Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity
AT Macias, DS Williamson, N Allen… - Journal of medicinal …, 2011 - ACS Publications
AT Macias, DS Williamson, N Allen, J Borgognoni, A Clay, Z Daniels, P Dokurno…
Journal of medicinal chemistry, 2011•ACS Publications78 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 …
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 …
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.
ACS Publications