Enteropeptidase

"Enteropeptidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

A specialized proteolytic enzyme secreted by intestinal cells. It converts TRYPSINOGEN into its active form TRYPSIN by removing the N-terminal peptide. EC 3.4.21.9.

Descriptor ID

D004765

MeSH Number(s)

D08.811.277.656.300.760.284

D08.811.277.656.959.350.284

Concept/Terms

Enteropeptidase

Below are MeSH descriptors whose meaning is more general than "Enteropeptidase".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Hydrolases [D08.811.277]
Peptide Hydrolases [D08.811.277.656]
Endopeptidases [D08.811.277.656.300]
Serine Endopeptidases [D08.811.277.656.300.760]
Enteropeptidase [D08.811.277.656.300.760.284]
Serine Proteases [D08.811.277.656.959]
Serine Endopeptidases [D08.811.277.656.959.350]
Enteropeptidase [D08.811.277.656.959.350.284]

Below are MeSH descriptors whose meaning is more specific than "Enteropeptidase".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Enteropeptidase" by people in Harvard Catalyst Profiles by year, and whether "Enteropeptidase" was a major or minor topic of these publication.

Bar chart showing 7 publications over 6 distinct years, with a maximum of 2 publications in 1999

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1994	0	1	1
1995	1	0	1
1998	0	1	1
1999	0	2	2
2000	0	1	1
2015	0	1	1

Below are the most recent publications written about "Enteropeptidase" by people in Profiles.

A High Yield and Cost-efficient Expression System of Human Granzymes in Mammalian Cells. J Vis Exp. 2015 Jun 10; (100):e52911.

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A study of conformational restraints on reactivity of human PR3-specific autoantibodies (ANCA) facilitated through protein folding manipulations of a new recombinant proteinase 3 protein. Autoimmunity. 2007 Nov; 40(7):503-11.

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Large scale production of recombinant antibodies by utilizing cellulose-binding domains. Methods Mol Biol. 2003; 207:443-54.

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Formation of enzymatically active, homotypic, and heterotypic tetramers of mouse mast cell tryptases. Dependence on a conserved Trp-rich domain on the surface. J Biol Chem. 2000 Jan 07; 275(1):351-8.

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Trypsin and activation of circulating trypsinogen contribute to pancreatitis-associated lung injury. Am J Physiol. 1999 11; 277(5):G1008-16.

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Interstitial trypsinogen release and its relevance to the transformation of mild into necrotizing pancreatitis in rats. Gastroenterology. 1999 Sep; 117(3):717-25.

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Induction of a selective and persistent extravasation of neutrophils into the peritoneal cavity by tryptase mouse mast cell protease 6. J Immunol. 1998 Feb 15; 160(4):1910-9.

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Quantitative assay of trypsinogen by measurement of cleaved activation peptide after activation with enterokinase. Anal Biochem. 1995 Sep 20; 230(2):348-50.

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Interstitial protease activation is the central event in progression to necrotizing pancreatitis. Surgery. 1994 Sep; 116(3):497-504.

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The cloned platelet thrombin receptor couples to at least two distinct effectors to stimulate phosphoinositide hydrolysis and inhibit adenylyl cyclase. J Biol Chem. 1992 Oct 15; 267(29):20831-4.

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