1 |
Scarpa, E.S., Fabrizio, G., and Di Girolamo, M. (2013). A role of intracellular mono-ADP-ribosylation in cancer biology. FEBS J. 280, 3551-3562.
DOI
ScienceOn
|
2 |
Schreiber, V., Ame, J.C., Dolle, P., Schultz, I., Rinaldi, B., Fraulob, V., Menissier-de Murcia, J., and de Murcia, G. (2002). Poly(ADPribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem. 277, 23028-23036.
DOI
ScienceOn
|
3 |
Schreiber, V., Dantzer, F., Ame, J.C., and de Murcia, G. (2006). Poly(ADP-ribose): novel functions for an old molecule. Nat. Rev. Mol. Cell Biol. 7, 517-528.
DOI
ScienceOn
|
4 |
Smith, S., Giriat, I., Schmitt, A., and de Lange, T. (1998). Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 282, 1484-1487.
DOI
ScienceOn
|
5 |
Sharifi, R., Morra, R., Appel, C.D., Tallis, M., Chioza, B., Jankevicius, G., Simpson, M.A., Matic, I., Ozkan, E., Golia, B., et al. (2013). Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease. EMBO J. 32, 1225-1237.
DOI
ScienceOn
|
6 |
Slade, D., Dunstan, M.S., Barkauskaite, E., Weston, R., Lafite, P., Dixon, N., Ahel, M., Leys, D., and Ahel, I. (2011). The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. Nature 477, 616-620.
DOI
ScienceOn
|
7 |
Smith, S., and de Lange, T. (2000). Tankyrase promotes telomere elongation in human cells. Curr. Biol. 10, 1299-1302.
DOI
ScienceOn
|
8 |
Tuncel, H., Tanaka, S., Oka, S., Nakai, S., Fukutomi, R., Okamoto, M., Ota, T., Kaneko, H., Tatsuka, M., and Shimamoto, F. (2012). PARP6, a mono(ADP-ribosyl) transferase and a negative regulator of cell proliferation, is involved in colorectal cancer development. Int. J. Oncol. 41, 2079-2086.
DOI
|
9 |
Wang, Z., Michaud, G.A., Cheng, Z., Zhang, Y., Hinds, T.R., Fan, E., Cong, F., and Xu, W. (2012). Recognition of the iso-ADPribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination. Genes Dev. 26, 235-240.
DOI
ScienceOn
|
10 |
Yan, Q., Xu, R., Zhu, L., Cheng, X., Wang, Z., Manis, J., and Shipp, M.A. (2013). BAL1 and its partner E3 ligase, BBAP, link Poly(ADPribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8. Mol. Cell. Biol. 33, 845-857.
DOI
|
11 |
Zhang, Y., Liu, S., Mickanin, C., Feng, Y., Charlat, O., Michaud, G.A., Schirle, M., Shi, X., Hild, M., Bauer, A., et al. (2011a). RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling. Nat. Cell Biol. 13, 623-629.
DOI
ScienceOn
|
12 |
Yu, X., Chini, C.C., He, M., Mer, G., and Chen, J. (2003). The BRCT domain is a phospho-protein binding domain. Science 302, 639-642.
DOI
ScienceOn
|
13 |
Yu, M., Schreek, S., Cerni, C., Schamberger, C., Lesniewicz, K., Poreba, E., Vervoorts, J., Walsemann, G., Grotzinger, J., Kremmer, E., et al. (2005). PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation. Oncogene 24, 1982-1993.
DOI
ScienceOn
|
14 |
Yu, S.W., Andrabi, S.A., Wang, H., Kim, N.S., Poirier, G.G., Dawson, T.M., and Dawson, V.L. (2006). Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death. Proc. Natl. Acad. Sci. USA 103, 18314-18319.
DOI
ScienceOn
|
15 |
Zhang, Y., Liu, S.M., Mickanin, C., Feng, Y., Charlat, O., Michaud, G.A., Schirle, M., Shi, X.Y., Hild, M., Bauer, A., et al. (2011b). RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling. Nat. Cell Biol. 13, 623-U292.
DOI
ScienceOn
|
16 |
Ame, J.C., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Hoger, T., Menissier-de Murcia, J., and de Murcia, G. (1999). PARP-2, A novel mammalian DNA damagedependent poly(ADP-ribose) polymerase. J. Biol. Chem. 274, 17860-17868.
DOI
|
17 |
Zhong, Q., Gao, W., Du, F., and Wang, X. (2005). Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121, 1085-1095.
DOI
ScienceOn
|
18 |
Andrabi, S.A., Kang, H.C., Haince, J.F., Lee, Y.I., Zhang, J., Chi, Z., West, A.B., Koehler, R.C., Poirier, G.G., Dawson, T.M., et al. (2011). Iduna protects the brain from glutamate excitotoxicity and stroke by interfering with poly(ADP-ribose) polymer-induced cell death. Nat. Med. 17, 692-699.
DOI
ScienceOn
|
19 |
Aguiar, R.C., Takeyama, K., He, C., Kreinbrink, K., and Shipp, M.A. (2005). B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity. J. Biol. Chem. 280, 33756-33765.
DOI
ScienceOn
|
20 |
Ahel, I., Ahel, D., Matsusaka, T., Clark, A.J., Pines, J., Boulton, S.J., and West, S.C. (2008). Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature 451, 81-85.
DOI
ScienceOn
|
21 |
Aravind, L. (2001). The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. Trends Biochem. Sci. 26, 273-275.
DOI
ScienceOn
|
22 |
Atasheva, S., Akhrymuk, M., Frolova, E.I., and Frolov, I. (2012). New PARP gene with an anti-alphavirus function. J. Virol. 86, 8147-8160.
DOI
|
23 |
Bryant, H.E., Schultz, N., Thomas, H.D., Parker, K.M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N.J., and Helleday, T. (2005). Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase. Nature 434, 913-917.
DOI
ScienceOn
|
24 |
Costanzi, C., and Pehrson, J.R. (2001). MACROH2A2, a new member of the MARCOH2A core histone family. J. Biol. Chem. 276, 21776-21784.
DOI
ScienceOn
|
25 |
Chang, W., Dynek, J.N., and Smith, S. (2005). NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis. Biochem. J. 391, 177-184.
DOI
ScienceOn
|
26 |
Changolkar, L.N., Costanzi, C., Leu, N.A., Chen, D., McLaughlin, K.J., and Pehrson, J.R. (2007). Developmental changes in histone macroH2A1-mediated gene regulation. Mol. Cell. Biol. 27, 2758-2764.
DOI
ScienceOn
|
27 |
Fahrer, J., Kranaster, R., Altmeyer, M., Marx, A., and Burkle, A. (2007). Quantitative analysis of the binding affinity of poly(ADPribose) to specific binding proteins as a function of chain length. Nucleic Acids Res. 35, e143.
DOI
ScienceOn
|
28 |
Chen, D., Vollmar, M., Rossi, M.N., Phillips, C., Kraehenbuehl, R., Slade, D., Mehrotra, P.V., von Delft, F., Crosthwaite, S.K., Gileadi, O., et al. (2011). Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J. Biol. Chem. 286, 13261-13271.
DOI
ScienceOn
|
29 |
de Murcia, J.M.N., Ricoul, M., Tartier, L., Niedergang, C., Huber, A., Dantzer, F., Schreiber, V., Ame, J.C., Dierich, A., LeMeur, M., et al. (2003). Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse. EMBO J. 22, 2255-2263.
DOI
ScienceOn
|
30 |
Di Paola, S., Micaroni, M., Di Tullio, G., Buccione, R., and Di Girolamo, M. (2012). PARP16/ARTD15 is a novel endoplasmicreticulum- associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-beta 1. PLoS One 7, e37352.
DOI
|
31 |
Farmer, H., McCabe, N., Lord, C.J., Tutt, A.N., Johnson, D.A., Richardson, T.B., Santarosa, M., Dillon, K.J., Hickson, I., Knights, C., et al. (2005). Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 434, 917-921.
DOI
ScienceOn
|
32 |
Glover, J.N., Williams, R.S., and Lee, M.S. (2004). Interactions between BRCT repeats and phosphoproteins: tangled up in two. Trends Biochem. Sci. 29, 579-585.
DOI
ScienceOn
|
33 |
Gao, G., Guo, X., and Goff, S.P. (2002). Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297, 1703-1706.
DOI
ScienceOn
|
34 |
Gibson, B.A., and Kraus, W.L. (2012). New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell Biol. 13, 411-424.
DOI
ScienceOn
|
35 |
Hassa, P.O., and Hottiger, M.O. (2008). The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADPribose polymerases. Front Biosci. 13, 3046-3082.
DOI
|
36 |
Gonzalez, M., Nampoothiri, S., Kornblum, C., Oteyza, A.C., Walter, J., Konidari, I., Hulme, W., Speziani, F., Schols, L., Zuchner, S., et al. (2013). Mutations in phospholipase DDHD2 cause autosomal recessive hereditary spastic paraplegia (SPG54). Eur. J. Hum. Genet. [Epub ahead of print]
|
37 |
Gudjonsson, T., Altmeyer, M., Savic, V., Toledo, L., Dinant, C., Grofte, M., Bartkova, J., Poulsen, M., Oka, Y., Bekker-Jensen, S., et al. (2012). TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes. Cell 150, 697-709.
DOI
ScienceOn
|
38 |
Han, W., Li, X., and Fu, X. (2011). The macro domain protein family: structure, functions, and their potential therapeutic implications. Mutat. Res. 727, 86-103.
DOI
ScienceOn
|
39 |
Iles, N., Rulten, S., El-Khamisy, S.F., and Caldecott, K.W. (2007). APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Mol. Cell. Biol. 27, 3793-3803.
DOI
ScienceOn
|
40 |
Hsiao, S.J., and Smith, S. (2008). Tankyrase function at telomeres, spindle poles, and beyond. Biochimie 90, 83-92.
DOI
ScienceOn
|
41 |
Huang, S.M., Mishina, Y.M., Liu, S., Cheung, A., Stegmeier, F., Michaud, G.A., Charlat, O., Wiellette, E., Zhang, Y., Wiessner, S., et al. (2009). Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling. Nature 461, 614-620.
DOI
ScienceOn
|
42 |
Ikejima, M., and Gill, D.M. (1988). Poly(ADP-ribose) degradation by glycohydrolase starts with an endonucleolytic incision. J. Biol. Chem. 263, 11037-11040.
|
43 |
Levaot, N., Voytyuk, O., Dimitriou, I., Sircoulomb, F., Chandrakumar, A., Deckert, M., Krzyzanowski, P.M., Scotter, A., Gu, S., Janmohamed, S., et al. (2011). Loss of Tankyrase-mediated destruction of 3BP2 is the underlying pathogenic mechanism of cherubism. Cell 147, 1324-1339.
DOI
ScienceOn
|
44 |
Jankevicius, G., Hassler, M., Golia, B., Rybin, V., Zacharias, M., Timinszky, G., and Ladurner, A.G. (2013). A family of macrodomain proteins reverses cellular mono-ADP-ribosylation. Nat. Struct. Mol. Biol. 20, 508-514.
DOI
ScienceOn
|
45 |
Juszczynski, P., Kutok, J.L., Li, C., Mitra, J., Aguiar, R.C., and Shipp, M.A. (2006). BAL1 and BBAP are regulated by a gamma interferon-responsive bidirectional promoter and are overexpressed in diffuse large B-cell lymphomas with a prominent inflammatory infiltrate. Mol. Cell. Biol. 26, 5348-5359.
DOI
ScienceOn
|
46 |
Jwa, M., and Chang, P. (2012). PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1 alphamediated unfolded protein response. Nat. Cell Biol. 14, 1223-1230.
DOI
ScienceOn
|
47 |
Kleine, H., Poreba, E., Lesniewicz, K., Hassa, P.O., Hottiger, M.O., Litchfield, D.W., Shilton, B.H., and Luscher, B. (2008). Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation. Mol. Cell 32, 57-69.
DOI
ScienceOn
|
48 |
Koh, D.W., Lawler, A.M., Poitras, M.F., Sasaki, M., Wattler, S., Nehls, M.C., Stoger, T., Poirier, G.G., Dawson, V.L., and Dawson, T.M. (2004). Failure to degrade poly(ADP-ribose) causes increased sensitivity to cytotoxicity and early embryonic lethality. Proc. Natl. Acad. Sci. USA 101, 17699-17704.
DOI
ScienceOn
|
49 |
Kraus, W.L. (2008). Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 20, 294-302.
DOI
ScienceOn
|
50 |
Li, M., and Yu, X. (2013). Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation. Cancer Cell 23, 693-704.
DOI
ScienceOn
|
51 |
Li, J., Williams, B.L., Haire, L.F., Goldberg, M., Wilker, E., Durocher, D., Yaffe, M.B., Jackson, S.P., and Smerdon, S.J. (2002). Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2. Mol. Cell 9, 1045-1054.
DOI
ScienceOn
|
52 |
Li, B., Navarro, S., Kasahara, N., and Comai, L. (2004). Identification and biochemical characterization of a Werner's syndrome protein complex with Ku70/80 and poly(ADP-ribose) polymerase-1. J. Biol. Chem. 279, 13659-13667.
DOI
ScienceOn
|
53 |
Li, M., Lu, L.Y., Yang, C.Y., Wang, S., and Yu, X. (2013). The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response. Genes Dev. 27, 1752-1768.
DOI
ScienceOn
|
54 |
Mehrotra, P., Riley, J.P., Patel, R., Li, F., Voss, L., and Goenka, S. (2011). PARP-14 functions as a transcriptional switch for Stat6-dependent gene activation. J. Biol. Chem. 286, 1767-1776.
DOI
ScienceOn
|
55 |
Lin, W., Ame, J.C., Aboul-Ela, N., Jacobson, E.L., and Jacobson, M.K. (1997). Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 272, 11895-11901.
DOI
ScienceOn
|
56 |
MacPherson, L., Tamblyn, L., Rajendra, S., Bralha, F., McPherson, J.P., and Matthews, J. (2013). 2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation. Nucleic Acids Res. 41, 1604-1621.
DOI
|
57 |
Matsuno, K., Eastman, D., Mitsiades, T., Quinn, A.M., Carcanciu, M.L., Ordentlich, P., Kadesch, T., and Artavanis-Tsakonas, S. (1998). Human deltex is a conserved regulator of Notch signalling. Nat. Genet. 19, 74-78.
DOI
ScienceOn
|
58 |
Oberoi, J., Richards, M.W., Crumpler, S., Brown, N., Blagg, J., and Bayliss, R. (2010). Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkheadassociated and RING Domains (CHFR). J. Biol. Chem. 285, 39348-39358.
DOI
|
59 |
Meyer-Ficca, M.L., Meyer, R.G., Coyle, D.L., Jacobson, E.L., and Jacobson, M.K. (2004). Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments. Exp. Cell Res. 297, 521-532.
DOI
ScienceOn
|
60 |
Neuvonen, M., and Ahola, T. (2009). Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites. J. Mol. Biol. 385, 212-225.
DOI
ScienceOn
|
61 |
Patel, A.G., Sarkaria, J.N., and Kaufmann, S.H. (2011). Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells. Proc. Natl. Acad. Sci. USA 108, 3406-3411.
DOI
ScienceOn
|
62 |
Ozaki, Y., Matsui, H., Asou, H., Nagamachi, A., Aki, D., Honda, H., Yasunaga, S., Takihara, Y., Yamamoto, T., Izumi, S., et al. (2012). Poly-ADP ribosylation of Miki by tankyrase-1 promotes centrosome maturation. Mol. Cell 47, 694-706.
DOI
ScienceOn
|
63 |
Parsons, J.L., Dianova, II, Allinson, S.L., and Dianov, G.L. (2005). Poly(ADP-ribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts. FEBS J. 272, 2012-2021.
DOI
ScienceOn
|
64 |
Pehrson, J.R., and Fried, V.A. (1992). MacroH2A, a core histone containing a large nonhistone region. Science 257, 1398-1400.
DOI
|
65 |
Pleschke, J.M., Kleczkowska, H.E., Strohm, M., and Althaus, F.R. (2000). Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40974-40980.
DOI
ScienceOn
|
66 |
Ruscetti, T., Lehnert, B.E., Halbrook, J., Le Trong, H., Hoekstra, M.F., Chen, D.J., and Peterson, S.R. (1998). Stimulation of the DNA-dependent protein kinase by poly(ADP-ribose) polymerase. J. Biol. Chem. 273, 14461-14467.
DOI
ScienceOn
|
67 |
Raval-Fernandes, S., Kickhoefer, V.A., Kitchen, C., and Rome, L.H. (2005). Increased susceptibility of vault poly(ADP-ribose) polymerase-deficient mice to carcinogen-induced tumorigenesis. Cancer Res. 65, 8846-8852.
DOI
ScienceOn
|
68 |
Riffell, J.L., Lord, C.J., and Ashworth, A. (2012). Tankyrase-targeted therapeutics: expanding opportunities in the PARP family. Nat Rev. Drug Discov. 11, 923-936.
DOI
ScienceOn
|
69 |
Rosenthal, F., Feijs, K.L.H., Frugier, E., Bonalli, M., Forst, A.H., Imhof, R., Winkler, H.C., Fischer, D., Caflisch, A., Hassa, P.O., et al. (2013). Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases. Nat. Struct. Mol. Biol. 20, 502-507.
DOI
ScienceOn
|
70 |
Rouleau, M., Patel, A., Hendzel, M.J., Kaufmann, S.H., and Poirier, G.G. (2010). PARP inhibition: PARP1 and beyond. Nat. Rev. Cancer 10, 293-301.
DOI
ScienceOn
|
71 |
Rulten, S.L., Cortes-Ledesma, F., Guo, L., Iles, N.J., and Caldecott, K.W. (2008). APLF (C2orf13) is a novel component of poly(ADPribose) signaling in mammalian cells. Mol. Cell. Biol. 28, 4620-4628.
DOI
ScienceOn
|
72 |
Rulten, S.L., Fisher, A.E., Robert, I., Zuma, M.C., Rouleau, M., Ju, L., Poirier, G., Reina-San-Martin, B., and Caldecott, K.W. (2011). PARP-3 and APLF function together to accelerate nonhomologous end-joining. Mol. Cell 41, 33-45.
DOI
ScienceOn
|
73 |
Sbodio, J.I., Lodish, H.F., and Chi, N.W. (2002). Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomererepeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase). Biochem. J. 361, 451-459.
DOI
|
74 |
Oka, S., Kato, J., and Moss, J. (2006). Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 281, 705-713.
DOI
ScienceOn
|
75 |
Gottschalk, A.J., Timinszky, G., Kong, S.E., Jin, J., Cai, Y., Swanson, S.K., Washburn, M.P., Florens, L., Ladurner, A.G., Conaway, J.W., et al. (2009). Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler. Proc. Natl. Acad. Sci. USA 106, 13770-13774.
DOI
ScienceOn
|
76 |
Kang, H.C., Lee, Y.I., Shin, J.H., Andrabi, S.A., Chi, Z.K., Gagne, J.P., Lee, Y.J., Ko, H.S., Lee, B.D., Poirier, G.G., et al. (2011). Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage. Proc. Natl. Acad. Sci. USA 108, 14103-14108.
DOI
ScienceOn
|
77 |
Moss, J., Stanley, S.J., Nightingale, M.S., Murtagh, J.J., Jr., Monaco, L., Mishima, K., Chen, H.C., Williamson, K.C., and Tsai, S.C. (1992). Molecular and immunological characterization of ADPribosylarginine hydrolases. J. Biol. Chem. 267, 10481-10488.
|
78 |
Scolnick, D.M., and Halazonetis, T.D. (2000). Chfr defines a mitotic stress checkpoint that delays entry into metaphase. Nature 406, 430-435.
DOI
ScienceOn
|
79 |
Venkannagari, H., Fallarero, A., Feijs, K.L.H., Luscher, B., and Lehtio, L. (2013). Activity-based assay for human mono-ADPribosyltransferases ARTD7/PARP15 and ARTD10/PARP10 aimed at screening and profiling inhibitors. Eur. J. Pharm. Sci. 49, 148-156.
DOI
ScienceOn
|
80 |
Gagne, J.P., Isabelle, M., Lo, K.S., Bourassa, S., Hendzel, M.J., Dawson, V.L., Dawson, T.M., and Poirier, G.G. (2008). Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes. Nucleic Acids Res. 36, 6959-6976.
DOI
ScienceOn
|