 Micrococcal Nuclease
"Micrococcal Nuclease" 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.
An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1.
| Descriptor ID |
D008836
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| MeSH Number(s) |
D08.811.277.352.335.350.500 D08.811.277.352.355.325.500 D08.811.277.352.355.350.500 D08.811.277.352.700.350.500
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| Concept/Terms |
Micrococcal Nuclease- Micrococcal Nuclease
- Nuclease, Micrococcal
- TNase
- Thermostable Nuclease
- Nuclease, Thermostable
- Staphylococcal Nuclease
- Nuclease, Staphylococcal
- Thermonuclease
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Below are MeSH descriptors whose meaning is more general than "Micrococcal Nuclease".
Below are MeSH descriptors whose meaning is more specific than "Micrococcal Nuclease".
This graph shows the total number of publications written about "Micrococcal Nuclease" by people in this website by year, and whether "Micrococcal Nuclease" 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 |
|---|
| 2006 | 1 | 0 | 1 | | 2008 | 1 | 0 | 1 | | 2009 | 0 | 1 | 1 | | 2010 | 1 | 0 | 1 | | 2011 | 1 | 0 | 1 | | 2013 | 1 | 0 | 1 | | 2014 | 1 | 2 | 3 | | 2017 | 0 | 2 | 2 | | 2021 | 1 | 1 | 2 |
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Below are the most recent publications written about "Micrococcal Nuclease" by people in Profiles.
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Rao S, Ahmad K, Ramachandran S. Cooperative binding between distant transcription factors is a hallmark of active enhancers. Mol Cell. 2021 04 15; 81(8):1651-1665.e4.
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Wiemels RE, Keogh RA, Carroll RK. Detection and Quantification of Secreted Nuclease Activity in Staphylococcus aureus Culture Supernatants. Methods Mol Biol. 2021; 2341:17-24.
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Ramachandran S, Ahmad K, Henikoff S. Transcription and Remodeling Produce Asymmetrically Unwrapped Nucleosomal Intermediates. Mol Cell. 2017 12 21; 68(6):1038-1053.e4.
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Flenker KS, Burghardt EL, Dutta N, Burns WJ, Grover JM, Kenkel EJ, Weaver TM, Mills J, Kim H, Huang L, Owczarzy R, Musselman CA, Behlke MA, Ford B, McNamara JO. Rapid Detection of Urinary Tract Infections via Bacterial Nuclease Activity. Mol Ther. 2017 06 07; 25(6):1353-1362.
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Ramachandran S, Zentner GE, Henikoff S. Asymmetric nucleosomes flank promoters in the budding yeast genome. Genome Res. 2015 Mar; 25(3):381-90.
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Moormeier DE, Bose JL, Horswill AR, Bayles KW. Temporal and stochastic control of Staphylococcus aureus biofilm development. mBio. 2014 Oct 14; 5(5):e01341-14.
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Hernandez FJ, Huang L, Olson ME, Powers KM, Hernandez LI, Meyerholz DK, Thedens DR, Behlke MA, Horswill AR, McNamara JO. Noninvasive imaging of Staphylococcus aureus infections with a nuclease-activated probe. Nat Med. 2014 Mar; 20(3):301-6.
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Olson ME, Nygaard TK, Ackermann L, Watkins RL, Zurek OW, Pallister KB, Griffith S, Kiedrowski MR, Flack CE, Kavanaugh JS, Kreiswirth BN, Horswill AR, Voyich JM. Staphylococcus aureus nuclease is an SaeRS-dependent virulence factor. Infect Immun. 2013 Apr; 81(4):1316-24.
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Kiedrowski MR, Kavanaugh JS, Malone CL, Mootz JM, Voyich JM, Smeltzer MS, Bayles KW, Horswill AR. Nuclease modulates biofilm formation in community-associated methicillin-resistant Staphylococcus aureus. PLoS One. 2011; 6(11):e26714.
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Berends ET, Horswill AR, Haste NM, Monestier M, Nizet V, von K?ckritz-Blickwede M. Nuclease expression by Staphylococcus aureus facilitates escape from neutrophil extracellular traps. J Innate Immun. 2010; 2(6):576-86.
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