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Structural analysis of point mutations at the Vaccinia virus A20/D4 interface
The Vaccinia virus polymerase holoenzyme is composed of three subunits: E9, the catalytic DNA polymerase subunit; D4, a uracil-DNA glycosylase; and A20, a protein with no known enzymatic activity. The D4/A20 heterodimer is the DNA polymerase cofactor, the function of which is essential for processiv...
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| Foilsithe in: | Acta Crystallogr F Struct Biol Commun |
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| Main Authors: | , , , , , |
| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
International Union of Crystallography
2016
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5012208/ https://ncbi.nlm.nih.gov/pubmed/27599859 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X16011778 |
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