 Catalytic Domain
"Catalytic Domain" 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.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
| Descriptor ID |
D020134
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| MeSH Number(s) |
G02.111.570.120.704 G02.111.570.790.709.610.189
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| Concept/Terms |
Catalytic Domain- Catalytic Domain
- Catalytic Domains
- Domain, Catalytic
- Domains, Catalytic
- Catalytic Region
- Catalytic Regions
- Region, Catalytic
- Regions, Catalytic
- Catalytic Subunit
- Catalytic Subunits
- Subunit, Catalytic
- Subunits, Catalytic
- Catalytic Core
- Catalytic Cores
- Core, Catalytic
- Cores, Catalytic
Active Site- Active Site
- Active Sites
- Site, Active
- Sites, Active
- Reactive Site
- Reactive Sites
- Site, Reactive
- Sites, Reactive
- Catalytic Site
- Catalytic Sites
- Site, Catalytic
- Sites, Catalytic
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Below are MeSH descriptors whose meaning is more general than "Catalytic Domain".
Below are MeSH descriptors whose meaning is more specific than "Catalytic Domain".
This graph shows the total number of publications written about "Catalytic Domain" by people in UAMS Profiles by year, and whether "Catalytic Domain" 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 |
|---|
| 2021 | 0 | 2 | 2 | | 2020 | 0 | 1 | 1 | | 2018 | 0 | 3 | 3 | | 2017 | 0 | 1 | 1 | | 2016 | 0 | 2 | 2 | | 2015 | 0 | 2 | 2 | | 2014 | 0 | 1 | 1 | | 2013 | 0 | 1 | 1 | | 2012 | 0 | 1 | 1 | | 2010 | 1 | 0 | 1 | | 2009 | 0 | 3 | 3 | | 2008 | 1 | 0 | 1 | | 2006 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2002 | 0 | 1 | 1 | | 2001 | 1 | 0 | 1 | | 2000 | 0 | 1 | 1 | | 1999 | 0 | 1 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Catalytic Domain" by people in Profiles over the past ten years.
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Xie SC, Metcalfe RD, Mizutani H, Puhalovich T, Hanssen E, Morton CJ, Du Y, Dogovski C, Huang SC, Ciavarri J, Hales P, Griffin RJ, Cohen LH, Chuang BC, Wittlin S, Deni I, Yeo T, Ward KE, Barry DC, Liu B, Gillett DL, Crespo-Fernandez BF, Ottilie S, Mittal N, Churchyard A, Ferguson D, Aguiar ACC, Guido RVC, Baum J, Hanson KK, Winzeler EA, Gamo FJ, Fidock DA, Baud D, Parker MW, Brand S, Dick LR, Griffin MDW, Gould AE, Tilley L. Design of proteasome inhibitors with oral efficacy in vivo against Plasmodium falciparum and selectivity over the human proteasome. Proc Natl Acad Sci U S A. 2021 09 28; 118(39).
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Brosey CA, Houl JH, Katsonis P, Balapiti-Modarage LPF, Bommagani S, Arvai A, Moiani D, Bacolla A, Link T, Warden LS, Lichtarge O, Jones DE, Ahmed Z, Tainer JA. Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors. Prog Biophys Mol Biol. 2021 08; 163:171-186.
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Balasubramaniam M, Mainali N, Bowroju SK, Atluri P, Penthala NR, Ayyadevera S, Crooks PA, Shmookler Reis RJ. Structural modeling of GSK3? implicates the inactive (DFG-out) conformation as the target bound by TDZD analogs. Sci Rep. 2020 10 27; 10(1):18326.
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Yan W, Lakkaniga NR, Carlomagno F, Santoro M, McDonald NQ, Lv F, Gunaganti N, Frett B, Li HY. Insights into Current Tropomyosin Receptor Kinase (TRK) Inhibitors: Development and Clinical Application. J Med Chem. 2019 02 28; 62(4):1731-1760.
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Prakash D, Walters KA, Martinie RJ, McCarver AC, Kumar AK, Lessner DJ, Krebs C, Golbeck JH, Ferry JG. Toward a mechanistic and physiological understanding of a ferredoxin:disulfide reductase from the domains Archaea and Bacteria. J Biol Chem. 2018 06 15; 293(24):9198-9209.
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Gokulan K, Khare S, Cerniglia CE, Foley SL, Varughese KI. Structure and Inhibitor Specificity of L,D-Transpeptidase (LdtMt2) from Mycobacterium tuberculosis and Antibiotic Resistance: Calcium Binding Promotes Dimer Formation. AAPS J. 2018 03 09; 20(2):44.
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Shwab EK, Juvvadi PR, Waitt G, Soderblom EJ, Moseley MA, Nicely NI, Asfaw YG, Steinbach WJ. A Novel Phosphoregulatory Switch Controls the Activity and Function of the Major Catalytic Subunit of Protein Kinase A in Aspergillus fumigatus. mBio. 2017 02 07; 8(1).
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Choudhury SR, Cui Y, Lubecka K, Stefanska B, Irudayaraj J. CRISPR-dCas9 mediated TET1 targeting for selective DNA demethylation at BRCA1 promoter. Oncotarget. 2016 Jul 19; 7(29):46545-46556.
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Culbertson AT, Tietze AA, Tietze D, Chou YH, Smith AL, Young ZT, Zabotina OA. A homology model of Xyloglucan Xylosyltransferase 2 reveals critical amino acids involved in substrate binding. Glycobiology. 2016 09; 26(9):961-972.
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Ferdaoussi M, Dai X, Jensen MV, Wang R, Peterson BS, Huang C, Ilkayeva O, Smith N, Miller N, Hajmrle C, Spigelman AF, Wright RC, Plummer G, Suzuki K, Mackay JP, van de Bunt M, Gloyn AL, Ryan TE, Norquay LD, Brosnan MJ, Trimmer JK, Rolph TP, Kibbey RG, Manning Fox JE, Colmers WF, Shirihai OS, Neufer PD, Yeh ET, Newgard CB, MacDonald PE. Isocitrate-to-SENP1 signaling amplifies insulin secretion and rescues dysfunctional ? cells. J Clin Invest. 2015 Oct 01; 125(10):3847-60.
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