 Cathepsins
"Cathepsins" 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 group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
| Descriptor ID |
D002403
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| MeSH Number(s) |
D08.811.277.656.224
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Cathepsins".
Below are MeSH descriptors whose meaning is more specific than "Cathepsins".
This graph shows the total number of publications written about "Cathepsins" by people in this website by year, and whether "Cathepsins" 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 |
|---|
| 1988 | 1 | 0 | 1 | | 1989 | 1 | 0 | 1 | | 1990 | 1 | 0 | 1 | | 1991 | 0 | 2 | 2 | | 1993 | 0 | 1 | 1 | | 1994 | 0 | 1 | 1 | | 2001 | 0 | 1 | 1 | | 2002 | 2 | 1 | 3 | | 2003 | 1 | 0 | 1 | | 2006 | 0 | 1 | 1 | | 2007 | 1 | 0 | 1 | | 2010 | 0 | 1 | 1 | | 2013 | 1 | 0 | 1 | | 2014 | 1 | 0 | 1 | | 2015 | 1 | 0 | 1 | | 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Cathepsins" by people in Profiles.
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Han D, Liu J, Chen C, Dong L, Liu Y, Chang R, Huang X, Liu Y, Wang J, Dougherty U, Bissonnette MB, Shen B, Weichselbaum RR, Xu MM, He C. Anti-tumour immunity controlled through mRNA m6A methylation and YTHDF1 in dendritic cells. Nature. 2019 02; 566(7743):270-274.
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Kumar S, Briguglio JS, Turkewitz AP. Secretion of Polypeptide Crystals from Tetrahymena thermophila Secretory Organelles (Mucocysts) Depends on Processing by a Cysteine Cathepsin, Cth4p. Eukaryot Cell. 2015 Aug; 14(8):817-33.
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Kumar S, Briguglio JS, Turkewitz AP. An aspartyl cathepsin, CTH3, is essential for proprotein processing during secretory granule maturation in Tetrahymena thermophila. Mol Biol Cell. 2014 Aug 15; 25(16):2444-60.
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Ingle JN, Liu M, Wickerham DL, Schaid DJ, Wang L, Mushiroda T, Kubo M, Costantino JP, Vogel VG, Paik S, Goetz MP, Ames MM, Jenkins GD, Batzler A, Carlson EE, Flockhart DA, Wolmark N, Nakamura Y, Weinshilboum RM. Selective estrogen receptor modulators and pharmacogenomic variation in ZNF423 regulation of BRCA1 expression: individualized breast cancer prevention. Cancer Discov. 2013 Jul; 3(7):812-25.
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Dawson G, Qin J. Gilenya (FTY720) inhibits acid sphingomyelinase by a mechanism similar to tricyclic antidepressants. Biochem Biophys Res Commun. 2011 Jan 07; 404(1):321-3.
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Tu HC, Ren D, Wang GX, Chen DY, Westergard TD, Kim H, Sasagawa S, Hsieh JJ, Cheng EH. The p53-cathepsin axis cooperates with ROS to activate programmed necrotic death upon DNA damage. Proc Natl Acad Sci U S A. 2009 Jan 27; 106(4):1093-8.
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Keerthivasan S, Keerthivasan G, Mittal S, Chauhan SS. Transcriptional upregulation of human cathepsin L by VEGF in glioblastoma cells. Gene. 2007 Sep 15; 399(2):129-36.
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Röcken C, Fändrich M, Stix B, Tannert A, Hortschansky P, Reinheckel T, Saftig P, Kähne T, Menard R, Ancsin JB, Bühling F. Cathepsin protease activity modulates amyloid load in extracerebral amyloidosis. J Pathol. 2006 Dec; 210(4):478-87.
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Shames DS, Girard L, Gao B, Sato M, Lewis CM, Shivapurkar N, Jiang A, Perou CM, Kim YH, Pollack JR, Fong KM, Lam CL, Wong M, Shyr Y, Nanda R, Olopade OI, Gerald W, Euhus DM, Shay JW, Gazdar AF, Minna JD. A genome-wide screen for promoter methylation in lung cancer identifies novel methylation markers for multiple malignancies. PLoS Med. 2006 Dec; 3(12):e486.
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Dan S, Shirakawa M, Mukai Y, Yoshida Y, Yamazaki K, Kawaguchi T, Matsuura M, Nakamura Y, Yamori T. Identification of candidate predictive markers of anticancer drug sensitivity using a panel of human cancer cell lines. Cancer Sci. 2003 Dec; 94(12):1074-82.
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