Rezaei-Ghaleh, Nasrollah

[["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","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"]]

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[["dc.bibliographiccitation.firstpage","9933"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry Letters"],["dc.bibliographiccitation.lastpage","9939"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Vemulapalli, Sahithya Phani Babu"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.date.accessioned","2021-12-01T09:20:45Z"],["dc.date.available","2021-12-01T09:20:45Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1021/acs.jpclett.1c02595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94265"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1948-7185"],["dc.relation.issn","1948-7185"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Combined High-Pressure and Multiquantum NMR and Molecular Simulation Propose a Role for N-Terminal Salt Bridges in Amyloid-Beta"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","cphc.202100542"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.contributor.author","Mamone, Salvatore"],["dc.contributor.author","Glöggler, Stefan"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Rezaei‐Ghaleh, Nasrollah"],["dc.date.accessioned","2021-09-01T06:42:49Z"],["dc.date.available","2021-09-01T06:42:49Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1002/cphc.202100542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89150"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation.eissn","1439-7641"],["dc.relation.issn","1439-4235"],["dc.title","Early Divergence in Misfolding Pathways of Amyloid‐Beta Peptides"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2007765"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Advanced Functional Materials"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Aliakbari, Farhang"],["dc.contributor.author","Mohammad‐Beigi, Hossein"],["dc.contributor.author","Abbasi, Shahsanam"],["dc.contributor.author","Rezaei‐Ghaleh, Nasrollah"],["dc.contributor.author","Lermyte, Frederik"],["dc.contributor.author","Parsafar, Soha"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Tafreshi, Azita Parvaneh"],["dc.contributor.author","O'Connor, Peter B."],["dc.contributor.author","Collingwood, Joanna F."],["dc.contributor.author","Christiansen, Gunna"],["dc.contributor.author","Sutherland, Duncan S."],["dc.contributor.author","Jensen, Poul Henning"],["dc.contributor.author","Morshedi, Dina"],["dc.contributor.author","Otzen, Daniel E."],["dc.date.accessioned","2021-04-14T08:31:00Z"],["dc.date.available","2021-04-14T08:31:00Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1002/adfm.202007765"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83448"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1616-3028"],["dc.relation.issn","1616-301X"],["dc.title","Multiple Protective Roles of Nanoliposome‐Incorporated Baicalein against Alpha‐Synuclein Aggregates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9174"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Nanoscale"],["dc.bibliographiccitation.lastpage","9185"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Aliakbari, Farhang"],["dc.contributor.author","Mohammad-Beigi, Hossein"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Dehghani Esmatabad, Faezeh"],["dc.contributor.author","Eslampanah Seyedi, Hadieh Alsadat"],["dc.contributor.author","Bardania, Hassan"],["dc.contributor.author","Tayaranian Marvian, Amir"],["dc.contributor.author","Collingwood, Joanna F."],["dc.contributor.author","Christiansen, Gunna"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Otzen, Daniel E."],["dc.contributor.author","Morshedi, Dina"],["dc.date.accessioned","2020-12-10T18:11:23Z"],["dc.date.available","2020-12-10T18:11:23Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1039/C8NR00632F"],["dc.identifier.eissn","2040-3372"],["dc.identifier.issn","2040-3364"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73993"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16201"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","16209"],["dc.bibliographiccitation.volume","136"],["dc.contributor.author","Parigi, Giacomo"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Giachetti, Andrea"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Blackledge, Martin"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Luchinat, Claudio"],["dc.date.accessioned","2017-09-07T11:45:24Z"],["dc.date.available","2017-09-07T11:45:24Z"],["dc.date.issued","2014"],["dc.description.abstract","Intrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP alpha-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in alpha-synuclein, which are related to genetic forms of Parkinson's disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems."],["dc.identifier.doi","10.1021/ja506820r"],["dc.identifier.gro","3142017"],["dc.identifier.isi","000345308700018"],["dc.identifier.pmid","25331250"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3623"],["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","Long-Range Correlated Dynamics in Intrinsically Disordered Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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.journal","Protein Science"],["dc.contributor.author","Fuentes‐Monteverde, Juan Carlos"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Rezaei‐Ghaleh, Nasrollah"],["dc.date.accessioned","2021-04-14T08:30:54Z"],["dc.date.available","2021-04-14T08:30:54Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1002/pro.4010"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83406"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1469-896X"],["dc.relation.issn","0961-8368"],["dc.title","Biomolecular phase separation through the lens of sodium‐23 NMR"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]