Becker, Stefan T.

[["dc.bibliographiccitation.firstpage","41"],["dc.bibliographiccitation.lastpage","59"],["dc.contributor.author","Kneuper, H."],["dc.contributor.author","Scheu, Stefan"],["dc.contributor.author","Etzkorn, Manuel"],["dc.contributor.author","Sevvana, M."],["dc.contributor.author","Dünnwald, Pia"],["dc.contributor.author","Becker, S."],["dc.contributor.author","Baldus, Marc"],["dc.contributor.author","Unden, Gottfried"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.editor","Spiro, Stephen"],["dc.contributor.editor","Dixon, Ray"],["dc.date.accessioned","2017-09-07T11:44:57Z"],["dc.date.available","2017-09-07T11:44:57Z"],["dc.date.issued","2010"],["dc.identifier.gro","3145436"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3142"],["dc.notes.intern","lifescience"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","chake"],["dc.publisher","Caister Academic Press"],["dc.publisher.place","Norfolk"],["dc.relation.isbn","1-904455-69-7"],["dc.relation.ispartof","Sensory Mechanisms in Bacteria: Molecular Aspects of Signal Recognition"],["dc.title","Sensing ligands by periplasmic sensing histidine kinases with sensory PAS domains"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3256"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","3268"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Karpinar, Damla Pinar"],["dc.contributor.author","Balija, Madhu Babu Gajula"],["dc.contributor.author","Kügler, Sebastian"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Wender, Nora"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Taschenberger, Grit"],["dc.contributor.author","Falkenburger, Bjoern H."],["dc.contributor.author","Heise, Henrike"],["dc.contributor.author","Kumar, Ashutosh"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Fichtner, Lars"],["dc.contributor.author","Voigt, Aaron"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Herzig, Alf"],["dc.contributor.author","Baldus, Marc"],["dc.contributor.author","Jaeckle, Herbert"],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Schulz, Joerg B."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:46:48Z"],["dc.date.available","2017-09-07T11:46:48Z"],["dc.date.issued","2009"],["dc.description.abstract","The relation of alpha-synuclein (alpha S) aggregation to Parkinson's disease (PD) has long been recognized, but the mechanism of toxicity, the pathogenic species and its molecular properties are yet to be identified. To obtain insight into the function different aggregated alpha S species have in neurotoxicity in vivo, we generated alpha S variants by a structure-based rational design. Biophysical analysis revealed that the alpha S mutants have a reduced fibrillization propensity, but form increased amounts of soluble oligomers. To assess their biological response in vivo, we studied the effects of the biophysically defined pre-fibrillar alpha S mutants after expression in tissue culture cells, in mammalian neurons and in PD model organisms, such as Caenorhabditis elegans and Drosophila melanogaster. The results show a striking correlation between alpha S aggregates with impaired beta-structure, neuronal toxicity and behavioural defects, and they establish a tight link between the biophysical properties of multimeric aS species and their in vivo function. The EMBO Journal (2009) 28, 3256-3268. doi:10.1038/emboj.2009.257; Published online 10 September 2009"],["dc.identifier.doi","10.1038/emboj.2009.257"],["dc.identifier.gro","3143038"],["dc.identifier.isi","000271008200017"],["dc.identifier.pmid","19745811"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/508"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1031"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","1039"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Etzkorn, Manuel"],["dc.contributor.author","Kneuper, Holger"],["dc.contributor.author","Dünnwald, Pia"],["dc.contributor.author","Vijayan, Vinesh"],["dc.contributor.author","Krämer, Jens"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Unden, Gottfried"],["dc.contributor.author","Baldus, Marc"],["dc.date.accessioned","2017-09-07T11:48:11Z"],["dc.date.available","2017-09-07T11:48:11Z"],["dc.date.issued","2008"],["dc.description.abstract","The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to protein regions close to the transmembrane segment. Data from isolated and multidomain constructs favor a disordered N-terminal helix in the cytoplasmic domain. Mutations of residues in this region strongly influence function, suggesting that protein flexibility is related to signal transduction toward the kinase domain and regulation of kinase activity."],["dc.identifier.doi","10.1038/nsmb.1493"],["dc.identifier.gro","3143231"],["dc.identifier.isi","000259777000008"],["dc.identifier.pmid","18820688"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/722"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [BA 1700/6-2, UN 49/6, UN49/8]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9985"],["dc.title","Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS"],["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","4369"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","4376"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Seidel, Karsten"],["dc.contributor.author","Andronesi, Ovidiu C."],["dc.contributor.author","Krebs, Joachim"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Young, Howard S."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Baldus, Marc"],["dc.date.accessioned","2017-09-07T11:48:45Z"],["dc.date.available","2017-09-07T11:48:45Z"],["dc.date.issued","2008"],["dc.description.abstract","Phospholamban (PLN) regulates cardiac contractility by modulation of sarco(endo)plasmic reticulum calcium ATPase (SERCA) activity. While PLN and SERCAla, an isoform from skeletal muscle, have been structurally characterized in great detail, direct information about the conformation of PLN in complex with SERCA has been limited. We used solid-state NMR (ssNMR) spectroscopy to deduce structural properties of both the A(36)F(41)A(46) mutant (AFA-PLN) and wild-type PLN (WT-PLN) when bound to SERCA I a after reconstitution in a functional lipid bilayer environment. Chemical-shift assignments in all domains of AFA-PLN provide direct evidence for the presence of two terminal a helices connected by a linker region of reduced structural order that differs from previous findings on free PLN. ssNMR experiments on WT-PLN show no significant difference in binding compared to AFA-PLN and do not support the coexistence of a significantly populated dynamic state of PLN after formation of the PLN/ SERCA complex. A combination of our spectroscopic data with biophysical and biochemical data using flexible protein-protein docking simulations provides a structural basis for understanding the interaction between PLN and SERCAla."],["dc.identifier.doi","10.1021/bi7024194"],["dc.identifier.gro","3143315"],["dc.identifier.isi","000254818100003"],["dc.identifier.pmid","18355039"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/816"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","Structural characterization of Ca2+-ATPase-bound phospholarnban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) Spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]