A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

[6] Use of T7 RNA polymerase to direct expression of cloned genes

F. William Studier, Alan H. Rosenberg, John J. Dunn et al. · Methods in enzymology on CD-ROM/Methods in enzymology · 1990 · 6.6K citations · Full text

Engineering, Rna Biology, Molecular Biology +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

Peptide-binding specificity of the molecular chaperone BiP

Gregory C. Flynn, Jan Pohl, Mark T. Flocco et al. · Nature · 1991 · 773 citations

Biochemistry, Protein Assembly, Protein Folding +4

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

Judith Frydman, Elmar Nimmesgern, Kenzo Ohtsuka et al. · Nature · 1994 · 654 citations

Molecular Chaperones, Protein Assembly, Protein Folding +7