Zobrazeno 1 - 4
of 4
pro vyhledávání: '"David S. Culbertson"'
Autor:
Nina R. Ortiz, Laura J. Blair, Marc B. Cox, Jeffrey C. Sivils, David S. Culbertson, Jane Dyson, Ashley N Payan, Dan Finley, Jazzmin Jovonna Owens, Jason E. Gestwicki, Szu Yu Kuo, William E. Balch, Jaideep Chaudhary, Jay Singh, Darren M. Hutt, Chad A. Dickey, Naihsuan Guy, Bradley D. Tait, Shravan Kumar Komaragiri
Publikováno v:
Cell chemical biology, vol 27, iss 3
Cell Chem Biol
Cell Chem Biol
Summary Hsp90 plays an important role in health and is a therapeutic target for managing misfolding disease. Compounds that disrupt co-chaperone delivery of clients to Hsp90 target a subset of Hsp90 activities, thereby minimizing the toxicity of pan-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c800b824e420391f461894a73274c69
https://escholarship.org/uc/item/3k55j4vx
https://escholarship.org/uc/item/3k55j4vx
Autor:
Marc B. Cox, Jay Singh, David S. Culbertson, William E. Balch, Darren M. Hutt, Chad A. Dickey, Naihsuan Guy, Bradley D. Tait, Jane Dyson, Jeffrey C. Sivils, Szu Yu Kuo, Jason E. Gestwicki
The core cytosolic Hsp90 chaperone/co-chaperone complex plays a critical role in proteostasis management of human health and disease. To identify novel compounds that alter the ability of the Hsp90 co-chaperone Aha1 to modulate the ATPase activity fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f853874b526418c3bf886b9aa7a25c43
https://doi.org/10.1101/412908
https://doi.org/10.1101/412908
Autor:
John S. Olson, David S. Culbertson
Publikováno v:
Biochemistry. 49:6052-6063
The unfolding of wild-type holomyoglobin in the ferric state (metMb) appears to be a simple two-state process, even though hemichrome spectra are often observed and apoMb denaturation involves an intermediate. To resolve these discrepancies, we measu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::272143d6a36c19188f7395225a98c8b9
https://doi.org/10.1021/bi1006942
https://doi.org/10.1021/bi1006942
Autor:
John S. Olson, David S. Culbertson
Publikováno v:
Biophysical Journal. 98:639a
Mammalian myoglobin has served as the archetype globin for understanding the folding properties of single domain globins with the 3 on 3 helical fold. After removal of heme, the resultant apo-Mb shows a loss of structure in the proximal F helix and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c69b8ffe03ae0139c61a9f2e07637986
https://doi.org/10.1016/j.bpj.2009.12.3501
https://doi.org/10.1016/j.bpj.2009.12.3501