Human Topoisomerase I is Phosphorylafedin vitroon its Amino Terminal Domain by Protein Kinase NII
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm3.1994.375.4.255/pdf
Reference16 articles.
1. Protein kinase nii from calf thymus chromatin. isolation, characterization and some functional properties
2. [11] Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
3. Phosphorylation of human topoisomerase I by protein kinase C in vitro and in phorbol 12-myristate 13-acetate-activated HL-60 promyelocytic leukaemia cells
4. Acidic pentapeptide phosphorylated in vitro by calf thymus protein kinase NII binds to DNA in the presence of Mg2+cations
5. cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment.
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2. Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain;Amino Acids;2010-11-03
3. Mitotic Phosphorylation Stimulates DNA Relaxation Activity of Human Topoisomerase I;Journal of Biological Chemistry;2008-06
4. Altered phosphorylation of topoisomerase I following overexpression in an ovarian cancer cell line;Biochemistry and Cell Biology;2006-02-01
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