The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.

Speculations on the functions of the major heat shock and glucose-regulated proteins

Hugh R.B. Pelham · Cell · 1986 · 1.6K citations

Protein Chemistry, Protein Function, Protein Assembly +10

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

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

Krzysztof Liberek, D. D. Ang, Costa Georgopoulos et al. · Proceedings of the National Academy of Sciences · 1991 · 850 citations

Atpase Activity, Biochemistry, Protein Folding +12

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

Hartwig Schröder, Thomas Langer, F. Ulrich Hartl et al. · The EMBO Journal · 1993 · 607 citations

Chromatin, Genome Instability, Protein Function +10

The multicatalytic and 26 S proteases.

Martin Rechsteiner, Laura Hoffman, Wolfgang Dubiel · Journal of Biological Chemistry · 1993 · 473 citations · Full text

Biochemistry, Natural Sciences, Biocatalysis +2