Recombinant pro-regions from papain and papaya proteinase IV-are selective high affinity inhibitors of the mature papaya enzymes.

No abstract is available for this paper.

• Publication year

  1995

• Venue

  Protein Engineering

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1093/PROTEIN/8.1.59PMID 7770454
• 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.

• The proregion of cathepsin L is required for proper folding, stability, and ER exit.

  1994cited by this paper
• Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in

  1994cited by this paper
• Nucleotide sequence and expression in Escherichia coli of cDNAs encoding papaya proteinase omega from Carica papaya.

  1993cited by this paper
• Two distinct gene subfamilies within the family of cysteine protease genes.

  1993cited by this paper
• Protein folding in the cell

  1992cited by this paper
• Active papain renatured and processed from insoluble recombinant propapain expressed in Escherichia coli.

  1992cited by this paper
• Protease pro region required for folding is a potent inhibitor of the mature enzyme

  1992cited by this paper
• Potent slow-binding inhibition of cathepsin B by its propeptide.

  1992cited by this paper
• Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.

  1991cited by this paper
• Interactions of papaya proteinase IV with inhibitors

  1990cited by this paper
• Use of T7 RNA polymerase to direct expression of cloned genes.

  1990cited by this paper
• Secretion of functional papain precursor from insect cells. Requirement for N-glycosylation of the pro-region.

  1990cited by this paper
• Synthesis of papain in Escherichia coli.

  1990cited by this paper
• Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli.

  1989cited by this paper
• Papaya proteinase IV amino acid sequence

  1989cited by this paper
• Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process

  1989cited by this paper
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  1988cited by this paper
• Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.

  1987cited by this paper
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  1986cited by this paper
• Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

  1986cited by this paper
• Cathepsin B, Cathepsin H, and cathepsin L.

  1981cited by this paper
• Human cathepsin B1. Purification and some properties of the enzyme.

  1973cited by this paper
• On the size of the active site in proteases. I. Papain.

  1967cited by this paper

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  2011cites this paper
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  2011cites this paper
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  2011cites this paper
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  2003cites this paper
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  2002influential citation
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