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10.1101/cshperspect.a012583

http://scihub22266oqcxt.onion/10.1101/cshperspect.a012583
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C3683898!3683898 !23545420
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suck abstract from ncbi


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pmid23545420
      Cold+Spring+Harb+Perspect+Biol 2013 ; 5 (4 ): a012583
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  • Base excision repair #MMPMID23545420
  • Krokan HE ; Bjørås M
  • Cold Spring Harb Perspect Biol 2013[Apr]; 5 (4 ): a012583 PMID23545420 show ga
  • Base excision repair (BER) corrects DNA damage from oxidation, deamination and alkylation. Such base lesions cause little distortion to the DNA helix structure. BER is initiated by a DNA glycosylase that recognizes and removes the damaged base, leaving an abasic site that is further processed by short-patch repair or long-patch repair that largely uses different proteins to complete BER. At least 11 distinct mammalian DNA glycosylases are known, each recognizing a few related lesions, frequently with some overlap in specificities. Impressively, the damaged bases are rapidly identified in a vast excess of normal bases, without a supply of energy. BER protects against cancer, aging, and neurodegeneration and takes place both in nuclei and mitochondria. More recently, an important role of uracil-DNA glycosylase UNG2 in adaptive immunity was revealed. Furthermore, other DNA glycosylases may have important roles in epigenetics, thus expanding the repertoire of BER proteins.
  • |*DNA Repair [MESH]
  • |Animals [MESH]
  • |Cell Nucleus/metabolism [MESH]
  • |DNA Damage [MESH]
  • |DNA Glycosylases/genetics [MESH]
  • |DNA Polymerase beta/metabolism [MESH]
  • |DNA/*genetics [MESH]
  • |Epigenesis, Genetic [MESH]
  • |Escherichia coli/enzymology [MESH]
  • |Humans [MESH]
  • |Mice [MESH]
  • |Mice, Knockout [MESH]
  • |Mitochondria/metabolism [MESH]
  • |Models, Molecular [MESH]
  • |Mutagenesis [MESH]
  • |Neoplasms/enzymology [MESH]
  • |Oxygen/chemistry [MESH]
  • |Poly(ADP-ribose) Polymerases/metabolism [MESH]


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