期刊
CHEMISTRY & BIOLOGY
卷 11, 期 9, 页码 1261-1267出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2004.06.014
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资金
- NCI NIH HHS [CA31845] Funding Source: Medline
- NIMH NIH HHS [MH064801] Funding Source: Medline
Structurally simplified analogs of bryostatin 1, a marine natural product in clinical trials for the treatment of cancer, have been shown to be up to 50 times more potent than bryostatin 1 at inducing the translocation of PKCdelta-GFP from the cytosol of rat basophilic leukemia (RBL) cells. The end distribution of the protein is similar for all three compounds, despite a significant difference in translocation kinetics. The potency of the compounds for inducing the translocation response appears to be only qualitatively related to their binding affinity for PKC, highlighting the importance of using binding affinity in conjunction with real-time measurements of protein localization for the pharmacological profiling of biologically active agents.
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