Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Experimental Cell Research

• Publication date

  2001-08-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1006/EXCR.2001.5263PMID 11461113
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins*

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• Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions.

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• Assignment1 of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization

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• Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein.

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• A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues.

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• pADPRT‐2: a novel mammalian polymerizing(ADP‐ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans 1

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  1998cited by this paper
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• Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

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  1993cited by this paper
• Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis.

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• Role of poly(ADP-ribose) formation in DNA repair

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