Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity.
J Med Chem
; 54(12): 4034-41, 2011 Jun 23.
Article
in En
| MEDLINE
| ID: mdl-21526763
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 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Purines
/
Adenosine Triphosphatases
/
Furans
/
Heat-Shock Proteins
Language:
En
Journal:
J Med Chem
Journal subject:
QUIMICA
Year:
2011
Type:
Article
Affiliation country:
United kingdom