Savastano, Adriana

[["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.volume","119"],["dc.contributor.author","Cario, Alisa"],["dc.contributor.author","Savastano, Adriana"],["dc.contributor.author","Wood, Neil B."],["dc.contributor.author","Liu, Zhu"],["dc.contributor.author","Previs, Michael J."],["dc.contributor.author","Hendricks, Adam G."],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Berger, Christopher L."],["dc.date.accessioned","2022-04-01T10:02:46Z"],["dc.date.available","2022-04-01T10:02:46Z"],["dc.date.issued","2022"],["dc.description.abstract","Significance The microtubule-associated protein Tau is strongly linked to a number of neurological diseases. Disease onset is typically associated with weakened interaction with the microtubule, but this widely accepted model is based on hyperphosphorylation or mutations within the C-terminal microtubule-binding domain of Tau. Here, we find that an N-terminal disease-associated mutation in Tau, R5L, does not reduce Tau affinity for microtubules but instead, modifies the N-terminal structure, altering Tau’s behavior and ability to condense on the microtubule surface. Our findings challenge the current paradigms of both how mutations in Tau lead to disease and the functional role of the N-terminal region of Tau."],["dc.identifier.doi","10.1073/pnas.2114215119"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106002"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.title","The pathogenic R5L mutation disrupts formation of Tau complexes on the microtubule by altering local N-terminal structure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Protein Science"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Zachrdla, Milan"],["dc.contributor.author","Savastano, Adriana"],["dc.contributor.author","Ibáñez de Opakua, Alain"],["dc.contributor.author","Cima‐Omori, Maria‐Sol"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2022-09-01T09:50:32Z"],["dc.date.available","2022-09-01T09:50:32Z"],["dc.date.issued","2022"],["dc.description.sponsorship"," H2020 European Research Council https://doi.org/10.13039/100010663"],["dc.identifier.doi","10.1002/pro.4409"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113734"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1469-896X"],["dc.relation.issn","0961-8368"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.title","Contributions of the N‐terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA‐induced phase separation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Nature Chemistry"],["dc.contributor.author","Ibáñez de Opakua, Alain"],["dc.contributor.author","Geraets, James A."],["dc.contributor.author","Frieg, Benedikt"],["dc.contributor.author","Dienemann, Christian"],["dc.contributor.author","Savastano, Adriana"],["dc.contributor.author","Rankovic, Marija"],["dc.contributor.author","Cima-Omori, Maria-Sol"],["dc.contributor.author","Schröder, Gunnar F."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2022-10-04T10:21:34Z"],["dc.date.available","2022-10-04T10:21:34Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient β-structure and a stable preformed α-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG–FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities."],["dc.identifier.doi","10.1038/s41557-022-01035-7"],["dc.identifier.pii","1035"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114448"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-600"],["dc.relation.eissn","1755-4349"],["dc.relation.issn","1755-4330"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Molecular interactions of FG nucleoporin repeats at high resolution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]