytotic or late endosomal SNAREs. We conclude that the specificity of SNARE pairing does not suffice to determine the specificity of organelle fusion."],["dc.identifier.doi","10.1073/pnas.0511138103"],["dc.identifier.gro","3143735"],["dc.identifier.isi","000235554900041"],["dc.identifier.pmid","16469845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1282"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5675"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","5685"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Nagy, Gábor"],["dc.contributor.author","Milošević, Ira"],["dc.contributor.author","Fasshauer, Dirk"],["dc.contributor.author","Müller, E. Matthias"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Wilson, Michael C."],["dc.contributor.author","Sørensen, Jakob B."],["dc.date.accessioned","2021-03-05T08:58:51Z"],["dc.date.available","2021-03-05T08:58:51Z"],["dc.date.issued","2005"],["dc.description.abstract","The essential membrane fusion apparatus in mammalian cells, the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, consists of four α-helices formed by three proteins: SNAP-25, syntaxin 1, and synaptobrevin 2. SNAP-25 contributes two helices to the complex and is targeted to the plasma membrane by palmitoylation of four cysteines in the linker region. It is alternatively spliced into two forms, SNAP-25a and SNAP-25b, differing by nine amino acids substitutions. When expressed in chromaffin cells from SNAP-25 null mice, the isoforms support different levels of secretion. Here, we investigated the basis of that different secretory phenotype. We found that two nonconservative substitutions in the N-terminal SNARE domain and not the different localization of one palmitoylated cysteine cause the functional difference between the isoforms. Biochemical and molecular dynamic simulation experiments revealed that the two substitutions do not regulate secretion by affecting the property of SNARE complex itself, but rather make the SNAP-25b-containing SNARE complex more available for the interaction with accessory factor(s)."],["dc.description.abstract","The essential membrane fusion apparatus in mammalian cells, the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, consists of four α-helices formed by three proteins: SNAP-25, syntaxin 1, and synaptobrevin 2. SNAP-25 contributes two helices to the complex and is targeted to the plasma membrane by palmitoylation of four cysteines in the linker region. It is alternatively spliced into two forms, SNAP-25a and SNAP-25b, differing by nine amino acids substitutions. When expressed in chromaffin cells from SNAP-25 null mice, the isoforms support different levels of secretion. Here, we investigated the basis of that different secretory phenotype. We found that two nonconservative substitutions in the N-terminal SNARE domain and not the different localization of one palmitoylated cysteine cause the functional difference between the isoforms. Biochemical and molecular dynamic simulation experiments revealed that the two substitutions do not regulate secretion by affecting the property of SNARE complex itself, but rather make the SNAP-25b-containing SNARE complex more available for the interaction with accessory factor(s)."],["dc.identifier.doi","10.1091/mbc.e05-07-0595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80276"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Alternative Splicing of SNAP-25 Regulates Secretion through Nonconservative Substitutions in the SNARE Domain"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","502"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Pharmacology"],["dc.bibliographiccitation.lastpage","513"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Renner, Ute"],["dc.contributor.author","Glebov, Konstantin"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Papusheva, Ekaterina"],["dc.contributor.author","Balakrishnan, Saju"],["dc.contributor.author","Keller, Bernhard U."],["dc.contributor.author","Richter, Diethelm W."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.date.accessioned","2018-11-07T10:59:14Z"],["dc.date.available","2018-11-07T10:59:14Z"],["dc.date.issued","2007"],["dc.description.abstract","In the present study, we have used wild- type and palmitoylationdeficient mouse 5- hydroxytryptamine (1A) receptor ( 5- HT1A) receptors fused to the yellow fluorescent protein- and the cyan fluorescent protein ( CFP)- tagged alpha (i3) subunit of heterotrimeric G- protein to study spatiotemporal distribution of the 5- HT1Amediated signaling in living cells. We also addressed the question on the molecular mechanisms by which receptor palmitoylation may regulate communication between receptors and G i- proteins. Our data demonstrate that activation of the 5- HT1A receptor caused a partial release of G alpha(i) protein into the cytoplasm and that this translocation is accompanied by a significant increase of the intracellular Ca2+ concentration."],["dc.identifier.doi","10.1124/mol.107.037085"],["dc.identifier.isi","000248976400003"],["dc.identifier.pmid","17540717"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50651"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","0026-895X"],["dc.title","Localization of the mouse 5-Hydroxytryptamine(1A) receptor in lipid Microdomains depends on its palmitoylation and is involved in receptor-mediated signaling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2843"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2851"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Sieber, Jochen J."],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Heintzmann, Rainer"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Lang, Thorsten"],["dc.date.accessioned","2017-09-07T11:53:10Z"],["dc.date.available","2017-09-07T11:53:10Z"],["dc.date.issued","2006"],["dc.description.abstract","In the plasma membrane, syntaxin 1 and syntaxin 4 clusters de. ne sites at which secretory granules and caveolae fuse, respectively. It is widely believed that lipid phases are mandatory for cluster formation, as cluster integrity depends on cholesterol. Here we report that the native lipid environment is not sufficient for correct syntaxin 1 clustering and that additional cytoplasmic protein-protein interactions, primarily involving the SNARE motif, are required. Apparently no specific cofactors are needed because i\\), clusters form equally well in nonneuronal cells, and ii\\), as revealed by nanoscale subdiffraction resolution provided by STED microscopy, the number of clusters directly depends on the syntaxin 1 concentration. For syntaxin 4 clustering the N-terminal domain and the linker region are also dispensable. Moreover, clustering is specific because in both cluster types syntaxins mutually exclude one another at endogenous levels. We suggest that the SNARE motifs of syntaxin 1 and 4 mediate specific syntaxin clustering by homooligomerization, thereby spatially separating sites for different biological activities. Thus, syntaxin clustering represents a mechanism of membrane patterning that is based on protein-protein interactions."],["dc.identifier.doi","10.1529/biophysj.105.079574"],["dc.identifier.gro","3143708"],["dc.identifier.isi","000236226900019"],["dc.identifier.pmid","16443657"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1252"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.title","The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Membrane Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Borroni, V."],["dc.contributor.author","Baier, C. J."],["dc.contributor.author","Lang, T."],["dc.contributor.author","Bonini, I."],["dc.contributor.author","White, M. M."],["dc.contributor.author","Garbus, I."],["dc.contributor.author","Barrantes, F. J."],["dc.date.accessioned","2017-09-07T11:49:53Z"],["dc.date.available","2017-09-07T11:49:53Z"],["dc.date.issued","2007"],["dc.description.abstract","Novel effects of cholesterol (Chol) on nicotinic acetylcholine receptor (AChR) cell-surface stability, internalization and function are reported. AChRs are shown to occur in the form of submicron-sized (240-280 nm) domains that remain stable at the cell-surface membrane of CHO-K1/A5 cells over a period of hours. Acute (30 min, 37 degrees C) exposure to methyl-beta-cycloclextrin (CDx), commonly used as a diagnostic tool of endocytic mechanisms, is shown here to enhance AChR internalization kinetics in the receptor-expressing clonal cell line. This treatment drastically reduced (similar to 50%) the number of receptor domains by accelerating the rate of enclocytosis (t(1/2) decreased from 1.5-0.5 h). In addition, Chol depletion produced ion channel gain-of-function of the remaining cell-surface AChR, whereas Chol enrichment had the opposite effect. Fluorescence measurements under conditions of direct excitation of the probe Laurdan and of Forster-type resonance energy transfer (FRET) using the intrinsic protein fluorescence as donor both indicated an increase in membrane fluidity in the bulk membrane and in the immediate environment of the AChR protein upon Chol depletion. Homeostatic control of Chol content at the plasmalemma may thus modulate cell-surface organization and stability of receptor domains, and fine tune receptor channel function to temporarily compensate for acute AChR loss from the cell surface."],["dc.identifier.doi","10.1080/09687860600903387"],["dc.identifier.gro","3143563"],["dc.identifier.isi","000244534700001"],["dc.identifier.pmid","17453409"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1091"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0968-7688"],["dc.relation.issn","0968-7688"],["dc.title","Cholesterol depletion activates rapid internalization of submicron-sized acetylcholine receptor domains at the cell membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]