Poly (ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly (ADP-ribose), a reversible covalent-modifier of chromosomal proteins. The protein is found in many tissues and may be subject to proteolysis generating smaller, active products.[5]
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Golovanov, A. P.; Barillà, D.; Golovanova, M.; Hayes, F.; Lian, L. Y. (2003). "ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure". Molecular Microbiology. 50 (4): 1141–1153. doi:10.1046/j.1365-2958.2003.03750.x. PMID14622405. S2CID45704180.
Keil, C.; Petermann, E.; Oei, S. L. (2004). "Tannins elevate the level of poly(ADP–ribose) in HeLa cell extracts". Archives of Biochemistry and Biophysics. 425 (1): 115–121. doi:10.1016/j.abb.2004.02.024. PMID15081900.
Meyer-Ficca, M. L.; Meyer, R. G.; Coyle, D. L.; Jacobson, E. L.; Jacobson, M. K. (2004). "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments". Experimental Cell Research. 297 (2): 521–532. doi:10.1016/j.yexcr.2004.03.050. PMID15212953.
Putt, K. S.; Hergenrother, P. J. (2004). "A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): Application to inhibitor identification and evaluation". Analytical Biochemistry. 333 (2): 256–264. doi:10.1016/j.ab.2004.04.032. PMID15450800.
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