DNA Restriction-Modification Enzymes
"DNA Restriction-Modification Enzymes" 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.
Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues in the same target sequence that constitutes the restriction enzyme binding site. The methylation renders the target site resistant to restriction, thereby protecting DNA against cleavage.
Descriptor ID |
D015280
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MeSH Number(s) |
D08.811.150
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Concept/Terms |
DNA Restriction-Modification Enzymes- DNA Restriction-Modification Enzymes
- Enzymes, DNA Restriction-Modification
- Restriction-Modification Enzymes, DNA
- Restriction-Modification Systems
- Systems, Restriction-Modification
- Restriction Modification Systems
- Modification Systems, Restriction
- Systems, Restriction Modification
- DNA Restriction Modification Enzymes
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Below are MeSH descriptors whose meaning is more general than "DNA Restriction-Modification Enzymes".
Below are MeSH descriptors whose meaning is more specific than "DNA Restriction-Modification Enzymes".
This graph shows the total number of publications written about "DNA Restriction-Modification Enzymes" by people in this website by year, and whether "DNA Restriction-Modification Enzymes" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "DNA Restriction-Modification Enzymes" by people in Profiles.
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Analysis of a phase-variable restriction modification system of the human gut symbiont Bacteroides fragilis. Nucleic Acids Res. 2020 11 04; 48(19):11040-11053.
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Isolation of a Legionella pneumophila restriction mutant with increased ability to act as a recipient in heterospecific matings. J Bacteriol. 1989 Apr; 171(4):2238-40.