期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 54, 期 12, 页码 4034-4041出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm101625x
关键词
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78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved in protein folding that plays a role in cancer cell proliferation. Binding of adenosine-derived inhibitors to Grp78 was characterized by surface plasmon resonance and isothermal titration calorimetry. The most potent compounds were 13 (VER-155008) with K-D = 80 nM and 14 with K-D = 60 nM. X-ray crystal structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed differences in the binding site between Grp78 and homologous proteins.
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