Lang, Thorsten

[["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","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"]]