Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Alexander P. Ducruet"'
Autor:
John S. Lazo, Alexander P. Ducruet, Rachel P. Sikorski, Peter Wipf, Thomas H. Graham, Andreas Vogt
Publikováno v:
Chemical Biology Drug Design. 67:66-73
Structure–activity analyses of synthetic disorazole C1 and eight of its analogs indicate that the presence of a vinyl oxirane moiety or a tetraene sequence is not necessary for potent cytotoxic and antimitotic properties. Using an automated multipa
Publikováno v:
Annual Review of Pharmacology and Toxicology. 45:725-750
▪ Abstract The complete sequencing of the human genome is generating many novel targets for drug discovery. Understanding the pathophysiological roles of these putative targets and assessing their suitability for therapeutic intervention has become
Autor:
John S. Lazo, Alexander P. Ducruet
Publikováno v:
Journal of Biological Chemistry. 278:31838-31842
Cdc25A regulates cell cycle progression, has oncogenic and anti-apoptotic activity, and is over-expressed in many human tumors. Phosphorylation by Chk1 and Cds1/Chk2 down-regulates Cdc25A levels in response to genotoxic stresses. Nevertheless, it rem
Autor:
Beomjun Joo, John S. Lazo, Eileen C. Southwick, and Andreas Vogt, Peter Wipf, Diana C. Aslan, Kathleen A Cooley, Alexander P. Ducruet
Publikováno v:
Journal of Medicinal Chemistry. 44:4042-4049
The Cdc25 dual specificity phosphatases have central roles in coordinating cellular signaling processes and cell proliferation, but potent and selective inhibitors are lacking. We experimentally examined the 1990 compound National Cancer Institute Di
Autor:
Andreas Vogt, Jon Chesebrough, John S. Lazo, Alexander P. Ducruet, Takahito Adachi, Kaoru Nemoto, Brian I. Carr
Publikováno v:
Journal of Biological Chemistry. 276:20544-20550
Protein phosphorylation frequently results in the subcellular redistribution of key signaling molecules, and this spatial change is critical for their activity. Here we have probed the effects of a Cdc25 inhibitor, 2-(2-mercaptoethanol)-3-methyl-1,4-
Publikováno v:
Molecular Pharmacology. 64:199-201
Autor:
Bethany Petrik, John S. Lazo, Billy W. Day, Raghavan Balachandran, Carolyn A. Kitchens, Brianne S. Raccor, Jane R. Stout, Peter Wipf, Fengfeng L. Xu, Marni Brisson Tierno, Thomas H. Graham, Celeste E. Reese, William S. Saunders, Claire E. Walczak, Alexander P. Ducruet
Disorazoles comprise a family of 29 macrocyclic polyketides isolated from the fermentation broth of the myxobacterium Sorangium cellulosum. The major fermentation product, disorazole A(1), was found previously to irreversibly bind to tubulin and to h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::485e802de4275d3e915fdfd0842dfd6d
https://europepmc.org/articles/PMC2649750/
https://europepmc.org/articles/PMC2649750/
Autor:
Peter, Wipf, Thomas H, Graham, Andreas, Vogt, Rachel P, Sikorski, Alexander P, Ducruet, John S, Lazo
Publikováno v:
Chemical biologydrug design. 67(1)
Structure-activity analyses of synthetic disorazole C(1) and eight of its analogs indicate that the presence of a vinyl oxirane moiety or a tetraene sequence is not necessary for potent cytotoxic and antimitotic properties. Using an automated multipa
Publikováno v:
Nature reviews. Drug discovery. 1(12)
Dual-specificity protein phosphatases are a subclass of protein tyrosine phosphatases that are uniquely able to hydrolyse the phosphate ester bond on both a tyrosine and a threonine or serine residue on the same protein. Dual-specificity phosphatases
Publikováno v:
Oncogene. 19(56)
One hallmark of neoplasia is the deregulation of cell cycle control mechanisms, which is secondary to altered protein phosphorylation. Dual specificity protein phosphatases uniquely dephosphorylate both phosphoserines/threonines and phosphotyrosines