"Chymotrypsin" 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.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
| Descriptor ID |
D002918
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| MeSH Number(s) |
D08.811.277.656.300.760.176 D08.811.277.656.959.350.176
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Chymotrypsin".
Below are MeSH descriptors whose meaning is more specific than "Chymotrypsin".
This graph shows the total number of publications written about "Chymotrypsin" by people in this website by year, and whether "Chymotrypsin" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 |
| 2017 | 2 | 1 | 3 |
| 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Chymotrypsin" by people in Profiles.
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Evaluation of the Pathogenic Significance of the Novel p.T58M Chymotrypsin C Variant in Recurrent Acute Pancreatitis. Pancreas. 2019 02; 48(2):e12-e14.
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Novel PRSS1 Mutation p.P17T Validates Pathogenic Relevance of CTRC-Mediated Processing of the Trypsinogen Activation Peptide in Chronic Pancreatitis. Am J Gastroenterol. 2017 12; 112(12):1896-1898.
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Genome-wide association study identifies inversion in the CTRB1-CTRB2 locus to modify risk for alcoholic and non-alcoholic chronic pancreatitis. Gut. 2018 10; 67(10):1855-1863.
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Transfer Zymography. Methods Mol Biol. 2017; 1626:253-269.
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Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease. J Biochem. 2010 Sep; 148(3):349-58.
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Synthesis and evaluation of isatin derivatives as effective SARS coronavirus 3CL protease inhibitors. Bioorg Med Chem Lett. 2005 Jun 15; 15(12):3058-62.
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Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease. J Biol Chem. 2005 Jun 17; 280(24):22741-8.
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Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors. J Biol Chem. 2004 Jun 04; 279(23):24765-73.
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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. EMBO J. 2002 Jul 01; 21(13):3213-24.
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Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: identification of proteolytic products and cleavage sites common to pp1a and pp1ab. J Virol. 1999 Jan; 73(1):177-85.