Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Benita Jebarupa"'
Publikováno v:
Biophysical Chemistry. 241:27-37
The self-assembly of intrinsically disordered protein tau into paired helical filament forms one of the hallmarks of Alzheimer's disease. However, the facets of innately disordered structure of tau and its conversion to a β-sheet-rich fibril during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5de06f188f9d6a9447a38171ff7e4ca6
https://doi.org/10.1016/j.bpc.2018.07.005
https://doi.org/10.1016/j.bpc.2018.07.005
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866:668-679
Intrinsically disordered protein tau plays a central role in maintaining neuronal network by stabilizing microtubules in axon. Tau reportedly possesses random coil architecture, which is largely inert to alteration in solution conditions. However, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a79103f740e5e3a3bbd04945520a80b
https://doi.org/10.1016/j.bbapap.2018.04.004
https://doi.org/10.1016/j.bbapap.2018.04.004
Autor:
Aiswarya Sasikumaran, Gopa Mitra, Amit Kumar Mandal, Boby Mathew, Bindu Y. Srinivasu, Benita Jebarupa, Tinku Thomas, Smitha Joseph
Publikováno v:
Biochimica et biophysica acta. General subjects. 1863(6)
Background Aggregation of tau into paired helical filament (PHF) is a hallmark of Alzheimer's disease (AD), and Cys-mediated disulfide bond formation plays a vital role in tau fibrillation. While intermolecular disulfide bond between Cys residues in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c48a1e38bf29b71962df22a689cd51a2
https://pubmed.ncbi.nlm.nih.gov/30853336
https://pubmed.ncbi.nlm.nih.gov/30853336