Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity
Journal of Medicinal Chemistry2011Vol. 54(12), pp. 4034–4041
Citations Over TimeTop 10% of 2011 papers
Alba T. Macias, D.S. Williamson, Nicola J. Allen, Jenifer Borgognoni, Alexandra Clay, Zoe Daniels, P. Dokurno, Martin J. Drysdale, Geraint L. Francis, Christopher J Graham, Rob Howes, Natalia Matassova, James B. Murray, Rachel Parsons, T. Shaw, A.E. Surgenor, Lindsey Terry, Yikang Wang, Mike Wood, Andrew J. Massey
Abstract
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 KD = 80 nM and 14 with KD = 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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