Griesinger, Christian

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[["dc.bibliographiccitation.firstpage","4172"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","4175"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Sanchez-Pedregal, Victor M."],["dc.contributor.author","Reese, Marcel"],["dc.contributor.author","Meiler, Jens"],["dc.contributor.author","Blommers, Marcel J. J."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Carlomagno, Teresa"],["dc.date.accessioned","2017-09-07T11:43:03Z"],["dc.date.available","2017-09-07T11:43:03Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1002/anie.200500503"],["dc.identifier.gro","3143908"],["dc.identifier.isi","000230354100005"],["dc.identifier.pmid","15929149"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1474"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1433-7851"],["dc.title","The INPHARMA method: Protein-mediated interligand NOEs for pharmacophore mapping"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","680"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","691"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Rodriguez-Castaneda, Fernando"],["dc.contributor.author","Maestre-Martinez, Mitcheell"],["dc.contributor.author","Coudevylle, Nicolas"],["dc.contributor.author","Dimova, Kalina"],["dc.contributor.author","Junge, Harald J."],["dc.contributor.author","Lipstein, Noa"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Carlomagno, Teresa"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Ca²⁺ signalling in neurons through calmodulin (CaM) has a prominent function in regulating synaptic vesicle trafficking, transport, and fusion. Importantly, Ca²⁺–CaM binds a conserved region in the priming proteins Munc13‐1 and ubMunc13‐2 and thus regulates synaptic neurotransmitter release in neurons in response to residual Ca2+ signals. We solved the structure of Ca²⁺₄–CaM in complex with the CaM‐binding domain of Munc13‐1, which features a novel 1‐5‐8‐26 CaM‐binding motif with two separated mobile structural modules, each involving a CaM domain. Photoaffinity labelling data reveal the same modular architecture in the complex with the ubMunc13‐2 isoform. The N‐module can be dissociated with EGTA to form the half‐loaded Munc13/Ca²⁺₂–CaM complex. The Ca²⁺ regulation of these Munc13 isoforms can therefore be explained by the modular nature of the Munc13/Ca²⁺–CaM interactions, where the C‐module provides a high‐affinity interaction activated at nanomolar [Ca²⁺]i, whereas the N‐module acts as a sensor at micromolar [Ca²⁺]i. This Ca²⁺/CaM‐binding mode of Munc13 likely constitutes a key molecular correlate of the characteristic Ca²⁺‐dependent modulation of short‐term synaptic plasticity."],["dc.identifier.doi","10.1038/emboj.2009.373"],["dc.identifier.gro","3142967"],["dc.identifier.isi","000274233400015"],["dc.identifier.pmid","20010694"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/429"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max-Planck Society; Fonds der Chemischen Industrie"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca²⁺ and possible function in short-term synaptic plasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","319"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","329"],["dc.bibliographiccitation.volume","336"],["dc.contributor.author","Razeto, A."],["dc.contributor.author","Ramakrishnan, V"],["dc.contributor.author","Litterst, C. M."],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Carlomagno, Teresa"],["dc.contributor.author","Lakomek, Nils-Alexander"],["dc.contributor.author","Heimburg, T."],["dc.contributor.author","Lodrini, Marco"],["dc.contributor.author","Pfitzner, Edith"],["dc.contributor.author","Becker, S."],["dc.date.accessioned","2017-09-07T11:44:01Z"],["dc.date.available","2017-09-07T11:44:01Z"],["dc.date.issued","2004"],["dc.description.abstract","Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. The CREB-binding protein (p300/CBP) and the nuclear coactivator I (NCoA-1), a member of the p160/steroid receptor coactivator family, bind independently to specific regions of the STAT6 transactivation domain and act as coactivators. The interaction between STAT6 and NCoA-1 is mediated by an LXXLL motif in the transactivation domain of STAT6. To define the mechanism of coactivator recognition, we determined the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6 LXXLL motif. The amphipathic, alpha-helical STAT6 LXXLL motif binds mostly through specific hydrophobic interactions to NCoA-1. A single amino acid of the NCoA-1 PAS-B domain establishes hydrophilic interactions with the STAT6 peptide. STAT6 interacts only with the PAS-B domain of NCoA-1 but not with the homologous regions of NCoA-2 and NCoA-3. The residues involved in binding the STAT6 peptide are strongly conserved between the different NCoA family members. Therefore surface complementarity between the hydrophobic faces of the STAT6 fragment and of the NCoA-1 PAS-B domain almost exclusively defines the binding specificity between the two proteins. (C) 2003 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2003.12.057"],["dc.identifier.gro","3144010"],["dc.identifier.isi","000188783000003"],["dc.identifier.pmid","14757047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1587"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1089-8638"],["dc.relation.issn","0022-2836"],["dc.title","Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","18"],["dc.bibliographiccitation.issue","1-3"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","550"],["dc.contributor.author","Kipping, Marc"],["dc.contributor.author","Lilie, Hauke"],["dc.contributor.author","Lindenstrauss, Ute"],["dc.contributor.author","Andreesen, Jan R."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Carlomagno, Teresa"],["dc.contributor.author","Brüser, Thomas"],["dc.date.accessioned","2017-09-07T11:44:15Z"],["dc.date.available","2017-09-07T11:44:15Z"],["dc.date.issued","2003"],["dc.description.abstract","Translocation of folded proteins across biological membranes can be mediated by the so-called 'twin-arginine translocation' (Tat) system. To be translocated, Tat substrates require N-terminal signal sequences which usually contain the eponymous twin-arginine motif. Here we report the first structural analysis of a twin-arginine signal sequence, the signal sequence of the high potential iron-sulfur protein from Allochromatium vinosum. Nuclear magnetic resonance (NMR) analyses of amide proton resonances did not indicate a signal sequence structure. Accordingly, data from H/D exchange matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry showed that the amide protons of the signal sequence exchange rapidly, indicating the absence of secondary structure in the signal sequence up to L29. We conclude that the conserved twin-arginine motif does not form a structure by itself or as a result of intramolecular interactions. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies."],["dc.identifier.doi","10.1016/S0014-5793(03)00804-4"],["dc.identifier.gro","3144067"],["dc.identifier.isi","000185055000004"],["dc.identifier.pmid","12935879"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1650"],["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","0014-5793"],["dc.title","Structural studies on a twin-arginine signal sequence"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","161"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","170"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Carlomagno, T."],["dc.contributor.author","Maurer, M."],["dc.contributor.author","Sattler, M."],["dc.contributor.author","Schwendinger, M. G."],["dc.contributor.author","Glaser, S. J."],["dc.contributor.author","Griesinger, C."],["dc.date.accessioned","2018-04-23T11:47:40Z"],["dc.date.available","2018-04-23T11:47:40Z"],["dc.date.issued","1996"],["dc.description.abstract","A new homonuclear Hartmann-Hahn-type mixing scheme is introduced that effects coherence transfer between resonances in two separated frequency bands. The mixing scheme relies on the irradiation of two-band selective shaped pulses that are expanded in an MLEV-16 supercycle. Similar to heteronuclear Hartmann-Hahn experiments, a planar effective coupling tensor is created. This novel mixing scheme is applied to Cα,C′ transfer and to the transfer between Cβ and aromatic carbon spins."],["dc.identifier.doi","10.1007/bf00211162"],["dc.identifier.gro","3142251"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13376"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0925-2738"],["dc.title","PLUSH TACSY: Homonuclear planar TACSY with two-band selective shaped pulses applied to Cα,C′ transfer and Cβ,Caromatic correlations"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7954"],["dc.bibliographiccitation.issue","47"],["dc.bibliographiccitation.journal","Angewandte Chemie"],["dc.bibliographiccitation.lastpage","7956"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Lakomek, Nils-Alexander"],["dc.contributor.author","Farès, Christophe"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Carlomagno, Teresa"],["dc.contributor.author","Meiler, Jens"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:52:24Z"],["dc.date.available","2017-09-07T11:52:24Z"],["dc.date.issued","2005"],["dc.description.abstract","Ordnungsparameter, wie sie aus dipolaren Restkopplungen in NH‐Gruppen abgeleitet wurden, belegen eine Beweglichkeit des Proteinrückgrats auf einer gegenüber der Korrelationszeit τC langsamen Zeitskala. Wenig bewegliche Amide (blau und grün) z. B. im Ubiquitin sind wasserstoffverbrückt und gehören zu Aminosäureresten, deren Seitenketten zum hydrophoben Kern zeigen, wohingegen bewegliche Amide (gelb, orange, rot) solvensexponierte Seitenketten haben und weniger H‐Bindungen eingehen."],["dc.identifier.doi","10.1002/ange.200502573"],["dc.identifier.gro","3144924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2602"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0044-8249"],["dc.title","Side-Chain Orientation and Hydrogen-Bonding Imprint Supra-τc Motion on the Protein Backbone of Ubiquitin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1945"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","1948"],["dc.bibliographiccitation.volume","121"],["dc.contributor.author","Carlomagno, Teresa"],["dc.contributor.author","Felli, I. C."],["dc.contributor.author","Czech, M."],["dc.contributor.author","Fischer, R"],["dc.contributor.author","Sprinzl, M."],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:47:33Z"],["dc.date.available","2017-09-07T11:47:33Z"],["dc.date.issued","1999"],["dc.identifier.doi","10.1021/ja9835887"],["dc.identifier.gro","3144484"],["dc.identifier.isi","000079143700023"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2113"],["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","0002-7863"],["dc.title","Transferred cross-correlated relaxation: Application to the determination of sugar pucker in an aminoacylated tRNA-mimetic weakly bound to EF-Tu"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]