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Rezaei-Ghaleh, Nasrollah
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Rezaei-Ghaleh, Nasrollah
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Rezaei-Ghaleh, Nasrollah
Alternative Name
Rezaei-Ghaleh, N.
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2012Journal Article [["dc.bibliographiccitation.firstpage","930"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","ChemBioChem"],["dc.bibliographiccitation.lastpage","950"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Blackledge, Martin"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-06-01T10:49:44Z"],["dc.date.available","2021-06-01T10:49:44Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1002/cbic.201200093"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86393"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","1439-4227"],["dc.title","Intrinsically Disordered Proteins: From Sequence and Conformational Properties toward Drug Discovery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2014Journal Article [["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"]]Details DOI PMID PMC WOS2014Conference Abstract [["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Buhl, Timo"],["dc.contributor.author","Braun, Alexander"],["dc.contributor.author","Forkel, Susann"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","van Werven, Lars"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Mempel, Martin"],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Haenssle, Holger Andreas"],["dc.date.accessioned","2018-11-07T09:43:01Z"],["dc.date.available","2018-11-07T09:43:01Z"],["dc.date.issued","2014"],["dc.format.extent","E32"],["dc.identifier.isi","000332335500205"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34085"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Cologne, GERMANY"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","Routes of internalization for Melan-A/TAT fusion peptides differ considerably between human dendritic cells and other non-phagocytic cell types"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS2018Journal Article [["dc.bibliographiccitation.firstpage","15262"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Angewandte Chemie. International Edition"],["dc.bibliographiccitation.lastpage","15266"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Rezaei‐Ghaleh, Nasrollah"],["dc.contributor.author","Parigi, Giacomo"],["dc.contributor.author","Soranno, Andrea"],["dc.contributor.author","Holla, Andrea"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Schuler, Benjamin"],["dc.contributor.author","Luchinat, Claudio"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2020-12-10T14:05:34Z"],["dc.date.available","2020-12-10T14:05:34Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1002/anie.201808172"],["dc.identifier.eissn","1521-3773"],["dc.identifier.issn","1433-7851"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69576"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Local and Global Dynamics in Intrinsically Disordered Synuclein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2021Journal Article [["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"]]Details DOI2012Journal Article [["dc.bibliographiccitation.firstpage","no"],["dc.bibliographiccitation.issue","29"],["dc.bibliographiccitation.journal","ChemInform"],["dc.bibliographiccitation.lastpage","no"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Blackledge, Martin"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-12-08T12:30:02Z"],["dc.date.available","2021-12-08T12:30:02Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1002/chin.201229271"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96301"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.issn","0931-7597"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","ChemInform Abstract: Intrinsically Disordered Proteins: From Sequence and Conformational Toward Drug Discovery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2021Journal Article [["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"]]Details DOI2020Journal Article [["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"]]Details DOI2018Journal Article [["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"]]Details DOI2014Journal Article Research Paper [["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"]]Details DOI PMID PMC WOS
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