Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kourtney M. Goode"'
Autor:
Timothy L. Ratliff, Renee E. Vickman, Kourtney M. Goode, Tony R. Hazbun, Dino P. Petrov, V. Jo Davisson, Pete E. Pascuzzi, Scott A. Crist
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1861:1992-2006
Background Inhibition of Hsp90 is desirable due to potential downregulation of oncogenic clients. Early generation inhibitors bind to the N-terminal domain (NTD) but C-terminal domain (CTD) inhibitors are a promising class because they do not induce
Autor:
Larisa Avramova, Fiona M. Thomas, Andrew A. Bieberich, V. Jo Davisson, Kourtney M. Goode, Tony R. Hazbun, Bartek Rajwa
Publikováno v:
SLAS Discovery. 22:706-719
Compounds that modulate the heat shock protein (HSP) network have potential in a broad range of research applications and diseases. A yeast-based liquid culture assay that measured time-dependent turbidity enabled the high-throughput screening of dif
Autor:
Tony R. Hazbun, Jean-Christophe Rochet, Lake N. Paul, Holli M. Drendel, Kiran Aslam, Kourtney M. Goode, Chai-jui Tsai, Josephat M. Asiago
Publikováno v:
Department of Medicinal Chemistry and Molecular Pharmacology Faculty Publications
The Saccharomyces cerevisiae heat shock protein Hsp31 is a stress-inducible homodimeric protein that is involved in diauxic shift reprogramming and has glyoxalase activity. We show that substoichiometric concentrations of Hsp31 can abrogate aggregati
Publikováno v:
Molecular Cancer Therapeutics. 14:B89-B89
The 90-kDa heat shock protein 90 (Hsp90) is a chaperone protein responsible for the folding and activation of numerous proteins disregulated in various cancers that drive oncogenesis. Consequently, inhibition of Hsp90 is thought to be an attractive a