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

Data up to Jan 2025

Published1989
Citations317
References50

Total Citations Per Year

Abstract

References (50)

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

1951 • 319,299 citations

A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding

1976 • 225,752 citations

An improved assay for nanomole amounts of inorganic phosphate

1979 • 2,157 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

An enzymic method for the trace iodination of immunoglobulins and other proteins

1969 • 1,414 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

Proteins as molecular chaperones

1987 • 910 citations

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

1989 • 703 citations

E. coli mutant pleiotropically defective in the export of secreted proteins

1981 • 512 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

Signal sequences

1989 • 417 citations

SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.

1989 • 406 citations

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

1988 • 388 citations

Suppressor mutations that restore export of a protein with a defective signal sequence

1981 • 382 citations

Protein localization in E. coli: Is there a common step in the secretion of periplasmic and outer-membrane proteins?

1981 • 359 citations

Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle.

1986 • 337 citations

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

1988 • 326 citations

RNA Synthesis Initiates In Vitro Conversion of M13 DNA to Its Replicative Form

1972 • 304 citations

A signal sequence receptor in the endoplasmic reticulum membrane

1987 • 291 citations

Evidence for specificity at an early step in protein export in Escherichia coli

1985 • 272 citations

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

1979 • 272 citations

Mutations in a new gene, secB, cause defective protein localization in Escherichia coli

1983 • 270 citations

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

1987 • 257 citations

Modulation of Folding Pathways of Exported Proteins by the Leader Sequence

1988 • 243 citations

Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.

1988 • 243 citations

SecA protein is required for secretory protein translocation into E. coli membrane vesicles

1988 • 239 citations

Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation

1983 • 234 citations

Unity in Function in the Absence of Consensus in Sequence: Role of Leader Peptides in Export

1989 • 222 citations

Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein.

1978 • 209 citations

SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

1989 • 206 citations

Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein.

1980 • 200 citations

ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle

1988 • 196 citations

Uncoupling Translocation from Translation: Implications for Transport of Proteins Across Membranes

1986 • 195 citations

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

1988 • 187 citations

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

1986 • 181 citations

ATP is essential for protein translocation into Escherichia coli membrane vesicles.

1985 • 163 citations

The “trigger factor cycle” includes ribosomes, presecretory proteins, and the plasma membrane

1988 • 162 citations

Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12.

1980 • 156 citations

Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles.

1986 • 142 citations

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

1988 • 135 citations

Cell biology: An unfolding story of protein translocation

1986 • 126 citations

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

1988 • 117 citations

Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product).

1978 • 103 citations

The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export

1989 • 97 citations

Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins

1984 • 84 citations

Characterization of the Escherichia coli protein-export gene secB

1989 • 69 citations

Preprotein conformation: the year's major theme in translocation studies

1988 • 63 citations

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Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form… (1989) – The EMBO Journal | Metascience Observatory Explorer