A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane.

No abstract is available for this paper.

• Publication year

  1995

• Venue

  EMBO Journal

• Publication date

  1995-07-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1002/j.1460-2075.1995.tb07342.xPMID 7628437PMCID PMC394403
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  1994cited by this paper
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  1993cited by this paper
• Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli.

  1992cited by this paper
• Vesicle-mediated protein sorting.

  1992cited by this paper
• Export of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli

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  1991cited by this paper
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  1991cited by this paper
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  1990cited by this paper
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  1990cited by this paper
• The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

  1990cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1989cited by this paper
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  1989cited by this paper
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  1989cited by this paper
• A single amino acid determinant of the membrane localization of lipoproteins in E. coli.

  1988influential reference
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  1988cited by this paper
• SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

  1988cited by this paper
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  1988cited by this paper
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  1987cited by this paper
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  1987influential reference
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  1986influential reference
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  1985cited by this paper
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  1985cited by this paper
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  1984influential reference
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  1984cited by this paper
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  1981cited by this paper
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  1981cited by this paper
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  1981cited by this paper
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  1980influential reference
• Translocation and assembly of outer membrance proteins of Escherichia coli. Selective accumulation of precursors and novel assembly intermediates caused by phenethyl alcohol.

  1979cited by this paper
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  1976cited by this paper
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  1975cited by this paper
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  1974cited by this paper
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  1971cited by this paper
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