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Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

Data up to Jan 2025

Published1997
Citations80
References44

Total Citations Per Year

Abstract

References (44)

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SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF

1995 • 298 citations

Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme

1997 • 285 citations

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

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

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SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

1990 • 229 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

Two distinct ATP‐binding domains are needed to promote protein export by Escherichia coli SecA ATPase

1993 • 197 citations

Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli

1988 • 188 citations

The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids.

1993 • 176 citations

Bacterial periplasmic permeases belong to a family of transport proteins operating fromEscherichia colito human: Traffic ATPases

1990 • 174 citations

SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state

1994 • 158 citations

SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer

1993 • 139 citations

Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli.

1991 • 138 citations

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

1988 • 135 citations

Stepwise Movement of Preproteins in the Process of Translocation across the Cytoplasmic Membrane of Escherichia coli

1995 • 126 citations

SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase

1995 • 125 citations

Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region.

1990 • 115 citations

SecY, SecE, and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase.

1992 • 113 citations

SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimer

1991 • 108 citations

In vitro Analysis of the Process of Translocation of OmpA across the Escherichia coli Cytoplasmic Membrane

1989 • 103 citations

The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids.

1991 • 100 citations

Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide

1989 • 99 citations

A Significant Fraction of Functional SecA Is Permanently Embedded in the Membrane

1996 • 85 citations

Domain Interactions of the Peripheral Preprotein Translocase Subunit SecA

1996 • 73 citations

The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase

1997 • 69 citations

The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.

1993 • 69 citations

Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein Translocase

1996 • 54 citations

The major pathways of protein translocation across membranes

1996 • 33 citations

Protein translocation in Escherichia coli

1994 • 31 citations

The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane

1995 • 29 citations

Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1

1997 • 24 citations

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Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the… (1997) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer