Human Heat Shock 70kDa Binding

Stress Response Profiles in Human Fibroblasts Exposed to Heat Shock or Oxidative Stress

demonstrated a specific upregulation of Hsp70 mRNA and protein after heat shock, while heme oxygenase 1 (HO1 or Hsp32) mRNA and protein was specifically upregulated following H2 O2 -induced oxidative stress. Hsp70 and HO1 should therefore be considered

Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein

The 72 kDa heat shock protein (HSP72) is a molecular chaperone that binds native protein with low affinity. These interactions can alter function of the substrate, a property known as HSP-mediated activity control. In the present work, BIAcore

Determination of Metal Interactions with the Chaperone Hspa5 in Human Astrocytoma Cells and Rat Astrocyte Primary Cultures

with chaperones in these cells is of interest. Furthermore, Pb and Cu bind strongly to the molecular chaperone heat shock 70 kDa protein Hspa5, also known as glucose-regulated protein 78 (Grp78) or immunoglobulin-binding protein (BiP). This chapter describes