The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.

Principles that Govern the Folding of Protein Chains

1973 • 6,771 citations

A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots

1984 • 2,189 citations

Novel Method for Detection of β-Lactamases by Using a Chromogenic Cephalosporin Substrate

1972 • 1,857 citations

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

1986 • 1,574 citations

A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

1988 • 1,504 citations

The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure

1989 • 1,446 citations

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1988 • 1,316 citations

70K heat shock related proteins stimulate protein translocation into microsomes

1988 • 1,276 citations

Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea

1986 • 926 citations

Proteins as molecular chaperones

1987 • 910 citations

Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells

1989 • 884 citations

Protein translocation across the endoplasmic reticulum

1984 • 825 citations

Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly

1989 • 763 citations

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

1989 • 737 citations

Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria

1986 • 723 citations

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

1989 • 703 citations

Folding and association of proteins

1987 • 697 citations

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

1989 • 693 citations

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

1989 • 676 citations

Experimental studies of protein folding and unfolding

1979 • 535 citations

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

1989 • 491 citations

Catalysis of protein folding by prolyl isomerase

1987 • 488 citations

Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

1989 • 474 citations

Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli

1986 • 473 citations

Purification and properties of groE, a host protein involved in bacteriophage assembly

1979 • 426 citations

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein

1988 • 388 citations

Purification and properties of the groES morphogenetic protein of Escherichia coli.

1986 • 364 citations

Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains

1989 • 357 citations

The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle

1986 • 336 citations

Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes

1988 • 330 citations

The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein

1988 • 326 citations

Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.

1989 • 317 citations

The ‘molten globule’ state is involved in the translocation of proteins across membranes?

1988 • 275 citations

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

1979 • 272 citations

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.

1987 • 257 citations

Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.

1989 • 250 citations

A Highly Evolutionarily Conserved Mitochondrial Protein Is Structurally Related to the Protein Encoded by the Escherichia coli groEL Gene

1988 • 247 citations

Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes.

1988 • 187 citations

ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.

1988 • 135 citations

Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics.

1988 • 117 citations

The molecular chaperone concept.

1989 • 113 citations

The precursor of beta-lactamase: purification, properties and folding kinetics.

1989 • 110 citations

The Escherichia coli groE chaperonins.

1990 • 65 citations

Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding protein

1987 • 54 citations