Výsledky vyhledávání

Biochemical characterization of human DNA polymerase iota provides clues to its biological function

Autor: A, Tissier, E G, Frank, J P, McDonald, A, Vaisman, A R, Fernàndez de Henestrosa, F, Boudsocq, M P, McLenigan, R, Woodgate

Publikováno v: Biochemical Society transactions. 29(Pt 2)

The human RAD30B gene has recently been shown to encode a novel DNA polymerase, DNA polymerase iota (poliota). The role of poliota within the cell is presently unknown, and the only clues to its cellular function come from its biochemical characteriz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::80a546ec3b6d8cc8c43ab73024b4d19f
https://pubmed.ncbi.nlm.nih.gov/11356150

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Structural insights into the regulation of SOS mutagenesis

Autor: M, Gonzalez, E G, Frank, J P, McDonald, A S, Levine, R, Woodgate

Publikováno v: Acta biochimica Polonica. 45(1)

The Escherichia coli Umu proteins are best characterized by their role in damage inducible mutagenesis. Recently, we discovered that the intracellular levels of the UmuD and UmuC proteins are kept to a minimum by the Lon serine protease. Studies with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3378c61018d5d334f2869240f57afe5d
https://pubmed.ncbi.nlm.nih.gov/9701508

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Production and crystallization of a selenomethionyl variant of UmuD', an Escherichia coli SOS response protein

Autor: T S, Peat, E G, Frank, R, Woodgate, W A, Hendrickson

Publikováno v: Proteins. 25(4)

Crystals of both native and mutant Escherichia coli UmuD' protein were obtained using the hanging drop method. Soaking the native crystals in solutions of heavy metal ions failed to produce good isomorphous derivatives, and selenomethionine substitut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::451316fe9c6780f84cc88d3920c2e8d0
https://pubmed.ncbi.nlm.nih.gov/8865345

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[The existence of the ribonucleoprotein branching enzyme in rabbit skeletal muscle and ribozyme corresponding to it]

Autor: V M, Kochkina, I A, Morozov, E G, Frank, I V, Karpychev, O A, Rudik, G E, Pozmogova, B K, Chernov, T V, Venkstern, A A, Baev

Publikováno v: Molekuliarnaia biologiia. 25(6)

Amylose isomerase (AI) preparations were isolated from rabbit muscles after Petrova et al., as well as by the additional fractionation steps. Their homogeneity, enzymatic activity and RNA, isolated from those preparations, were characterized. AI prep

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d456ab0bd4eb725556dd30427e950e64
https://pubmed.ncbi.nlm.nih.gov/1726019

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