Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli.

This publication has 30 references indexed in Scilit:

• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
  Nature, 1991
• DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.
  Genes & Development, 1990
• The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
  Cell, 1990
• Renaturation of denatured λ repressor requires heat shock proteins
  Cell, 1990
• Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
  Nature, 1989
• Export of Protein: A Biochemical View
  Annual Review of Microbiology, 1987
• Speculations on the functions of the major heat shock and glucose-regulated proteins
  Cell, 1986
• Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors
  Gene, 1985
• Sequence analysis of mutations that prevent export of λ receptor, an Escherichia coli outer membrane protein
  Nature, 1980
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970