Griesinger, Christian

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Frieg, Benedikt"],["dc.contributor.author","Antonschmidt, Leif"],["dc.contributor.author","Dienemann, Christian"],["dc.contributor.author","Geraets, James A."],["dc.contributor.author","Najbauer, Eszter E."],["dc.contributor.author","Matthes, Dirk"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Andreas, Loren B."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Schröder, Gunnar F."],["dc.date.accessioned","2022-12-01T08:30:50Z"],["dc.date.available","2022-12-01T08:30:50Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n α-synuclein misfolding and aggregation into fibrils is a common feature of α-synucleinopathies, such as Parkinson’s disease, in which α-synuclein fibrils are a characteristic hallmark of neuronal inclusions called Lewy bodies. Studies on the composition of Lewy bodies extracted postmortem from brain tissue of Parkinson’s patients revealed that lipids and membranous organelles are also a significant component. Interactions between α-synuclein and lipids have been previously identified as relevant for Parkinson’s disease pathology, however molecular insights into their interactions have remained elusive. Here we present cryo-electron microscopy structures of six α-synuclein fibrils in complex with lipids, revealing specific lipid-fibril interactions. We observe that phospholipids promote an alternative protofilament fold, mediate an unusual arrangement of protofilaments, and fill the central cavities of the fibrils. Together with our previous studies, these structures also indicate a mechanism for fibril-induced lipid extraction, which is likely to be involved in the development of α-synucleinopathies. Specifically, one potential mechanism for the cellular toxicity is the disruption of intracellular vesicles mediated by fibrils and oligomers, and therefore the modulation of these interactions may provide a promising strategy for future therapeutic interventions."],["dc.identifier.doi","10.1038/s41467-022-34552-7"],["dc.identifier.pii","34552"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/117993"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","2041-1723"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The 3D structure of lipidic fibrils of α-synuclein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12404"],["dc.bibliographiccitation.issue","82"],["dc.bibliographiccitation.journal","Chemical Communications"],["dc.bibliographiccitation.lastpage","12407"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Munari, Francesca"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Assfalg, Michael"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2020-12-10T18:11:26Z"],["dc.date.available","2020-12-10T18:11:26Z"],["dc.date.issued","2019"],["dc.description.abstract","This NMR probe of water dynamics enables viscosity determination in concentrated and crowded solutions and allows quantifying internal fluidity within biological condensates."],["dc.description.abstract","We present an NMR method based on natural abundance 17 O relaxation of water to determine effective viscosity in biological aqueous samples. The method accurately captures viscosity of dilute and crowded protein solutions and offers a fairly simple way to quantify the internal fluidity of biological condensates formed through phase separation."],["dc.description.abstract","This NMR probe of water dynamics enables viscosity determination in concentrated and crowded solutions and allows quantifying internal fluidity within biological condensates."],["dc.description.abstract","We present an NMR method based on natural abundance 17 O relaxation of water to determine effective viscosity in biological aqueous samples. The method accurately captures viscosity of dilute and crowded protein solutions and offers a fairly simple way to quantify the internal fluidity of biological condensates formed through phase separation."],["dc.identifier.doi","10.1039/C9CC06124J"],["dc.identifier.eissn","1364-548X"],["dc.identifier.issn","1359-7345"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16666"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74010"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1364-548X"],["dc.relation.issn","1359-7345"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A facile oxygen-17 NMR method to determine effective viscosity in dilute, molecularly crowded and confined aqueous media"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","109"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","The European Physical Journal E - Soft Matter"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Jain, R."],["dc.contributor.author","Petri, M."],["dc.contributor.author","Kirschbaum, S."],["dc.contributor.author","Feindt, H."],["dc.contributor.author","Steltenkamp, Siegfried"],["dc.contributor.author","Sonnenkalb, S."],["dc.contributor.author","Becker, S."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Menzel, A."],["dc.contributor.author","Burg, T. P."],["dc.contributor.author","Techert, S."],["dc.date.accessioned","2017-09-07T11:47:08Z"],["dc.date.available","2017-09-07T11:47:08Z"],["dc.date.issued","2013"],["dc.description.abstract","Small-angle X-ray scattering provides global, shape-sensitive structural information about macromolecules in solution. Its extension to time dimension in the form of time-resolved SAXS investigations and combination with other time-resolved biophysical methods contributes immensely to the study of protein dynamics. TR-SAXS can also provide unique information about the global structures of transient intermediates during protein dynamics. An experimental set-up with low protein consumption is essential for an extensive use of TR-SAXS experiments on protein dynamics. In this direction, a newly developed 20-microchannel microfluidic continuous-flow mixer was combined with SAXS. With this set-up, we demonstrate ubiquitin unfolding dynamics after rapid mixing with the chaotropic agent Guanidinium-HCl within milliseconds using only similar to 40 nanoliters of the protein sample per scattering image. It is suggested that, in the future, this new TR-SAXS platform will help to increase the use of time-resolved small-angle X-ray scattering, wide-angle X-ray scattering and neutron scattering experiments for studying protein dynamics in the early millisecond regime. The potential research field for this set-up includes protein folding, protein misfolding, aggregation in amyloidogenic diseases, function of intrinsically disordered proteins and various protein-ligand interactions."],["dc.identifier.doi","10.1140/epje/i2013-13109-9"],["dc.identifier.gro","3142281"],["dc.identifier.isi","000325224100001"],["dc.identifier.pmid","24092048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6542"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Nanoscale Photon Imaging of the DFG [SFB 755]"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1292-8941"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Techert (Structural Dynamics in Chemical Systems)"],["dc.title","X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E4971"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E4977"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Turriani, Elisa"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Schön, Margarete"],["dc.contributor.author","Schön, Michael P."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Becker, Dorothea"],["dc.date.accessioned","2018-04-23T11:47:36Z"],["dc.date.available","2018-04-23T11:47:36Z"],["dc.date.issued","2017"],["dc.description.abstract","Recent epidemiological and clinical studies have reported a significantly increased risk for melanoma in people with Parkinson’s disease. Because no evidence could be obtained that genetic factors are the reason for the association between these two diseases, we hypothesized that of the three major Parkinson’s disease-related proteins—α-synuclein, LRRK2, and Parkin—α-synuclein might be a major link. Our data, presented here, demonstrate that α-synuclein promotes the survival of primary and metastatic melanoma cells, which is the exact opposite of the effect that α-synuclein has on dopaminergic neurons, where its accumulation causes neuronal dysfunction and death. Because this detrimental effect of α-synuclein on neurons can be rescued by the small molecule anle138b, we explored its effect on melanoma cells. We found that treatment with anle138b leads to massive melanoma cell death due to a major dysregulation of autophagy, suggesting that α-synuclein is highly beneficial to advanced melanoma because it ensures that autophagy is maintained at a homeostatic level that promotes and ensures the cell’s survival."],["dc.identifier.doi","10.1073/pnas.1700200114"],["dc.identifier.gro","3142238"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13362"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0027-8424"],["dc.title","Treatment with diphenyl–pyrazole compound anle138b/c reveals that α-synuclein protects melanoma cells from autophagic cell death"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Angewandte Chemie"],["dc.contributor.author","Karschin, Niels"],["dc.contributor.author","Wolkenstein, Klaus"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2020-08-04T08:39:39Z"],["dc.date.available","2020-08-04T08:39:39Z"],["dc.date.issued","2020"],["dc.description.abstract","Anisotropic NMR has gained increasing popularity to determine the structure and specifically the configuration of small, flexible, non‐crystallizable molecules. However, it suffers from the necessity to dissolve the analyte in special media such as liquid crystals or polymer gels. Generally, small degrees of alignment are also caused by an anisotropic magnetic susceptibility of the molecule, for example, induced by aromatic moieties. For this mechanism, the alignment can be predicted via density functional theory. Here we show that both residual dipolar couplings and residual chemical shift anisotropies can be acquired from natural products without special sample preparation using magnetically induced alignment. On the two examples of the novel natural product gymnochrome G and the alkaloid strychnine, these data, together with the predicted alignment, yield the correct configuration with high certainty."],["dc.identifier.doi","10.1002/ange.202004881"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67514"],["dc.language.iso","en"],["dc.relation.eissn","1521-3757"],["dc.relation.issn","0044-8249"],["dc.relation.orgunit","Abteilung Geobiologie"],["dc.title","Magnetically Induced Alignment of Natural Products for Stereochemical Structure Determination via NMR"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3875"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Helvetica Chimica Acta"],["dc.bibliographiccitation.lastpage","3888"],["dc.bibliographiccitation.volume","86"],["dc.contributor.author","Krebs, Joachim"],["dc.contributor.author","Helms, Volkhard"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Carafoli, E."],["dc.date.accessioned","2017-09-07T11:45:06Z"],["dc.date.available","2017-09-07T11:45:06Z"],["dc.date.issued","2003"],["dc.description.abstract","Calcium may have a static, structure-stabilizing role in biological organs like the bones and the teeth, or may fulfill a dynamic function in cells as a regulator of signal-transduction pathways. This is made possible by the properties of the Ca2+ ion (e.g., high dehydration rate, great flexibility in coordinating ligands, largely irregular geometry of the coordination sphere). Since Ca2+ is a universal carrier of signals, the control of its homeostasis is of central importance for the organism. It involves exchanges between the skeleton (which is the major calcium reservoir) and the extracellular and intracellular fluids. It also involves the intestine and the kidney, the organs of Ca absorption and release, respectively. The highly integrated homeostasis process consists of a number of hormonally controlled feedback loops, and an elaborate system of membrane channels, exchangers, and pumps that control the Ca2+ flux into and out of cells."],["dc.identifier.doi","10.1002/hlca.200390325"],["dc.identifier.gro","3144140"],["dc.identifier.isi","000187253800029"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1731"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","0018-019X"],["dc.title","The regulation of the calcium signal by membrane pumps"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11983"],["dc.bibliographiccitation.issue","43"],["dc.bibliographiccitation.journal","Chemistry - A European Journal"],["dc.bibliographiccitation.lastpage","11986"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Perez-Balado, Carlos"],["dc.contributor.author","Sun, Han"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lera, Angel R. de"],["dc.contributor.author","Navarro-Vazquez, Armando"],["dc.date.accessioned","2017-09-07T11:43:23Z"],["dc.date.available","2017-09-07T11:43:23Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1002/chem.201101385"],["dc.identifier.gro","3142653"],["dc.identifier.isi","000297316100005"],["dc.identifier.pmid","21922573"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0947-6539"],["dc.title","Residual Dipolar Coupling Enhanced NMR Spectroscopy and Chiroptics: A Powerful Combination for the Complete Elucidation of Symmetrical Small Molecules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","58"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Magnetic Resonance (1969)"],["dc.bibliographiccitation.lastpage","66"],["dc.bibliographiccitation.volume","149"],["dc.contributor.author","Kramer, Frank"],["dc.contributor.author","Peti, Wolfgang"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Glaser, Steffen J."],["dc.date.accessioned","2017-09-07T11:46:40Z"],["dc.date.available","2017-09-07T11:46:40Z"],["dc.date.issued","2001"],["dc.description.abstract","Modified phase-cycled Carr-Purcell-type multiple-pulse sequences are optimized for coherence and polarization transfer in homonuclear Hartmann-Hahn experiments applied to partially oriented samples. Compared to previously suggested experiments, the sequences yield considerably improved scaling factors for residual dipolar coupling constants, resulting in improved transfer efficiency. (C) 2001 Academic Press."],["dc.identifier.doi","10.1006/jmre.2000.2271"],["dc.identifier.gro","3144299"],["dc.identifier.isi","000168078800009"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1908"],["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","1090-7807"],["dc.title","Optimized homonuclear Carr-Purcell-type dipolar mixing sequences"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","81"],["dc.bibliographiccitation.journal","Archives of Biochemistry and Biophysics"],["dc.bibliographiccitation.lastpage","91"],["dc.bibliographiccitation.volume","628"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Smith, Colin A."],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2018-01-17T11:31:26Z"],["dc.date.available","2018-01-17T11:31:26Z"],["dc.date.issued","2017"],["dc.description.abstract","Protein function can be modulated or dictated by the amplitude and timescale of biomolecular motion, therefore it is imperative to study protein dynamics. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique capable of studying timescales of motion that range from those faster than molecular reorientation on the picosecond timescale to those that occur in real-time. Across this entire regime, NMR observables can report on the amplitude of atomic motion, and the kinetics of atomic motion can be ascertained with a wide variety of experimental techniques from real-time to milliseconds and several nanoseconds to picoseconds. Still a four orders of magnitude window between several nanoseconds and tens of microseconds has remained elusive. Here, we highlight new relaxation dispersion NMR techniques that serve to cover this \"hidden-time\" window up to hundreds of nanoseconds that achieve atomic resolution while studying the molecule under physiological conditions."],["dc.identifier.doi","10.1016/j.abb.2017.05.016"],["dc.identifier.pmid","28576576"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11679"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1096-0384"],["dc.title","Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","23"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","44"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Farès, Christophe"],["dc.contributor.author","Lakomek, Nils-Alexander"],["dc.contributor.author","Walter, Korvin F. A."],["dc.contributor.author","Frank, Benedikt T. C."],["dc.contributor.author","Meiler, Jens"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:46:50Z"],["dc.date.available","2017-09-07T11:46:50Z"],["dc.date.issued","2009"],["dc.description.abstract","This study presents the first application of the model-free analysis (MFA) (Meiler in J Am Chem Soc 123:6098-6107, 2001; Lakomek in J Biomol NMR 34:101-115, 2006) to methyl group RDCs measured in 13 different alignment media in order to describe their supra-tau (c) dynamics in ubiquitin. Our results indicate that methyl groups vary from rigid to very mobile with good correlation to residue type, distance to backbone and solvent exposure, and that considerable additional dynamics are effective at rates slower than the correlation time tau (c). In fact, the average amplitude of motion expressed in terms of order parameters S (2) associated with the supra-tau (c) window brings evidence to the existence of fluctuations contributing as much additional mobility as those already present in the faster ps-ns time scale measured from relaxation data. Comparison to previous results on ubiquitin demonstrates that the RDC-derived order parameters are dominated both by rotameric interconversions and faster libration-type motions around equilibrium positions. They match best with those derived from a combined J-coupling and residual dipolar coupling approach (Chou in J Am Chem Soc 125:8959-8966, 2003) taking backbone motion into account. In order to appreciate the dynamic scale of side chains over the entire protein, the methyl group order parameters are compared to existing dynamic ensembles of ubiquitin. Of those recently published, the broadest one, namely the EROS ensemble (Lange in Science 320:1471-1475, 2008), fits the collection of methyl group order parameters presented here best. Last, we used the MFA-derived averaged spherical harmonics to perform highly-parameterized rotameric searches of the side chains conformation and find expanded rotamer distributions with excellent fit to our data. These rotamer distributions suggest the presence of concerted motions along the side chains."],["dc.identifier.doi","10.1007/s10858-009-9354-7"],["dc.identifier.gro","3143062"],["dc.identifier.isi","000269079100005"],["dc.identifier.pmid","19652920"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/534"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0925-2738"],["dc.title","Accessing ns-mu s side chain dynamics in ubiquitin with methyl RDCs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]