Max-Planck-Institut für Biophysikalische Chemie

[["dc.bibliographiccitation.firstpage","16522"],["dc.bibliographiccitation.issue","26"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","16523"],["dc.bibliographiccitation.volume","99"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Neher, Erwin"],["dc.date.accessioned","2017-09-07T11:45:11Z"],["dc.date.available","2017-09-07T11:45:11Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1073/pnas.022708199"],["dc.identifier.gro","3144145"],["dc.identifier.isi","000180101600006"],["dc.identifier.pmid","12486246"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1737"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Specificity emerges in the dissection of diacylglycerol- and protein kinase C-mediated signalling pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","444"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Pflügers Archiv European Journal of Physiology"],["dc.bibliographiccitation.lastpage","449"],["dc.bibliographiccitation.volume","419"],["dc.contributor.author","Doroshenko, Peter"],["dc.contributor.author","Neher, Erwin"],["dc.date.accessioned","2022-03-01T11:47:08Z"],["dc.date.available","2022-03-01T11:47:08Z"],["dc.date.issued","1991"],["dc.identifier.doi","10.1007/BF00370786"],["dc.identifier.pii","BF00370786"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103925"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1432-2013"],["dc.relation.issn","0031-6768"],["dc.title","Pertussis-toxin-sensitive inhibition by (-) baclofen of Ca signals in bovine chromaffin cells"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["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.firstpage","341"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","351"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Buhr, Florian"],["dc.contributor.author","Jha, Sujata"],["dc.contributor.author","Thommen, Michael"],["dc.contributor.author","Mittelstaet, Joerg"],["dc.contributor.author","Kutz, Felicitas"],["dc.contributor.author","Schwalbe, Harald"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Komar, Anton A."],["dc.date.accessioned","2017-09-07T11:54:38Z"],["dc.date.available","2017-09-07T11:54:38Z"],["dc.date.issued","2016"],["dc.description.abstract","In all genomes, most amino acids are encoded by more than one codon. Synonymous codons can modulate protein production and folding, but the mechanism connecting codon usage to protein homeostasis is not known. Here we show that synonymous codon variants in the gene encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotranslational folding of protein domains monitored in real time by Forster resonance energy transfer and fluorescence-intensity changes. Gamma-B crystallins produced from mRNAs with changed codon bias have the same amino acid sequence but attain different conformations, as indicated by altered in vivo stability and in vitro protease resistance. 2D NMR spectroscopic data suggest that structural differences are associated with different cysteine oxidation states of the purified proteins, providing a link between translation, folding, and the structures of isolated proteins. Thus, synonymous codons provide a secondary code for protein folding in the cell."],["dc.identifier.doi","10.1016/j.molcel.2016.01.008"],["dc.identifier.gro","3141730"],["dc.identifier.isi","000372325800004"],["dc.identifier.pmid","26849192"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/435"],["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","1097-4164"],["dc.relation.issn","1097-2765"],["dc.title","Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","305"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Journal of Biochemistry"],["dc.bibliographiccitation.lastpage","310"],["dc.bibliographiccitation.volume","225"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","SEREBRYANIK, A. I."],["dc.contributor.author","Ovcharenko, G. V."],["dc.contributor.author","Elskaya, A. V."],["dc.date.accessioned","2017-09-07T11:51:25Z"],["dc.date.available","2017-09-07T11:51:25Z"],["dc.date.issued","1994"],["dc.description.abstract","80 S ribosomes from a number of higher eukaryotic organisms are able to hydrolyse ATP and GTP without the addition of soluble protein factors. ATPase seems to be an intrinsic activity of the ribosome, as indicated by the findings that ATPase activity is not diminished upon dissociation of ribosomes and reassociation of subunits, by washing with 0.66 M (KCl + NH4Cl) or 0.6 M LiCl treatment and ethanol precipitation; 1.5 M LiCl treatment removes only 40% ATPase activity. 80 S ribosomes are able to bind a variety of NTPs, NDPs and NTP analogues, with a preference for ATP. Effective inhibitors of the ribosomal ATPase are ammonium metavanadate and alcaloid emetine. The ATPase activity is present on both ribosomal subunits, which may reflect the existence of two catalytical sites for ATP on the 80 S ribosome. Ribosomal ATPase is stimulated by the occupancy of the A site, in particular with charged tRNA. The ATPase inhibitor adenylylimidodiphosphate almost completely prevents elongation-factor(EF)-1-dependent binding of Phe-tRNA(Phe) to the A site. The hydrolysis of ATP, therefore, is likely to be involved in the mechanism of tRNA binding to the A site of the 80 S ribosome. As far as wide substrate specificity and possible participation in tRNA interaction with the ribosome are concerned, the ribosomal ATPase seems to be similar to EF-3 found in fungi. A synergism in ATPase activities of yeast EF-3 and rabbit liver ribosomes at high ATP concentration and certain ribosome/EF-3 ratios have been observed. Rabbit liver ribosomes seem to stimulate the ATPase activity of yeast EF-3 similar to the mechanism in yeast ribosomes, though less efficiently."],["dc.identifier.doi","10.1111/j.1432-1033.1994.00305.x"],["dc.identifier.gro","3144718"],["dc.identifier.isi","A1994PJ53200033"],["dc.identifier.pmid","7925450"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2373"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.relation.issn","0014-2956"],["dc.title","ATPASE STRONGLY BOUND TO HIGHER EUKARYOTIC RIBOSOMES"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Walla, Peter Jomo"],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Grunwald, Matthias"],["dc.contributor.author","van den Heuvel, Laura"],["dc.contributor.author","Timo, Aspelmeier"],["dc.contributor.author","Zagrebelsky, Marta"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Munk, Axel"],["dc.date.accessioned","2018-11-07T09:44:56Z"],["dc.date.available","2018-11-07T09:44:56Z"],["dc.date.issued","2014"],["dc.identifier.isi","000337000400120"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34507"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","San Francisco, CA"],["dc.title","Nanoscopy by Fluorescence Demodulation and Polarization Angle Narrowing"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","871121"],["dc.bibliographiccitation.journal","Frontiers in Molecular Biosciences"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Mercier, Evan"],["dc.contributor.author","Wang, Xiaolin"],["dc.contributor.author","Bögeholz, Lena A. K."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-06-01T09:39:51Z"],["dc.date.available","2022-06-01T09:39:51Z"],["dc.date.issued","2022"],["dc.description.abstract","Nascent polypeptides emerging from the ribosome during translation are rapidly scanned and processed by ribosome-associated protein biogenesis factors (RPBs). RPBs cleave the N-terminal formyl and methionine groups, assist cotranslational protein folding, and sort the proteins according to their cellular destination. Ribosomes translating inner-membrane proteins are recognized and targeted to the translocon with the help of the signal recognition particle, SRP, and SRP receptor, FtsY. The growing nascent peptide is then inserted into the phospholipid bilayer at the translocon, an inner-membrane protein complex consisting of SecY, SecE, and SecG. Folding of membrane proteins requires that transmembrane helices (TMs) attain their correct topology, the soluble domains are inserted at the correct (cytoplasmic or periplasmic) side of the membrane, and – for polytopic membrane proteins – the TMs find their interaction partner TMs in the phospholipid bilayer. This review describes the recent progress in understanding how growing nascent peptides are processed and how inner-membrane proteins are targeted to the translocon and find their correct orientation at the membrane, with the focus on biophysical approaches revealing the dynamics of the process. We describe how spontaneous fluctuations of the translocon allow diffusion of TMs into the phospholipid bilayer and argue that the ribosome orchestrates cotranslational targeting not only by providing the binding platform for the RPBs or the translocon, but also by helping the nascent chains to find their correct orientation in the membrane. Finally, we present the auxiliary role of YidC as a chaperone for inner-membrane proteins. We show how biophysical approaches provide new insights into the dynamics of membrane protein biogenesis and raise new questions as to how translation modulates protein folding."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," European Research Council"],["dc.identifier.doi","10.3389/fmolb.2022.871121"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108581"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","2296-889X"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Cotranslational Biogenesis of Membrane Proteins in Bacteria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","299"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","307"],["dc.bibliographiccitation.volume","63"],["dc.contributor.author","Gapsys, Vytautas"],["dc.contributor.author","Narayanan, Raghavendran L."],["dc.contributor.author","Xiang, ShengQi"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:49:30Z"],["dc.date.available","2018-11-07T09:49:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Intrinsically disordered proteins (IDPs) are best described by ensembles of conformations and a variety of approaches have been developed to determine IDP ensembles. Because of the large number of conformations, however, cross-validation of the determined ensembles by independent experimental data is crucial. The (1)J(C alpha H alpha) coupling constant is particularly suited for cross-validation, because it has a large magnitude and mostly depends on the often less accessible dihedral angle psi. Here, we reinvestigated the connection between (1)J(C alpha H alpha) values and protein backbone dihedral angles. We show that accurate amino-acid specific random coil values of the (1)J(C alpha H alpha) coupling constant, in combination with a reparameterized empirical Karplus-type equation, allow for reliable cross-validation of molecular ensembles of IDPs."],["dc.description.sponsorship","DFG [ZW71/8-1]"],["dc.identifier.doi","10.1007/s10858-015-9990-z"],["dc.identifier.isi","000365088800008"],["dc.identifier.pmid","26433382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35521"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1573-5001"],["dc.relation.issn","0925-2738"],["dc.title","Improved validation of IDP ensembles by one-bond C alpha-H alpha scalar couplings"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","258a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Vaiana, Andrea C."],["dc.contributor.author","Bock, Lars V."],["dc.contributor.author","Blau, Christian"],["dc.contributor.author","Schroeder, Gunnar F."],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2022-03-01T11:44:56Z"],["dc.date.available","2022-03-01T11:44:56Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bpj.2012.11.1447"],["dc.identifier.pii","S0006349512026938"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103165"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Modulation of Intersubunit Interactions during tRNA Translocation through the Ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]