TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 276, No. 4, Issue of January 26, pp. 2935–2942, 2001 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis* Received for publication, August 10, 2000, and in revised form, October 20, 2000 Published, JBC Papers in Press, October 25, 2000, DOI 10.1074/jbc.M007269200 El Bachir Affar‡, Marc Germain‡, Eric Winstall‡, Momchil Vodenicharov‡, Rashmi G. Shah‡, Guy S. Salvesen§, and Guy G. Poirier‡¶ From the ‡Health and Environment Unit, Laval University Medical Research Center, Centre Hospitalier Universitaire de Que ´bec, and Faculty of Medicine, Laval University, Que ´bec G1V 4G2, Canada and the §Burnham Institute, San Diego, California 92037 Poly(ADP-ribose) glycohydrolase (PARG) is responsi- pADPr synthesizing enzymes were identified, suggesting the ble for the catabolism of poly(ADP-ribose) synthesized presence within mammalian cells of a PARP-1-like enzyme by poly(ADP-ribose) polymerase (PARP-1) and other family. A protein named tankyrase with homology to ankyrins PARP-1-like enzymes. In this work, we report that PARG and to the catalytic domain of PARP-1 was isolated from hu- is cleaved during etoposide-, staurosporine-, and Fas- man tissue and shown to be associated with telomeres (3). induced apoptosis in human 
TI - Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m007269200
DA - 2001-01-01
UR - https://www.deepdyve.com/lp/unpaywall/caspase-3-mediated-processing-of-poly-adp-ribose-glycohydrolase-during-c4vEILSW5v
DP - DeepDyve
ER -