Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

Small heat shock proteins are molecular chaperones.

Ursula Jakob, Matthias Gaestel, Katrin Engel et al. · Journal of Biological Chemistry · 1993 · 1.4K citations · Full text

Murine Hsp25, Protein Chemistry, Molecular Chaperones +14

THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN

Christian B. Anfinsen, E Haber, Michael Sela et al. · Proceedings of the National Academy of Sciences · 1961 · 1.2K citations · Full text

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

Thomas Langer, Chi Zen Lu, Harrison Echols et al. · Nature · 1992 · 966 citations

Protein Function, Protein Assembly, Biochemistry +9

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

Pierre Goloubinoff, John T. Christeller, Anthony A. Gatenby et al. · Nature · 1989 · 744 citations

Protein Chemistry, Unfolded State Depends, Cellular Enzymology +10

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

Pierre Goloubinoff, Anthony A. Gatenby, George H. Lorimer · Nature · 1989 · 703 citations

Protein Folding, Virulence Factor, Protein Biosynthesis +7