Giller, Karin

[["dc.bibliographiccitation.firstpage","3115"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America : PNAS"],["dc.bibliographiccitation.lastpage","3120"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Salvi, Michele"],["dc.contributor.author","Schomburg, Benjamin"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Graf, Sabrina"],["dc.contributor.author","Unden, Gottfried"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2018-01-17T11:33:34Z"],["dc.date.available","2018-01-17T11:33:34Z"],["dc.date.issued","2017"],["dc.description.abstract","Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of the PAS domain, which is well characterized for the isolated domain, is the signal transmitted to the transmembrane (TM) helices in a CitA construct in liposomes. Putting the extracytoplasmic PAS domain into context of the membrane-embedded CitA construct slows down citrate-binding kinetics by at least a factor of 60, confirming that TM helix motions are linked to the citrate-binding event. Our results are confirmation of a hallmark of the HK signal transduction mechanism with atomic resolution on a full-length construct lacking only the kinase core domain."],["dc.identifier.doi","10.1073/pnas.1620286114"],["dc.identifier.pmid","28265100"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11680"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1091-6490"],["dc.title","Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5857"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Fonseca-Ornelas, Luis"],["dc.contributor.author","Eisbach, Sibylle E."],["dc.contributor.author","Paulat, Maria"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:31:47Z"],["dc.date.available","2018-11-07T09:31:47Z"],["dc.date.issued","2014"],["dc.description.abstract","alpha-synuclein is an abundant presynaptic protein that is important for regulation of synaptic vesicle trafficking, and whose misfolding plays a key role in Parkinson's disease. While alpha-synuclein is disordered in solution, it folds into a helical conformation when bound to synaptic vesicles. Stabilization of helical, folded alpha-synuclein might therefore interfere with alpha-synuclein-induced neurotoxicity. Here we show that several small molecules, which delay aggregation of alpha-synuclein in solution, including the Parkinson's disease drug selegiline, fail to interfere with misfolding of vesicle-bound alpha-synuclein. In contrast, the porphyrin phtalocyanine tetrasulfonate directly binds to vesicle-bound alpha-synuclein, stabilizes its helical conformation and thereby delays pathogenic misfolding and aggregation. Our study suggests that small-molecule-mediated stabilization of helical vesicle-bound alpha-synuclein opens new possibilities to target Parkinson's disease and related synucleinopathies."],["dc.identifier.doi","10.1038/ncomms6857"],["dc.identifier.isi","000347683000001"],["dc.identifier.pmid","25524885"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31609"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.title","Small molecule-mediated stabilization of vesicle-associated helical alpha-synuclein inhibits pathogenic misfolding and aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9546"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","9555"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Kozuch, Jacek"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Millo, Diego"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Hildebrandt, Peter"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:46:55Z"],["dc.date.available","2017-09-07T11:46:55Z"],["dc.date.issued","2014"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is a transmembrane protein that regulates the transfer of metabolites between the cytosol and the mitochondrium. Opening and partial closing of the channel is known to be driven by the transmembrane potential via a mechanism that is not fully understood. In this work, we employed a spectroelectrochemical approach to probe the voltage-induced molecular structure changes of human VDAC1 (hVDAC1) embedded in a tethered bilayer lipid membrane on a nanostructured Au electrode. The model membrane consisted of a mixed self-assembled monolayer of 6-mercaptohexanol and (cholesterylpolyethylenoxy) thiol, followed by the deposition of 1-palmitoyl-2- oleoyl-sn-glycero-3-phosphocholine vesicles including hVDAC1. The stepwise assembly of the model membrane and the incorporation of hVDAC1 were monitored by surface enhanced infrared absorption and electrochemical impedance spectroscopy. Difference spectra allowed for identifying the spectral changes which may be associated with the transition from the open to the \"closed' states by shifting the potential above or below the transmembrane potential determined to be ca. 0.0 V vs. the open circuit potential. These spectral changes were interpreted on the basis of the orientation-and distancedependent IR enhancement and indicate alterations of the inclination angle of the beta-strands as crucial molecular events, reflecting an expansion or contraction of the beta-barrel pore. These protein structural changes that do not confirm nor exclude the reorientation of the alpha-helix are either directly induced by the electric field or a consequence of a potential-dependent repulsion or attraction of the bilayer."],["dc.identifier.doi","10.1039/c4cp00167b"],["dc.identifier.gro","3142210"],["dc.identifier.isi","000335818600039"],["dc.identifier.pmid","24728177"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5754"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.title","Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4913"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","4919"],["dc.bibliographiccitation.volume","136"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Amininasab, Mehriar"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Kumar, Sathish"],["dc.contributor.author","Stuendl, Anne"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Walter, Jochen"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:41:25Z"],["dc.date.available","2018-11-07T09:41:25Z"],["dc.date.issued","2014"],["dc.description.abstract","Pathogenesis of Alzheimer's disease (AD) is associated with aggregation of the amyloid-beta (A beta) peptide into oligomeric and fibrillar assemblies; however, little is known about the molecular basis of aggregation of A beta into distinct assembly states. Here we demonstrate that phosphorylation at serine 26 (S26) impairs A beta fibrillization while stabilizing its monomers and nontoxic soluble assemblies of nonfibrillar morphology. NMR spectroscopy and replica-exchange molecular dynamics indicate that introduction of a phosphate group or phosphomimetic at position 26 diminishes A beta's propensity to form a beta-hairpin, rigidifies the region around the modification site, and interferes with formation of a fibril-specific salt bridge between aspartic acid 23 and lysine 28. The combined data demonstrate that phosphorylation of S26 prevents a distinct conformational rearrangement that is required for progression of A beta aggregation toward fibrils and provide a basis for a possible role of phosphorylation at serine 26 in AD."],["dc.description.sponsorship","DFG [ZW 71/2-2, ZW 71/3-2, WA1477/6-2]"],["dc.identifier.doi","10.1021/ja411707y"],["dc.identifier.isi","000333947900030"],["dc.identifier.pmid","24617810"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33723"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Turn Plasticity Distinguishes Different Modes of Amyloid-beta Aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Chakrabarti, Kalyan S."],["dc.contributor.author","Olsson, Simon"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Overkamp, Kerstin"],["dc.contributor.author","Lee, Ko On"],["dc.contributor.author","Gapsys, Vytautas"],["dc.contributor.author","Ryu, Kyoung-Seok"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Noé, Frank"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2022-09-01T09:50:00Z"],["dc.date.available","2022-09-01T09:50:00Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n Partner recognition in protein binding is critical for all biological functions, and yet, delineating its mechanism is challenging, especially when recognition happens within microseconds. We present a theoretical and experimental framework based on straight-forward nuclear magnetic resonance relaxation dispersion measurements to investigate protein binding mechanisms on sub-millisecond timescales, which are beyond the reach of standard rapid-mixing experiments. This framework predicts that conformational selection prevails on ubiquitin’s paradigmatic interaction with an SH3 (Src-homology 3) domain. By contrast, the SH3 domain recognizes ubiquitin in a two-state binding process. Subsequent molecular dynamics simulations and Markov state modeling reveal that the ubiquitin conformation selected for binding exhibits a characteristically extended C-terminus. Our framework is robust and expandable for implementation in other binding scenarios with the potential to show that conformational selection might be the design principle of the hubs in protein interaction networks."],["dc.identifier.doi","10.1038/s41467-022-31374-5"],["dc.identifier.pii","31374"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113597"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","2041-1723"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A litmus test for classifying recognition mechanisms of transiently binding proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","16555"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Chemistry - A European Journal"],["dc.bibliographiccitation.lastpage","16563"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Jaremko, Lukasz"],["dc.contributor.author","Jaremko, Mariusz"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:48:59Z"],["dc.date.available","2018-11-07T09:48:59Z"],["dc.date.issued","2015"],["dc.description.abstract","The translocator protein (TSPO) is an integral membrane protein that interacts with a wide variety of endogenous ligands, such as cholesterol and porphyrins, and is also the target for several small molecules with substantial in vivo efficacy. When complexed with the TSPO-specific radioligand (R)-PK11195, TSPO folds into a rigid five-helix bundle. However, little is known about the structure and dynamics of TSPO in the absence of high-affinity ligands. By means of NMR spectroscopy, we show that TSPO exchanges between multiple conformations in the absence of (R)-PK11195. Extensive motions on time scales from pico- to microseconds occur all along the primary sequence of the protein, leading to a loss of stable tertiary interactions and local unfolding of the helical structure in the vicinity of the ligand-binding site. The flexible nature of TSPO highlights the importance of conformational plasticity in integral membrane proteins."],["dc.identifier.doi","10.1002/chem.201502314"],["dc.identifier.isi","000365132100035"],["dc.identifier.pmid","26394723"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35421"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1521-3765"],["dc.relation.issn","0947-6539"],["dc.title","Conformational Flexibility in the Transmembrane Protein TSPO"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10367"],["dc.bibliographiccitation.issue","39"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","10371"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Michielssens, Servaas"],["dc.contributor.author","Peters, Jan Henning"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Seeliger, Daniel"],["dc.contributor.author","Sharma, Monika"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Sabo, Thomas Michael"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Groot, Bert L. de"],["dc.date.accessioned","2017-09-07T11:45:30Z"],["dc.date.available","2017-09-07T11:45:30Z"],["dc.date.issued","2014"],["dc.description.abstract","In a conformational selection scenario, manipulating the populations of binding-competent states should be expected to affect protein binding. We demonstrate how in silico designed point mutations within the core of ubiquitin, remote from the binding interface, change the binding specificity by shifting the conformational equilibrium of the ground-state ensemble between open and closed substates that have a similar population in the wild-type protein. Binding affinities determined by NMR titration experiments agree with the predictions, thereby showing that, indeed, a shift in the conformational equilibrium enables us to alter ubiquitin's binding specificity and hence its function. Thus, we present a novel route towards designing specific binding by a conformational shift through exploiting the fact that conformational selection depends on the concentration of binding-competent substates."],["dc.identifier.doi","10.1002/anie.201403102"],["dc.identifier.gro","3142049"],["dc.identifier.isi","000342760700013"],["dc.identifier.pmid","25115701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3978"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","A Designed Conformational Shift To Control Protein Binding Specificity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","184a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","185a"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Smith, Colin A."],["dc.contributor.author","Ban, David"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Groot, Bert L. de"],["dc.date.accessioned","2017-09-07T11:52:26Z"],["dc.date.available","2017-09-07T11:52:26Z"],["dc.date.issued","2015"],["dc.description.abstract","Motion is involved in a large number of protein functions. Relaxation dispersion (RD) NMR experiments sensitively probe microsecond to millisecond motions. We conducted an in-depth RD analysis of the backbone and side chain methyl groups of ubquitin. This survey showed a large number of atoms (>30) with microsecond fluctuations. These atoms are distributed throughout the structure. Strikingly, nearly all show the same exchange rate, which suggests that ubiquitin undergoes collective motion involving both the backbone and side chains. Furthermore, comparison of different methyl nuclei indicates that the nature of the side chain fluctuations is almost entirely due to changes in rotamer populations. Thus, collective microsecond backbone motion is coupled to redistribution of side chain rotamer populations through a mechanism we term “population shuffling”. We present a single collective mode of motion that yields a reaction coordinate corresponding to the relaxation dispersion data. The resulting model indicates that a localized conformational switch distant from the binding interface propagates changes throughout the structure. Analysis of crystal structures confirms this allosteric network and suggests that the microsecond motion modulates binding to particular interaction partners."],["dc.identifier.doi","10.1016/j.bpj.2014.11.1020"],["dc.identifier.gro","3144936"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2615"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0006-3495"],["dc.title","Microsecond Motion Modulates Ubiquitin Binding through an Allosteric Backbone/Side Chain Network"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","14893"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Jaipuria, Garima"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Vasa, Suresh Kumar"],["dc.contributor.author","Jaremko, Lukasz"],["dc.contributor.author","Jaremko, Mariusz"],["dc.contributor.author","Linser, Rasmus"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T10:26:01Z"],["dc.date.available","2018-11-07T10:26:01Z"],["dc.date.issued","2017"],["dc.description.abstract","Cholesterol is an important regulator of membrane protein function. However, the exact mechanisms involved in this process are still not fully understood. Here we study how the tertiary and quaternary structure of the mitochondrial translocator protein TSPO, which binds cholesterol with nanomolar affinity, is affected by this sterol. Residue-specific analysis of TSPO by solid-state NMR spectroscopy reveals a dynamic monomer-dimer equilibrium of TSPO in the membrane. Binding of cholesterol to TSPO's cholesterol-recognition motif leads to structural changes across the protein that shifts the dynamic equilibrium towards the translocator monomer. Consistent with an allosteric mechanism, a mutation within the oligomerization interface perturbs transmembrane regions located up to 35 angstrom away from the interface, reaching TSPO's cholesterol-binding motif. The lower structural stability of the intervening transmembrane regions provides a mechanistic basis for signal transmission. Our study thus reveals an allosteric signal pathway that connects membrane protein tertiary and quaternary structure with cholesterol binding."],["dc.identifier.doi","10.1038/ncomms14893"],["dc.identifier.isi","000397799000001"],["dc.identifier.pmid","28358007"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14416"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42959"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]