Hsp104 is a heat-shock protein. It is known to reverse toxicity of mutant α-synuclein, TDP-43, FUS, and TAF15 in yeast cells. Conserved in prokaryotes...
8 KB (813 words) - 21:01, 20 June 2024
to a prion negative phenotype). This is the result of inhibition of the Hsp104 chaperone protein known to play an important role in prion fiber fragmentation...
6 KB (673 words) - 16:00, 2 October 2023
classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. The Hsp60 family of protein chaperones are termed chaperonins...
29 KB (3,499 words) - 07:16, 20 February 2024
[PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104". J Biol Chem. 278 (49): 49636–43. doi:10.1074/jbc.M307996200. PMID 14507919...
44 KB (5,063 words) - 06:38, 22 August 2024
of steroid receptors and transcription factors 100 kDa ClpB, ClpA, ClpX Hsp104 (CLPB) Unfolding of insoluble protein aggregates; co-factor of DnaK/Hsp70...
49 KB (5,533 words) - 10:41, 19 July 2024
refolding to the prion configuration is assisted by chaperone proteins such as Hsp104. All known prions induce the formation of an amyloid fold, in which the...
99 KB (10,708 words) - 11:17, 27 August 2024
[PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104". The Journal of Biological Chemistry. 278 (49): 49636–43. doi:10.1074/jbc...
34 KB (4,134 words) - 03:30, 12 July 2024
heritable forms of protein. Because of the action of chaperones, especially Hsp104, proteins that code for [PSI+] and [URE3] can convert from non-prion to...
23 KB (2,738 words) - 14:54, 15 August 2024
coli and Ssa1-Ydj1/Sis1-Sse1/Fe1 in yeast) and Hsp100 (ClpB in E. coli and Hsp104 in yeast) chaperones for protein disaggregation and refolding. Hsp70 interacts...
24 KB (2,885 words) - 02:45, 28 March 2024
thermotolerance in Saccharomyces cerevisiae without heat shock protein hsp104 and in the absence of protein synthesis". FEBS Letters. 288 (1–2): 86–90...
6 KB (667 words) - 10:44, 19 February 2024
Michaelis, S.; Brodsky, J. L. (2018). "Substrate Insolubility Dictates Hsp104-Dependent Endoplasmic-Reticulum-Associated Degradation". Molecular Cell...
8 KB (1,015 words) - 01:22, 18 June 2024
Nups. Several of these inducible genes, including GAL1, INO1, TSA2, and HSP104 contain gene recruitment sequences (GRSs) found in the promoter, which are...
12 KB (1,588 words) - 11:37, 28 July 2024
have functions other than proteolysis. ClpB (human CLPB "Hsp78", yeast Hsp104) break up insoluble protein aggregates in conjunction with DnaK/Hsp70. They...
7 KB (794 words) - 21:54, 1 September 2023
potassium transport mutant: identification of a mammalian member of the Clp/HSP104 family". Gene. 152 (2): 157–63. doi:10.1016/0378-1119(94)00697-Q. PMID 7835694...
18 KB (2,098 words) - 10:50, 5 January 2024
[PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104". Journal of Biological Chemistry. 278 (49): 49636–43. doi:10.1074/jbc.M307996200...
6 KB (709 words) - 23:29, 15 February 2024
the disaggregase chaperone, AAA protein HSP104, localizes to the IPOD. It is yet to be determined if HSP104 functions in the IPOD or is simply sequestered...
22 KB (2,457 words) - 09:53, 31 July 2024