Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Gary Flom"'
Publikováno v:
Current Genetics. 58:149-163
The molecular chaperone Hsp90 cooperates with multiple cochaperone proteins as it promotes the folding and activation of diverse client proteins. Some cochaperones regulate the ATPase activity of Hsp90, while others appear to promote Hsp90 interactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d19385e1b728418dabf3dce0389b90f
https://doi.org/10.1007/s00294-012-0373-7
https://doi.org/10.1007/s00294-012-0373-7
Publikováno v:
Molecular Biology of the Cell. 19:5249-5258
Ydj1 of Saccharomyces cerevisiae is an abundant cytosolic Hsp40, or J-type, molecular chaperone. Ydj1 cooperates with Hsp70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the maturation of Hsp90 client protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a01887136872eb879a5bc02b706b324
https://doi.org/10.1091/mbc.e08-04-0435
https://doi.org/10.1091/mbc.e08-04-0435
Publikováno v:
Biochemical Journal. 404:159-167
The molecular chaperone Hsp (heat-shock protein) 90 is critical for the activity of diverse cellular client proteins. In a current model, client proteins are transferred from Hsp70 to Hsp90 in a process mediated by the co-chaperone Sti1/Hop, which ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa4315fe3a481fc07a7994dd0861fe67
https://doi.org/10.1042/bj20070084
https://doi.org/10.1042/bj20070084
Publikováno v:
Genetics. 172:41-51
Through simultaneous interactions with Hsp70 and Hsp90 via separate tetratricopeptide repeat (TPR) domains, the cochaperone protein Hop/Sti1 has been proposed to play a critical role in the transfer of client proteins from Hsp70 to Hsp90. However, no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6114ec378c27a97288a26d88837dbf68
https://doi.org/10.1534/genetics.105.045815
https://doi.org/10.1534/genetics.105.045815
Publikováno v:
Molecular and cellular biology. 27(2)
The ATP-dependent molecular chaperone Hsp90 and partner cochaperone proteins are required for the folding and activity of diverse cellular client proteins, including steroid hormone receptors and multiple oncogenic kinases. Hsp90 undergoes nucleotide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d83a0ec5471fb9097087cff572e6c2e6
https://pubmed.ncbi.nlm.nih.gov/17101799
https://pubmed.ncbi.nlm.nih.gov/17101799
Publikováno v:
Biochemical Journal; 2007, Vol. 404 Issue 1, p159-167, 9p