Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4095
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dc.contributor.authorKumar, Harishen_US
dc.contributor.authorUDGAONKAR, JAYANT B.en_US
dc.date.accessioned2019-09-27T06:03:04Z
dc.date.available2019-09-27T06:03:04Z
dc.date.issued2019-10en_US
dc.identifier.citationBiochimica et Biophysica Acta-Proteins and Proteomics, 1867(10), 922-932.en_US
dc.identifier.issn1570-9639en_US
dc.identifier.issn1878-1454en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4095-
dc.identifier.urihttps://doi.org/10.1016/j.bbapap.2019.04.004en_US
dc.description.abstractThe dynamic nature of the tau protein under physiological conditions is likely to be critical for it to perform its diverse functions inside a cell. Under some conditions, this intrinsically disordered protein assembles into pathogenic aggregates that are self-perpetuating, toxic and infectious in nature. The role of liquid-liquid phase separation in the initiation of the aggregation reaction remains to be delineated. Depending on the nature of the aggregate, its structure, and its localization, neurodegenerative disorders with diverse clinical features are manifested. The prion-like mechanism by which these aggregates propagate and spread across the brain is not well understood. Various factors (PTMs, mutations) have been strongly associated with the pathological aggregates of tau. However, little is known about how these factors modulate the pathological properties linked to aggregation. This review describes the current progress towards understanding the mechanism of propagation of tau aggregates.en_US
dc.language.isoenen_US
dc.publisherElsevier B.V.en_US
dc.subjectMicrotubule-Associated Proteinen_US
dc.subjectPaired Helical Filamentsen_US
dc.subjectProgressive Supranuclear Palsyen_US
dc.subjectAmyloid Fibril Formationen_US
dc.subjectSingle-Molecule Freten_US
dc.subjectAlzheimers-Diseaseen_US
dc.subjectAlpha-Synucleinen_US
dc.subjectPhase-Separationen_US
dc.subjectIn-Vitroen_US
dc.subjectNeurofibrillary Tanglesen_US
dc.subjectTOC-SEP-2019en_US
dc.subject2019en_US
dc.titleMechanistic approaches to understand the prion-like propagation of aggregates of the human tau proteinen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Biologyen_US
dc.identifier.sourcetitleBiochimica et Biophysica Acta-Proteins and Proteomicsen_US
dc.publication.originofpublisherForeignen_US
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