 Metalloendopeptidases
"Metalloendopeptidases" 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.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
| Descriptor ID |
D008666
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| MeSH Number(s) |
D08.811.277.656.300.480 D08.811.277.656.675.374
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Metalloendopeptidases".
Below are MeSH descriptors whose meaning is more specific than "Metalloendopeptidases".
This graph shows the total number of publications written about "Metalloendopeptidases" by people in this website by year, and whether "Metalloendopeptidases" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1990 | 3 | 0 | 3 | | 1991 | 1 | 1 | 2 | | 1992 | 1 | 0 | 1 | | 1993 | 2 | 0 | 2 | | 1994 | 0 | 1 | 1 | | 1995 | 1 | 1 | 2 | | 1996 | 0 | 1 | 1 | | 1997 | 2 | 0 | 2 | | 1998 | 2 | 1 | 3 | | 1999 | 2 | 0 | 2 | | 2000 | 0 | 1 | 1 | | 2001 | 1 | 1 | 2 | | 2002 | 1 | 1 | 2 | | 2003 | 2 | 0 | 2 | | 2004 | 1 | 1 | 2 | | 2005 | 1 | 0 | 1 | | 2006 | 2 | 1 | 3 | | 2007 | 0 | 1 | 1 | | 2011 | 0 | 1 | 1 | | 2013 | 1 | 0 | 1 | | 2014 | 1 | 0 | 1 | | 2015 | 1 | 0 | 1 | | 2016 | 2 | 0 | 2 | | 2017 | 0 | 1 | 1 | | 2018 | 2 | 0 | 2 | | 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Metalloendopeptidases" by people in Profiles.
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Caminero A, McCarville JL, Galipeau HJ, Deraison C, Bernier SP, Constante M, Rolland C, Meisel M, Murray JA, Yu XB, Alaedini A, Coombes BK, Bercik P, Southward CM, Ruf W, Jabri B, Chirdo FG, Casqueiro J, Surette MG, Vergnolle N, Verdu EF. Duodenal bacterial proteolytic activity determines sensitivity to dietary antigen through protease-activated receptor-2. Nat Commun. 2019 03 13; 10(1):1198.
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Park MH, Zhong R, Lamppa G. Chloroplast stromal processing peptidase activity is modulated by transit peptide determinants that include inhibitory roles for its N-terminal domain and initial Met. Biochem Biophys Res Commun. 2018 09 18; 503(4):3149-3154.
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Kayatekin C, Amasino A, Gaglia G, Flannick J, Bonner JM, Fanning S, Narayan P, Barrasa MI, Pincus D, Landgraf D, Nelson J, Hesse WR, Costanzo M. Translocon Declogger Ste24 Protects against IAPP Oligomer-Induced Proteotoxicity. Cell. 2018 03 22; 173(1):62-73.e9.
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Cohen JE, Wang R, Shen RF, Wu WW, Keller JE. Comparative pathogenomics of Clostridium tetani. PLoS One. 2017; 12(8):e0182909.
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Herrou J, Choi VM, Bubeck Wardenburg J, Crosson S. Activation Mechanism of the Bacteroides fragilis Cysteine Peptidase, Fragipain. Biochemistry. 2016 07 26; 55(29):4077-84.
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Choi VM, Herrou J, Hecht AL, Teoh WP, Turner JR, Crosson S, Bubeck Wardenburg J. Activation of Bacteroides fragilis toxin by a novel bacterial protease contributes to anaerobic sepsis in mice. Nat Med. 2016 05; 22(5):563-7.
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Gomez CM, Kawakami H. Neurogenetics: The expanding horizons of diagnosis and disease pathogenesis. Neurology. 2015 Mar 17; 84(11):1070-1.
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Hines CS, Ray K, Schmidt JJ, Xiong F, Feenstra RW, Pras-Raves M, de Moes JP, Lange JH, Melikishvili M, Fried MG, Mortenson P, Charlton M, Patel Y, Courtney SM, Kruse CG, Rodgers DW. Allosteric inhibition of the neuropeptidase neurolysin. J Biol Chem. 2014 Dec 19; 289(51):35605-19.
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Peng YJ, Nanduri J, Raghuraman G, Wang N, Kumar GK, Prabhakar NR. Role of oxidative stress-induced endothelin-converting enzyme activity in the alteration of carotid body function by chronic intermittent hypoxia. Exp Physiol. 2013 Nov; 98(11):1620-30.
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Le Berre R, Nguyen S, Nowak E, Kipnis E, Pierre M, Quenee L, Ader F, Lancel S, Courcol R, Guery BP, Faure K. Relative contribution of three main virulence factors in Pseudomonas aeruginosa pneumonia. Crit Care Med. 2011 Sep; 39(9):2113-20.
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