Schwiegk, Claudia

[["dc.bibliographiccitation.firstpage","751"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS"],["dc.bibliographiccitation.lastpage","756"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Himmel, Sebastian"],["dc.contributor.author","Grosse, Christian"],["dc.contributor.author","Wolff, Sebastian"],["dc.contributor.author","Schwiegk, C."],["dc.contributor.author","Becker, Stefan"],["dc.date.accessioned","2018-11-07T09:08:37Z"],["dc.date.available","2018-11-07T09:08:37Z"],["dc.date.issued","2012"],["dc.description.abstract","GlcT is a transcriptional antiterminator protein that is involved in regulation of glucose metabolism in Bacillus subtilis. Antiterminator proteins bind specific RNA sequences, thus preventing the formation of overlapping terminator stem-loops. The structure of a fragment (residues 3-170) comprising the RNA-binding domain (RBD) and the first regulatory domain (PRDI) of GlcT was solved at 2.0 angstrom resolution with one molecule in the asymmetric unit. The two domains are connected by a helical linker. Their interface is mostly constituted by hydrophobic interactions."],["dc.description.sponsorship","Max Planck Society"],["dc.identifier.doi","10.1107/S1744309112020635"],["dc.identifier.isi","000305967100004"],["dc.identifier.pmid","22750856"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26076"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1744-3091"],["dc.title","Structure of the RBD-PRDI fragment of the antiterminator protein GlcT"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","ra66"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","434"],["dc.bibliographiccitation.journal","Science Signaling"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kühn, Julius"],["dc.contributor.author","Wong, Leo E."],["dc.contributor.author","Pirkuliyeva, Sona"],["dc.contributor.author","Schulz, Kathrin"],["dc.contributor.author","Schwiegk, Claudia"],["dc.contributor.author","Fünfgeld, Kevser Gencalp"],["dc.contributor.author","Keppler, Selina"],["dc.contributor.author","Batista, Facundo D."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Habeck, Michael"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Wienands, Jürgen"],["dc.date.accessioned","2017-09-07T11:44:50Z"],["dc.date.available","2017-09-07T11:44:50Z"],["dc.date.issued","2016"],["dc.description.abstract","The adaptor molecule Cbl-interacting protein of 85 kD (CIN85) regulates signaling from a number of cell surface receptors, such as growth factor receptors and antigen receptors on lymphocytes. Because of its multidomain structure, CIN85 is thought to act as a classical adaptor protein that connects functionally distinct components of a given signaling pathway through diverse protein domains. However, we found that in B lymphocytes, CIN85 functions to oligomerize SLP-65, which is the central effector protein of the B cell receptor (BCR). Therefore, CIN85 trimerizes through a carboxyl-terminal, coiled-coil domain. The multiple Src homology 3 (SH3) domains of trimeric CIN85 molecules associated with multiple SLP- 65 molecules, which recruited further CIN85 trimers, thereby perpetuating the oligomerization process. Formation of this oligomeric signaling complex in resting B cells rendered the cells poised for the efficient initiation of intracellular signaling upon BCR stimulation. Our data suggest that the functionality of signaling cascades does not rely solely on the qualitative linkage of their various components but requires a critical number of effectors to become concentrated in signaling complexes."],["dc.identifier.doi","10.1126/scisignal.aad6275"],["dc.identifier.gro","3141661"],["dc.identifier.isi","000378944100004"],["dc.identifier.pmid","27353366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6564"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 860, TRR 130]; Max Planck Society"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1937-9145"],["dc.relation.issn","1945-0877"],["dc.title","The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","207"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","210"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Smith, Colin A."],["dc.contributor.author","Ban, David"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Schwiegk, Claudia"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2017-09-07T11:44:42Z"],["dc.date.available","2017-09-07T11:44:42Z"],["dc.date.issued","2015"],["dc.description.abstract","Motions play a vital role in the functions of many proteins. Discrete conformational transitions to excited states, happening on timescales of hundreds of microseconds, have been extensively characterized. On the other hand, the dynamics of the ground state are widely unexplored. Newly developed high-power relaxation dispersion experiments allow the detection of motions up to a one-digit microsecond timescale. These experiments showed that side chains in the hydrophobic core as well as at protein-protein interaction surfaces of both ubiquitin and the third immunoglobulin binding domain of proteinG move on the microsecond timescale. Both proteins exhibit plasticity to this microsecond motion through redistribution of the populations of their side-chain rotamers, which interconvert on the picosecond to nanosecond timescale, making it likely that this population shuffling process is a general mechanism."],["dc.identifier.doi","10.1002/anie.201408890"],["dc.identifier.gro","3141974"],["dc.identifier.isi","000347065100028"],["dc.identifier.pmid","25377083"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3146"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society; EU (ERC) [233227]; Alexander von Humboldt Foundation"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","Population Shuffling of Protein Conformations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]