Toxoplasma gondii Hsp90 is a Potential Drug Target Whose Expression and Subcellular Localization are Developmentally Regulated

Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence

J. Robbins, Stephen M. Dilwortht, Ronald A. Laskey et al. · Cell · 1991 · 1.5K citations

Chromatin, Chromatin Remodeling, Natural Sciences +6

Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent

C. Erec Stebbins, Alicia A. Russo, Christine Schneider et al. · Cell · 1997 · 1.4K citations · Full text

Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone

Chrisostomos Prodromou, S. Mark Roe, Ronan O’Brien et al. · Cell · 1997 · 1.3K citations · Full text

Atp/adp-binding Site, Structural Characterization, Protein Function +11

The biology of heat shock proteins and molecular chaperones

Johannes Büchner · Trends in Biochemical Sciences · 1994 · 1.2K citations

Protein Chemistry, Molecular Chaperones, Protein Function +6

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone invivo

Barry Panaretou · The EMBO Journal · 1998 · 726 citations · Full text

Protein Function, Cellular Enzymology, Biochemistry +6