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ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.
EMBO J. 1988 Jun;7(6):1831-5
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Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.
Proc Natl Acad Sci U S A. 1988 Dec;85(23):8978-82
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SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.
EMBO J. 1989 Mar;8(3):955-9
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SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
EMBO J. 1989 Mar;8(3):961-6
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The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.
Cell. 1990 Aug 24;62(4):649-57
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The sec and prl genes of Escherichia coli.
J Bioenerg Biomembr. 1990 Jun;22(3):291-310
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The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.
Cell. 1990 Oct 19;63(2):269-79
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The secD locus of E.coli codes for two membrane proteins required for protein export.
EMBO J. 1990 Oct;9(10):3209-16
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Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase.
Cell. 1991 Mar 8;64(5):927-39
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Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.
Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6545-9
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SecY, SecE, and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase.
J Biol Chem. 1992 Feb 25;267(6):4166-70
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Sec61p and BiP directly facilitate polypeptide translocation into the ER.
Cell. 1992 Apr 17;69(2):353-65
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Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli.
Biochim Biophys Acta. 1992 Jul 13;1122(1):77-84
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Suppressor analysis suggests a multistep, cyclic mechanism for protein secretion in Escherichia coli.
EMBO J. 1992 Sep;11(9):3165-74
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SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli.
EMBO J. 1993 Jan;12(1):265-70
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Purified Escherichia coli preprotein translocase catalyzes multiple cycles of precursor protein translocation.
Biochemistry. 1993 Mar 16;32(10):2626-30
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The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.
Genetics. 1993 Apr;133(4):763-73
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A tetrameric complex of membrane proteins in the endoplasmic reticulum.
Eur J Biochem. 1993 Jun 1;214(2):375-81
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Genetic and molecular characterization of the Escherichia coli secD operon and its products.
J Bacteriol. 1994 Feb;176(3):804-14
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SecD and SecF facilitate protein export in Escherichia coli.
EMBO J. 1994 Feb 1;13(3):554-61
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Evolutionary conservation of components of the protein translocation complex.
Nature. 1994 Feb 17;367(6464):654-7
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SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation.
EMBO J. 1994 Feb 15;13(4):954-63
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Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes.
Mol Gen Genet. 1994 May 10;243(3):261-9
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Subunit dynamics in Escherichia coli preprotein translocase.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):4703-7
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SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane.
J Bacteriol. 1994 Jul;176(13):4111-6
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Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature.
EMBO J. 1994 Jul 15;13(14):3272-7
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Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.
J Cell Biol. 1994 Aug;126(4):935-43
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SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.
Cell. 1994 Sep 9;78(5):835-43
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SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state.
Cell. 1994 Sep 9;78(5):845-53
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Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12).
J Biol Chem. 1994 Sep 23;269(38):23625-31
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A double counter-selection system for the study of null alleles of essential genes in Escherichia coli.
Gene. 1995 Mar 21;155(1):1-7
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High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.
Trends Biochem Sci. 1995 Feb;20(2):65-9
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Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.
Cell. 1995 May 19;81(4):561-70
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The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system.
Cell. 1995 Jun 30;81(7):1085-93
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Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.
J Bacteriol. 1995 Jul;177(14):4121-30
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SecYEG and SecA are the stoichiometric components of preprotein translocase.
J Biol Chem. 1995 Aug 25;270(34):20106-11
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A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery.
EMBO J. 1995 Sep 15;14(18):4412-21
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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.
Cell. 1995 Dec 29;83(7):1171-81
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Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation.
Cell. 1996 Apr 5;85(1):71-81
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SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature.
FEBS Lett. 1996 Feb 26;381(1-2):25-8
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In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery.
J Biol Chem. 1996 Aug 16;271(33):19908-14
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Separable ATPase and membrane insertion domains of the SecA subunit of preprotein translocase.
J Biol Chem. 1996 Dec 6;271(49):31580-4
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Regulation of a membrane component required for protein secretion in Escherichia coli.
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