 Enzyme Assays
"Enzyme Assays" 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.
Methods used to measure the relative activity of a specific enzyme or its concentration in solution. Typically an enzyme substrate is added to a buffer solution containing enzyme and the rate of conversion of substrate to product is measured under controlled conditions. Many classical enzymatic assay methods involve the use of synthetic colorimetric substrates and measuring the reaction rates using a spectrophotometer.
| Descriptor ID |
D057075
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| MeSH Number(s) |
E05.196.427
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| Concept/Terms |
Enzyme Assays- Enzyme Assays
- Assay, Enzyme
- Assays, Enzyme
- Enzyme Assay
- Enzymatic Assays
- Assay, Enzymatic
- Assays, Enzymatic
- Enzymatic Assay
Indirect Enzyme Assays- Indirect Enzyme Assays
- Assay, Indirect Enzyme
- Assays, Indirect Enzyme
- Enzyme Assay, Indirect
- Enzyme Assays, Indirect
- Indirect Enzyme Assay
- Indirect Enzymatic Assays
- Assay, Indirect Enzymatic
- Assays, Indirect Enzymatic
- Enzymatic Assay, Indirect
- Enzymatic Assays, Indirect
- Indirect Enzymatic Assay
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Below are MeSH descriptors whose meaning is more general than "Enzyme Assays".
Below are MeSH descriptors whose meaning is more specific than "Enzyme Assays".
This graph shows the total number of publications written about "Enzyme Assays" by people in this website by year, and whether "Enzyme Assays" 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 |
|---|
| 2009 | 1 | 0 | 1 | | 2010 | 2 | 0 | 2 | | 2012 | 1 | 0 | 1 | | 2013 | 0 | 1 | 1 | | 2014 | 0 | 1 | 1 | | 2016 | 1 | 0 | 1 | | 2017 | 2 | 0 | 2 | | 2018 | 1 | 2 | 3 | | 2019 | 2 | 0 | 2 |
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Below are the most recent publications written about "Enzyme Assays" by people in Profiles.
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Zhai L, Ladomersky E, Bell A, Dussold C, Cardoza K, Qian J, Lauing KL, Wainwright DA. Quantification of IDO1 enzyme activity in normal and malignant tissues. Methods Enzymol. 2019; 629:235-256.
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Li G, Moellering RE. Chemical probes for spatially resolved measurement of active enzymes in single cells. Methods Enzymol. 2019; 628:243-262.
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Park MJ, Shen H, Kim NH, Gao F, Failor C, Knudtson JF, McLaughlin J, Halder SK, Heikkinen TA, Vahteristo P, Al-Hendy A, Schenken RS, Boyer TG. Mediator Kinase Disruption in MED12-Mutant Uterine Fibroids From Hispanic Women of South Texas. J Clin Endocrinol Metab. 2018 11 01; 103(11):4283-4292.
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Ou Y, Wilson RE, Weber SG. Methods of Measuring Enzyme Activity Ex Vivo and In Vivo. Annu Rev Anal Chem (Palo Alto Calif). 2018 06 12; 11(1):509-533.
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Kar UP, Dey H, Rahaman A. Tetrahymena dynamin-related protein 6 self-assembles independent of membrane association. J Biosci. 2018 Mar; 43(1):139-148.
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Li G, Montgomery JE, Eckert MA, Chang JW, Tienda SM, Lengyel E, Moellering RE. An activity-dependent proximity ligation platform for spatially resolved quantification of active enzymes in single cells. Nat Commun. 2017 11 24; 8(1):1775.
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Harris ME, York DM, Piccirilli JA, Anderson VE. Kinetic Isotope Effect Analysis of RNA 2'-O-Transphosphorylation. Methods Enzymol. 2017; 596:433-457.
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Duckworth BP, Wilson DJ, Aldrich CC. Measurement of Nonribosomal Peptide Synthetase Adenylation Domain Activity Using a Continuous Hydroxylamine Release Assay. Methods Mol Biol. 2016; 1401:53-61.
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Wagner SL, Zhang C, Cheng S, Nguyen P, Zhang X, Rynearson KD, Wang R, Li Y, Sisodia SS, Mobley WC, Tanzi RE. Soluble ?-secretase modulators selectively inhibit the production of the 42-amino acid amyloid ß peptide variant and augment the production of multiple carboxy-truncated amyloid ß species. Biochemistry. 2014 Feb 04; 53(4):702-13.
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Huynh T, Sun B, Li L, Nichols KP, Koyner JL, Ismagilov RF. Chemical analog-to-digital signal conversion based on robust threshold chemistry and its evaluation in the context of microfluidics-based quantitative assays. J Am Chem Soc. 2013 Oct 02; 135(39):14775-83.
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