Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Bryan A. Bernat"'
Autor:
Emanuel Zlibut, Jody C. May, Yansheng Wei, Dennis Gessmann, Constance S. Wood, Bryan A. Bernat, Teresa E. Pugh, Lauren Palmer-Jones, Ronan P. Cosquer, Eric Dybeck, John A. McLean
Publikováno v:
Analytical Chemistry.
Autor:
Eli Wallace, Kevin Koch, James D. Winkler, Patrice A. Lee, Joe Lyssikatos, Brian Hurley, Allison Marlow, Stefan Gross, Barbara J. Brandhuber, Darin Smith, Janet Parry, Ron J. Evans, Heidi Colwell, Josh Ballard, Bryan A. Bernat, Vivienne Marsh, Tammie C. Yeh
Supplementary Data, Yeh, et al. from Biological Characterization of ARRY-142886 (AZD6244), a Potent, Highly Selective Mitogen-Activated Protein Kinase Kinase 1/2 Inhibitor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cb220f9585897004967629e2407f636
https://doi.org/10.1158/1078-0432.22441213.v1
https://doi.org/10.1158/1078-0432.22441213.v1
Autor:
Eli Wallace, Kevin Koch, James D. Winkler, Patrice A. Lee, Joe Lyssikatos, Brian Hurley, Allison Marlow, Stefan Gross, Barbara J. Brandhuber, Darin Smith, Janet Parry, Ron J. Evans, Heidi Colwell, Josh Ballard, Bryan A. Bernat, Vivienne Marsh, Tammie C. Yeh
Purpose: The Ras-Raf-mitogen-activated protein kinase kinase (MEK) pathway is overactive in many human cancers and is thus a target for novel therapeutics. We have developed a highly potent and selective inhibitor of MEK1/2. The purpose of these stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::406a4a31b0cf89e0543cd3f66dfd4a9e
https://doi.org/10.1158/1078-0432.c.6518341.v1
https://doi.org/10.1158/1078-0432.c.6518341.v1
Publikováno v:
Journal of Bacteriology. 183:2380-2383
We demonstrate that the Bacillus subtilis fosB(yndN) gene encodes a fosfomycin resistance protein. Expression of fosB requires ς W , and both fosB and sigW mutants are fosfomycin sensitive. FosB is a metallothiol transferase related to the FosA clas
Publikováno v:
Biochemistry. 40:3378-3384
An important aspect of the catalytic mechanism of microsomal glutathione transferase (MGST1) is the activation of the thiol of bound glutathione (GSH). GSH binding to MGST1 as measured by thiolate anion formation, proton release, and Meisenheimer com
Publikováno v:
Chemico-Biological Interactions. :41-50
A number of glutathione (GSH) transferases are now known in prokaryotes and eukaryotes. The enzymes appear to be primarily involved in the metabolism of foreign compounds. At least six distinct classes of soluble GSH transferases have been identified
Publikováno v:
Biochemistry. 36:3050-3055
The enzyme conferring resistance to the antibiotic fosfomycin [(1R,2S)-1,2-epoxypropylphosphonic acid] originally reported by Suarez and co-workers [Area, P., Hardisson, C.,Suarez, J. E. (1990) Antimicrob. Agents Chemother. 34, 844-848] is demonstrat
Publikováno v:
The Journal of Organic Chemistry. 63:3778-3780
Autor:
Richard N. Armstrong, Christopher L. Rife, Stoyan K. Smoukov, Joshua Telser, Brian M. Hoffman, Bryan A Bernat
Publikováno v:
Journal of the American Chemical Society. 124(10)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid. The reaction catalyzed by FosA involves the attack by glutathione on fosfomycin to yield the p
Autor:
Richard N. Armstrong, Bryan A. Bernat
Publikováno v:
Biochemistry. 40(42)
The fosfomycin resistance protein, FosA, catalyzes the Mn(2+)-dependent addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering the antibiotic inactive. The enzyme is a homodimer of 16 kDa subunits, each of