Proteases in Escherichia coli.

No abstract is available for this paper.

• Publication year

  1993

• Venue

  Methods in Enzymology

• Publication date

  1993-10-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1126/SCIENCE.8211156PMID 7043205
• 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.

• Proteases in Escherichia coli.

  1993cited by this paper
• Isolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits.

  1983cited by this paper
• Mechanisms of intracellular protein breakdown.

  1982cited by this paper
• Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion.

  1982cited by this paper
• ATP-stimulated endoprotease is associated with the cell membrane of E. coli

  1981cited by this paper
• E. coli contains eight soluble proteolytic activities, one being ATP dependent

  1981cited by this paper
• The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La.

  1981cited by this paper
• Identification of protease IV of E, coli.

  1981cited by this paper
• ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12.

  1981cited by this paper
• The purification of protease IV of E. coli and the demonstration that it is an endoproteolytic enzyme.

  1981cited by this paper
• Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes.

  1980cited by this paper
• Purification and characterization of leader (signal) peptidase from Escherichia coli.

  1980cited by this paper
• ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.

  1980cited by this paper
• The mechanism of protein secretion across membranes

  1980cited by this paper
• The genetics of protein degradation in bacteria.

  1980cited by this paper
• Cleavage of the Escherichia coli lexA protein by the recA protease.

  1980cited by this paper
• Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis.

  1980cited by this paper
• Control of protein degradation in reticulocytes and reticulocyte extracts by hemin.

  1980cited by this paper
• Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes.

  1980cited by this paper
• Processing of alkaline phosphatase precursor to the mature enzyme by an Escherichia coli inner membrane preparation

  1980cited by this paper
• E. coli recA protein-directed cleavage of phage lambda repressor requires polynucleotide.

  1980cited by this paper
• Purification and characterization of protease III from Escherichia coli.

  1979cited by this paper
• The assembly of proteins into biological membranes: The membrane trigger hypothesis.

  1979cited by this paper
• Protein degradation is stimulated by ATP in extracts of Escherichia coli.

  1979cited by this paper
• Isolation and characterization of mutations in the structural gene for protease III (ptr)

  1979cited by this paper
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  1979cited by this paper
• The study of Escherichia coli proteases. Intracellular serine protease of E. coli-an analogue of bacillus proteases.

  1979cited by this paper
• Identification and partial purification of an ATP-stimulated alkaline protease in rat liver.

  1979cited by this paper
• Escherichia coli recA gene product inactivates phage lambda repressor.

  1978cited by this paper
• Peptidase-deficient mutants of Escherichia coli

  1978cited by this paper
• Deg phenotype of Escherichia coli lon mutants

  1978cited by this paper
• A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes.

  1977cited by this paper
• Intracellular protein degradation in mammalian and bacterial cells: Part 2.

  1976cited by this paper
• Protease I from Escherichia coli. Some physicochemical properties and substrate specificity.

  1976cited by this paper
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  1976cited by this paper
• Purification and properties of a new aminopeptidase from Escherichia COLI K12.

  1976cited by this paper
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  1975cited by this paper
• Properties of a cytoplasmic proteolytic enzyme from Escherichia coli.

  1975cited by this paper
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  1975cited by this paper
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  1975cited by this paper
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  1975cited by this paper
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  1975cited by this paper
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  1974cited by this paper
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  1973cited by this paper
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  1973cited by this paper
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  1973cited by this paper
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  1973cited by this paper
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  1973cited by this paper
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  1972cited by this paper
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  1972cited by this paper
• Radioactive labeling of proteins in vitro.

  1971cited by this paper
• Isolation and some propeties of a proteolytic enzyme from Escherichia coli (protease I).

  1971cited by this paper
• Peptide transport and metabolism in bacteria.

  1971cited by this paper
• Purification and properties of an aminopeptidase from Escherichia coli.

  1970cited by this paper
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  1968cited by this paper
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  1968cited by this paper
• Purification and properties of a ribosomal peptidase from Escherichia coli B.

  1965cited by this paper
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  1962cited by this paper
• The intracellular turnover of protein and nucleic acids and its role in biochemical differentiation.

  1960cited by this paper
• Cleavage of the haem-protein link by acid methylethylketone.

  1959cited by this paper

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  2011cites this paper
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  2008cites this paper
• Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase.

  2007cites this paper
• Energetics of Substrate Unfolding by ClpA

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• Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors.

  2007cites this paper
• Intracellular proteolysis: Signals of selective protein degradation

  2007cites this paper
• Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli.

  2006cites this paper
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  2006cites this paper
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  2005cites this paper
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  2005cites this paper
• The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site*

  2004cites this paper
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  2004cites this paper
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  2004cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2002cites this paper
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  2002cites this paper
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  2002cites this paper
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  2002cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2000cites this paper
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  2000cites this paper
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  2000cites this paper
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  2000cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1997cites this paper
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  1997cites this paper
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  1997cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996influential citation
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  1996cites this paper
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  1996cites this paper
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  1995cites this paper
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  1995cites this paper
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  1995cites this paper
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  1995cites this paper
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  1995cites this paper
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  1995cites this paper
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  1994cites this paper
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  1994cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1992influential citation
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper