"Bacteriophage T4" 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.
Virulent bacteriophage and type species of the genus T4-like phages, in the family MYOVIRIDAE. It infects E. coli and is the best known of the T-even phages. Its virion contains linear double-stranded DNA, terminally redundant and circularly permuted.
| Descriptor ID |
D017122
|
| MeSH Number(s) |
B04.123.150.500.350 B04.123.205.891.200 B04.280.090.500.350
|
| Concept/Terms |
Bacteriophage T4- Bacteriophage T4
- T4 Phage
- Phage, T4
- Phages, T4
- T4 Phages
- Enterobacteria phage T4
- Coliphage T4
- Phage T4
Bacteriophage T2- Bacteriophage T2
- Enterobacteria phage T2
- T2, Enterobacteria phage
- T2 Phage
- Phage, T2
- Phages, T2
- T2 Phages
- Coliphage T2
- Phage T2
|
Below are MeSH descriptors whose meaning is more general than "Bacteriophage T4".
Below are MeSH descriptors whose meaning is more specific than "Bacteriophage T4".
This graph shows the total number of publications written about "Bacteriophage T4" by people in this website by year, and whether "Bacteriophage T4" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1997 | 0 | 1 | 1 |
| 2003 | 2 | 0 | 2 |
| 2004 | 1 | 1 | 2 |
| 2009 | 2 | 0 | 2 |
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Below are the most recent publications written about "Bacteriophage T4" by people in Profiles.
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Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. Protein Sci. 2009 May; 18(5):871-80.
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Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Protein Sci. 2009 May; 18(5):863-70.
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Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods. Acta Crystallogr D Biol Crystallogr. 2004 Oct; 60(Pt 10):1726-37.
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Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry. 2004 Feb 10; 43(5):1296-301.
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Repacking the Core of T4 lysozyme by automated design. J Mol Biol. 2003 Sep 19; 332(3):741-56.
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Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Biophys Chem. 2003; 100(1-3):325-40.
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Efficient 5' end labeling of dephosphorylated DNA. Anal Biochem. 1997 Feb 15; 245(2):123-6.