Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Naihsuan, Guy"'
Autor:
Nina R. Ortiz, Naihsuan Guy, Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, Marc B. Cox
Publikováno v:
Subcellular Biochemistry ISBN: 9783031147395
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a4b09892f2b77ae7c0faa2f009173286
https://doi.org/10.1007/978-3-031-14740-1_2
https://doi.org/10.1007/978-3-031-14740-1_2
Autor:
Nina R, Ortiz, Naihsuan, Guy, Yenni A, Garcia, Jeffrey C, Sivils, Mario D, Galigniana, Marc B, Cox
Publikováno v:
Sub-cellular biochemistry. 101
The Hsp90 chaperone is known to interact with a diverse array of client proteins. However, in every case examined, Hsp90 is also accompanied by a single or several co-chaperone proteins. One class of co-chaperone contains a tetratricopeptide repeat (
Autor:
Cheryl Storer Samaniego, Ji Ho Suh, Arundhati Chattopadhyay, Karen Olivares, Naihsuan Guy, Jeffrey C Sivils, Prasenjit Dey, Fumiaki Yumoto, Robert J Fletterick, Anders M Strom, Jan-Åke Gustafsson, Paul Webb, Marc B Cox
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0134015 (2015)
FKBP52 and β-catenin have emerged in recent years as attractive targets for prostate cancer treatment. β-catenin interacts directly with the androgen receptor (AR) and has been characterized as a co-activator of AR-mediated transcription. FKBP52 is
Externí odkaz:
https://doaj.org/article/36f3df2021f144458e404729f6693ced
Autor:
Artem Cherkasov, Ashley N Payan, Fuqiang Ban, Naihsuan Guy, Huan Xie, Candace Cooper, Dong Liang, Oscar Ekpenyong, Jing Ma, Marc B. Cox
Publikováno v:
Pharmaceuticals
Volume 13
Issue 11
Pharmaceuticals, Vol 13, Iss 386, p 386 (2020)
Volume 13
Issue 11
Pharmaceuticals, Vol 13, Iss 386, p 386 (2020)
Background: GMC1 (2-(1H-benzimidazol-2-ylsulfanyl)-N-[(Z)-(4-methoxyphenyl) methylideneamino] acetamide) effectively inhibits androgen receptor function by binding directly to FKBP52. This is a novel mechanism for the treatment of castration resistan
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:
Valerie Chun Ling Lin, Fiona Tay, Naihsuan Guy, Paola Ramos, Marc B. Cox, Yu Zuan Or, Thomas Lufkin, Petra Kraus, Yenni A. Garcia, Smeeta Shrestha, Yang Sun
Publikováno v:
International Journal of Biological Sciences
Tetratricopeptide repeat domain 9A (TTC9A) is a target gene of estrogen and progesterone. It is over-expressed in breast cancer. However, little is known about the physiological function of TTC9A. The objectives of this study were to establish a Ttc9
Publikováno v:
Current molecular pharmacology. 9(2)
Steroid hormone receptors are ligand-dependent transcription factors that require the dynamic, ordered assembly of multimeric chaperone complexes to reach a functional conformation. Heat shock protein (Hsp) 70 and Hsp90 serve as the central chaperone
Publikováno v:
The Networking of chaperones by Co-chaperones
Subcellular Biochemistry ISBN: 9783319117300
Subcellular Biochemistry ISBN: 9783319117300
Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6db86085861402f7b019891d8736520d
https://link.springer.com/chapter/10.1007/978-3-319-11731-7_2
https://link.springer.com/chapter/10.1007/978-3-319-11731-7_2
Publikováno v:
The FASEB Journal. 28