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  1. Article: Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair.

    Weinfeld, Michael / Mani, Rajam S / Abdou, Ismail / Aceytuno, R Daniel / Glover, J N Mark

    Trends in biochemical sciences

    2011  Volume 36, Issue 5, Page(s) 262–271

    Abstract: ... Polynucleotide kinase/phosphatase (PNKP) serves a crucial role in the repair of DNA strand breaks by catalyzing ... The termini of DNA strand breaks induced by internal and external factors often require processing ... the restoration of 5'-phosphate and 3'-hydroxyl termini. It participates in several DNA repair pathways ...

    Abstract The termini of DNA strand breaks induced by internal and external factors often require processing before missing nucleotides can be replaced by DNA polymerases and the strands rejoined by DNA ligases. Polynucleotide kinase/phosphatase (PNKP) serves a crucial role in the repair of DNA strand breaks by catalyzing the restoration of 5'-phosphate and 3'-hydroxyl termini. It participates in several DNA repair pathways through interactions with other DNA repair proteins, notably XRCC1 and XRCC4. Recent studies have highlighted the physiological importance of PNKP in maintaining the genomic stability of normal tissues, particularly developing neural cells, as well as enhancing the resistance of cancer cells to genotoxic therapeutic agents.
    MeSH term(s) Amino Acid Sequence ; Animals ; DNA Breaks ; DNA Repair ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/metabolism ; DNA-Binding Proteins/metabolism ; Humans ; Phosphotransferases (Alcohol Group Acceptor)/genetics ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Protein Binding ; Sequence Homology, Amino Acid ; X-ray Repair Cross Complementing Protein 1
    Chemical Substances DNA-Binding Proteins ; X-ray Repair Cross Complementing Protein 1 ; XRCC1 protein, human ; XRCC4 protein, human ; PNKP protein, human (EC 2.7.1.-) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; DNA Repair Enzymes (EC 6.5.1.-)
    Language English
    Publishing date 2011-02-25
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2011.01.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair

    Weinfeld, Michael / Mani, Rajam S. / Abdou, Ismail / Aceytuno, R. Daniel / Glover, J.N. Mark

    Trends in biochemical sciences

    Volume v. 36,, Issue no. 5

    Abstract: ... Polynucleotide kinase/phosphatase (PNKP) serves a crucial role in the repair of DNA strand breaks by catalyzing ... The termini of DNA strand breaks induced by internal and external factors often require processing ... the restoration of 5′-phosphate and 3′-hydroxyl termini. It participates in several DNA repair pathways ...

    Abstract The termini of DNA strand breaks induced by internal and external factors often require processing before missing nucleotides can be replaced by DNA polymerases and the strands rejoined by DNA ligases. Polynucleotide kinase/phosphatase (PNKP) serves a crucial role in the repair of DNA strand breaks by catalyzing the restoration of 5′-phosphate and 3′-hydroxyl termini. It participates in several DNA repair pathways through interactions with other DNA repair proteins, notably XRCC1 and XRCC4. Recent studies have highlighted the physiological importance of PNKP in maintaining the genomic stability of normal tissues, particularly developing neural cells, as well as enhancing the resistance of cancer cells to genotoxic therapeutic agents.
    Keywords genotoxicity ; DNA ; DNA repair ; nucleotides ; proteins ; neoplasm cells ; ligases ; tissues
    Language English
    Document type Article
    ISSN 0968-0004
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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