Zobrazeno 1 - 10
of 1 001
pro vyhledávání: '"Hsp104"'
Multiple aspects of amyloid dynamics in vivo integrate to establish prion variant dominance in yeast
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 17 (2024)
Prion variants are self-perpetuating conformers of a single protein that assemble into amyloid fibers and confer unique phenotypic states. Multiple prion variants can arise, particularly in response to changing environments, and interact within an or
Externí odkaz:
https://doaj.org/article/09163c51c3bd47b7b5afff72eac803e7
Autor:
Samantha J. Ganser, Bridget A. McNish, Gillian L. Schwanitz, John L. Delaney, Bridget A. Corpus, Brenda A. Schilke, Anup K. Biswal, Chandan Sahi, Elizabeth A. Craig, Justin K. Hines
Publikováno v:
Frontiers in Molecular Biosciences, Vol 11 (2024)
J-domain proteins (JDPs) are obligate cochaperones of Hsp70s. The Class A JDP Apj1 of the yeast cytosol has an unusually complex region between the N-terminal J-domain and the substrate binding region—often called the Grich or GF region in Class A
Externí odkaz:
https://doaj.org/article/d1fe474f7674468bb48d114d8a70c204
Akademický článek
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Autor:
Adam S. Knier, Emily E. Davis, Hannah E. Buchholz, Jane E. Dorweiler, Lauryn E. Flannagan, Anita L. Manogaran
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 15 (2022)
Patients with the fatal disorder Transthyretin Amyloidosis (ATTR) experience polyneuropathy through the progressive destruction of peripheral nervous tissue. In these patients, the transthyretin (TTR) protein dissociates from its functional tetrameri
Externí odkaz:
https://doaj.org/article/2e5013c89f9c4db9a0cc7fdc6ee85038
Autor:
Erika V. Grosfeld, Anastasia Yu. Beizer, Alexander A. Dergalev, Michael O. Agaphonov, Alexander I. Alexandrov
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 16, p 12758 (2023)
Protein misfolding is a common feature of aging, various diseases and stresses. Recent work has revealed that misfolded proteins can be gathered into specific compartments, which can limit their deleterious effects. Chaperones play a central role in
Externí odkaz:
https://doaj.org/article/997fc914391a400f992b9260ada2808f
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 13, p 10833 (2023)
The yeast Sup35 protein misfolds into the infectious [PSI+] prion, which is then propagated by the severing activity of the molecular chaperone, Hsp104. Unlike other yeast prions, this prion is unique in that it is efficiently cured by the overexpres
Externí odkaz:
https://doaj.org/article/1371c4c7b1584fe8aae2bcddefde086a
Autor:
Jintana Wongwigkarn
Publikováno v:
Warasan Witthayasat Lae Theknoloyi Mahawitthayalai Mahasarakham, Vol 39, Iss 1, Pp 113-126 (2020)
Molecular chaperone Hsp104, also known as heat shock protein in yeast Saccharomyces cerevisiae, plays an essential role in thermotorelance response enabling yeast cell survival at high temperature. Hsp104 mediates the misfolding and the aggregation
Externí odkaz:
https://doaj.org/article/186c37dda1974f78801ce78765dc747c
Akademický článek
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Autor:
Chih-Yen King
Publikováno v:
Viruses, Vol 14, Iss 11, p 2337 (2022)
Prions replicate by a self-templating mechanism. Infidelity in the process can lead to the emergence of new infectious structures, referred to as variants or strains. The question of whether prions are prone to mis-templating is not completely answer
Externí odkaz:
https://doaj.org/article/d1c3bcfb0cfb444f978dfed3ae0cb697
Autor:
Huiqing Xia, Linlin Chen, Zhuo Fan, Mengya Peng, Jingya Zhao, Wenbo Chen, Haiyang Li, Yan Shi, Shengli Ding, Honglian Li
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
Heat shock protein Hsp104, a homolog of the bacterial chaperone ClpB and plant Hsp100, plays an essential part in the response to heat and various chemical agents in Saccharomyces cerevisiae. However, their functions remain largely unknown in plant f
Externí odkaz:
https://doaj.org/article/dcfb1f8dfea2439d89c9e55df5999c62