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Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.

Data up to Jan 2025

Published1993
Citations32
References33

Total Citations Per Year

Abstract

References (33)

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

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

1989 • 317 citations

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1990 • 291 citations

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

1985 • 272 citations

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

1983 • 270 citations

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein

1991 • 245 citations

A Kinetic Partitioning Model of Selective Binding of Nonnative Proteins by the Bacterial Chaperone SecB

1991 • 225 citations

Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.

1989 • 158 citations

No Specific Recognition of Leader Peptide by SecB, a Chaperone Involved in Protein Export

1990 • 141 citations

PrlA (SecY) and PrlG (SecE) interact directly and function sequentially during protein translocation in E. coli

1990 • 129 citations

Affinity chromatographic isolation of the periplasmic maltose binding protein of Escherichia coli

1978 • 124 citations

Escherichia coli SecB protein associates with exported protein precursors in vivo.

1989 • 123 citations

Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure

1992 • 120 citations

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

1988 • 117 citations

Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein.

1988 • 95 citations

Genetic studies on the inability of beta-galactosidase to be translocated across the Escherichia coli cytoplasmic membrane

1989 • 90 citations

Direct selection for gene replacement events in yeast

1983 • 86 citations

Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system

1989 • 84 citations

Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB.

1989 • 83 citations

Characterization of the Escherichia coli protein-export gene secB

1989 • 69 citations

A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.

1992 • 54 citations

SecB protein: A cytosolic export factor that associates with nascent exported proteins

1990 • 41 citations

Evidence for isopentenyladenine modification on a cell cycle-regulated protein

1991 • 41 citations

Two cellular components, PrlA and SecB, that recognize different sequence determinants are required for efficient protein export

1988 • 33 citations

Binding of a soluble factor of Escherichia coli to preproteins does not require ATP and appears to be the first step in protein export.

1989 • 20 citations

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