Altieri, Dario C.2022-08-232022-08-232004-01-172008-06-18<p>Cell Cycle. 2004 Mar;3(3):255-6. Epub 2004 Mar 1.</p>1538-4101 (Print)10.4161/cc.3.3.71114726679https://hdl.handle.net/20.500.14038/41130Understanding how tumor cells manage to survive and proliferate in ever-changing and often harmful microenvironments is a daunting challenge in tumor biology, and a major cause of treatment failure in the oncology clinic. Recent data have now demonstrated a direct link between the molecular chaperone Hsp90 and survivin, a dual regulator of cell proliferation and cell death over-expressed in virtually every human tumor. While the survivin-Hsp90 association may help tumor cells elevate their anti-apoptotic threshold and promote their proliferation, it may also provide new opportunities for rational cancer therapy.en-USAnimals*ApoptosisHSP90 Heat-Shock ProteinsHumansMicrotubule-Associated ProteinsNeoplasm ProteinsNeoplasmsProtein BindingLife SciencesMedicine and Health SciencesJournal Articlehttps://escholarship.umassmed.edu/oapubs/392533104oapubs/392