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PARP-2 Structure-Function Relationship

Valerie Schreiber, Michelle Ricoul, Jean-Christophe Am,  [Pg.13]

Fran oise Dantzer, V ronique Meder, Catherine Spenlehauer, [Pg.13]

Patrick Stiegler, Claude Niedergang, Laure Sabatier,Vincent Favaudon, Josiane Menissier-de Murcia and Gilbert de Murcia [Pg.13]

PARR poly(ADP-ribose) polymerase XRCCl, X-ray cross complementing faaor 1 BRCT, BRCAl c-terminus UVDE, UV damage endonuclease GFP, green fluorescent protein 3-AB, 3-aminobenzamide XPA, xeroderma pigmentosum group A DAPI, 4, 6-diamidino-2-phenylindol TDT, deoxynucleotidyl transferase PNK, polynucleotide kinase MEFs, mouse embryonic fibroblasts SSB, single strand breaks SSBR, single strand breaks repair DSB, double strand breaks. [Pg.13]

PARP-1 (113 kDa), the founding member, and PARP-2 (62 kDa) are so far the sole enzymes whose catalytic activity is immediately sdmulated by DNA strand-breaks, su esting that they are both involved in the cellular response to DNA damage. PARP-2 was discovered as a result of the presence of residual DNA-dependent PARP activity in embryonic fibroblasts [Pg.13]

See other pages where PARP-2 Structure-Function Relationship is mentioned: [Pg.13]    [Pg.15]    [Pg.17]    [Pg.19]    [Pg.21]    [Pg.23]    [Pg.27]    [Pg.29]    [Pg.31]    [Pg.13]    [Pg.15]    [Pg.17]    [Pg.19]    [Pg.21]    [Pg.23]    [Pg.27]    [Pg.29]    [Pg.31]    [Pg.61]   


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Function relationships

Functional relationships

PARPs

Structure-function relationship

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