↑(en) Wensheng Lin, Jean-Christophe Amé, Nasreen Aboul-Ela, Elaine L. Jacobson et Myron K. Jacobson, « Isolation and Characterization of the cDNA Encoding Bovine Poly(ADP-ribose) Glycohydrolase », Journal of Biological Chemistry, vol. 272, , p. 11895-11901 (PMID9115250, DOI10.1074/jbc.272.18.11895, lire en ligne)
↑(en) J.-C. Amé, F. Apiou, E. L. Jacobson et M. K. Jacobson, « Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization », Cytogenetic and Genome Research, vol. 85, , p. 269–270 (PMID10449915, DOI10.1159/000015310, lire en ligne)
(en) E. B. Affar, M. Germain, E. Winstall, M. Vodenicharov, R. G. Shah, G. S. Salvesen et G. G. Poirier, « Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis », Journal of Biological Chemistry, vol. 276, no 4, , p. 2935–2942 (PMID11053413, DOI10.1074/jbc.M007269200)
(en) S. Ohashi, M. Kanai, S. Hanai, F. Uchiumi, H. Maruta, S. Tanuma et M. Miwa, « Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells », Biochemical and Biophysical Research Communications, vol. 307, no 4, , p. 915–921 (PMID12878198, DOI10.1016/S0006-291X(03)01272-5)
(en) R. G. Meyer, M. L. Meyer-Ficca, E. L. Jacobson et M. K. Jacobson, « Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23) », Gene, vol. 314, , p. 181–190 (PMID14527731, DOI10.1016/S0378-1119(03)00738-8)
(en) A. P. Golovanov, D. Barillà, M. Golovanova, F. Hayes et L. Y. Lian, « ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure », Molecular microbiology, vol. 50, no 4, , p. 1141–1153 (PMID14622405)
(en) C. Keil, E. Petermann et S. L. Oei, « Tannins elevate the level of poly(ADP–ribose) in HeLa cell extracts », Archives of Biochemistry and Biophysics, vol. 425, no 1, , p. 115–121 (PMID15081900, DOI10.1016/j.abb.2004.02.024)
(en) M. L. Meyer-Ficca, R. G. Meyer, D. L. Coyle, E. L. Jacobson et M. K. Jacobson, « Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments », Experimental Cell Research, vol. 297, no 2, , p. 521–532 (PMID15212953, DOI10.1016/j.yexcr.2004.03.050)
(en) K. S. Putt et P. J. Hergenrother, « A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): Application to inhibitor identification and evaluation », Analytical Biochemistry, vol. 333, no 2, , p. 256–264 (PMID15450800, DOI10.1016/j.ab.2004.04.032)
(en) M. -E. Bonicalzi, J. -F. Haince, A. Droit et G. G. Poirier, « Poly-ADP-ribosylation in health and disease », CMLS Cellular and Molecular Life Sciences, vol. 62, nos 7–8, , p. 739–750 (PMID15868399, DOI10.1007/s00018-004-4505-1)
(en) M. È. Bonicalzi, J. P. Gagné, P. Gagné, M. È. Ouellet, M. J. Hendzel et G. G. Poirier, « Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles », Biochemical Journal, vol. 392, no 3, , p. 499–509 (PMID16117724, PMCID1316289, DOI10.1042/BJ20050792)