المؤلفون: S. Gross, E. Kotova Yu., N. Maluchenko V., J. Pascal M., V. Studitsky M., С. Гросс, Е. Котова Ю., Н. Малюченко В., Дж. Паскаль М., В. Студитский М.

المصدر: Vestnik Moskovskogo universiteta. Seriya 16. Biologiya; № 4 (2016); 61-65 ; Вестник Московского университета. Серия 16. Биология; № 4 (2016); 61-65 ; 0137-0952

مصطلحات موضوعية: PARP1, olaparib, gossypol, BRCT domain, Zn3 domain, WGR-domain, poly ADPribosylation, олапариб, госсипол, BRCT-домен, Zn3-домен, WGR-домен, поли(АДФ-рибозил)ирование

وصف الملف: application/pdf

Relation: https://vestnik-bio-msu.elpub.ru/jour/article/view/392/367; Ame J.C., Spenlehauer C., de Murcia G. The PARP superfamily // BioEssays. 2004. Vol. 26. N 8. P. 882–893; Ludwig A., Behnke B., Holtlund J., Hilz H. Immunoquantitation and size determination of intrinsic poly(ADPribose) polymerase from acid precipitates. An analysis of the in vivo status in mammalian species and in lower eukaryotes // J. Biol. Chem. 1988. Vol. 263. N 15. P.6993–6999.; Yamanaka H., Penning C.A., Willis E.H., Wasson D.B., Carson D.A. Characterization of human poly(ADP-ribose) polymerase with autoantibodies // J. Biol. Chem. 1988. Vol. 263. N 8. P. 3879–3883.; Haince JF., McDonald D., Rodrigue A., Dery U., Masson J.Y., Hendzel M.J., Poirier G.G. PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites // J. Biol. Chem. 2008. Vol. 283. N 2. P. 1197–1208.; Thomas C., Tulin A.V. Poly-ADP-ribose polymerase: machinery for nuclear processes // Mol. Aspects Med. 2013. Vol. 34. N 6. P. 1124–1137.; Nishikimi M., Ogasawara K., Kameshita I., Taniguchi T., Shizuta Y. Poly(ADP-ribose) synthetase. The DNA binding domain and the automodification domain // J. Biol. Chem. 1982. Vol. 257. N 11. P. 6102–6105.; Kameshita I., Matsuda Z., Taniguchi T., Shizuta Y. Poly (ADP-Ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain // J. Biol. Chem. 1984. Vol. 259. N 8. P. 4770–4776.; Gibson B.A., Kraus W.L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs // Nat. Rev. Mol. Cell Biol. 2012. Vol. 13 N 7. P. 411–424.; Langelier M.F., Servent K.M., Rogers E.E., Pascal J.M. A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation // J. Biol. Chem. 2008. Vol. 283. N 7. P. 4105–4114.; Tao Z., Gao P., Hoffman D.W., Liu H.W. Domain C of human poly(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif // Biochemistry. 2008. Vol. 47. N 21. P. 5804–5813.; Langelier M., Ruhl D. D., Planck J.L., Kraus W.L., Pascal J.M. The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction // J. Biol. Chem. 2010. Vol. 285. N 24. P. 18877–18887.; Langelier M.F., Planck J.L., Roy S., Pascal J.M. Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1 // Science 2012. Vol. 336. N 6082. P. 728–732.; Bork P., Hofman K., Buche P., Neuwal A.F., Altschu S.F., Koonin E.V. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins // Faseb J. 1997. Vol. 11. N 1. P. 68–76.; Masson M., Niedergang C., Schreiber V., Muller S., Menissier-de Murcia J., de Murcia G. XRCC1 is specifically associated with poly(ADPribose) polymerase and negatively regulates its activity following DNA damage // Mol. Cell. Biol. 1998. Vol. 18. N 6. P. 3563–3571.; Masson M., Menissier-de Murcia J., Mattei, M.G., de Murcia G., Niedergang C.P. Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9 // Gene. 1997. Vol. 190. N 2. P. 287–296.; Buki K.G., Bauer P.I., Hakam A., Kun E. Identification of domains of poly(ADP-ribose) polymerase for protein binding and selfassociation // J. Biol. Chem. 1995. Vol. 270. N 7. P. 3370–3377.; Nie J., Sakamoto S., Song D., Qu Z., Ota K., Taniguchi T. Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase // FEBS Lett. 1998. Vol. 424. N 1–2. P. 27–32.; Griesenbeck J., Ziegler M., Tomilin N., Schweiger M., Oei S.L. Stimulation of the catalytic activity of poly(ADP-ribosyl) transferase by transcription factor Yin Yang 1 // FEBS Lett. 1999. Vol. 443. N 1. P. 20–24.; Na Z., Peng B., Ng S., Pan S., Lee J.S., Shen H.M., Yao S.Q. A small-molecule protein-protein interaction inhibitor of PARP1 that targets its BRCT domain // Angew. Chem. Int. Ed. Engl. 2015. Vol. 54. N 8. P. 2515–2519.; Malyuchenko N.V., Kotova E.Yu., Kulaeva O.I., Kirpichnikov M.P., Studitskiy V.M. PARP1 inhibitors: Antitumor drug design // Acta Naturae. 2015. Vol. 7. N 3. P. 27–37.; Gilbert N.E. O’Reilly J.E., Chang C.J., Lin Y.C., Brueggemeier R.W. Antiproliferative activity of gossypol and gossypolone on human breast cancer cells // Life Sci. 1995. Vol. 57. N. 1. Р. 61–67.; Langelier M.F., Planck J.L., Servent K.M., Pascal J.M. Purification of human PARPI and PARPI domains from E.coli for structural and biochemical analysis // Methods Mol. Biol. 2011. Vol. 780. Р. 209–226.; Kotova E., Pinnola A.D., Tulin A.V. Small-molecule collection and high-throughput colorimetric assay to identify PARP-1 inhibitors // Methods Mol. Biol. 2011. Vol. 780. P. 491–516.; Dawicki-McKenna J.M., Langelier M.F., DeNizio J.E., Riccio A.A., Cao C.D., Karch K.R., McCauley M., Steffen J.D., Black B.E., Pascal J.M. PARP-1 activation requires local unfolding of an autoinhibitory domain // Mol. Cell. 2015. Vol. 60. N 5. P. 755–768.; https://vestnik-bio-msu.elpub.ru/jour/article/view/392

الاتاحة: https://vestnik-bio-msu.elpub.ru/jour/article/view/392