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Phosphorylation of serine residues in the N-terminal domains of eukaryotic type I topoisomerases.

作者信息

Staron K, Samuels D S

机构信息

Institute of Biochemistry, Warsaw University, Poland.

出版信息

Mol Biol Rep. 1998 Jul;25(3):157-61. doi: 10.1023/a:1006827925817.

DOI:10.1023/a:1006827925817
PMID:9700051
Abstract

Eukaryotic topoisomerase I polypeptides can be partitioned into four structural domains. The function of the N-terminal domain, which is a target for serine-specific phosphorylation, has not been fully defined. The number of serine residues in the N-terminal domain of topoisomerase I from different species is inversely proportional to the number of charged amino acids in this region of the protein. The significance of this correlation is discussed in terms of a possible role for serine-specific phosphorylation in the activity of the enzyme.

摘要

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本文引用的文献

1
How do protein kinases recognize their substrates?蛋白激酶如何识别其底物?
Biochim Biophys Acta. 1996 Dec 12;1314(3):191-225. doi: 10.1016/s0167-4889(96)00083-3.
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DNA topoisomerases.DNA拓扑异构酶
Annu Rev Biochem. 1996;65:635-92. doi: 10.1146/annurev.bi.65.070196.003223.
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The domain organization of human topoisomerase I.人类拓扑异构酶I的结构域组织
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4
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