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The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
Open accessAbstract
Poly-ADP-ribose metabolism plays a mayor role in a wide range of biological processes, such as maintenance of genomic stability, transcriptional regulation, energy metabolism and cell death. Poly-ADP-ribose polymerases (PARPs) are an ancient family of enzymes, as evidenced by the poly-ADP-ribosylating activities reported in dinoflagellates and archaebacteria and by the identification of Parp-like genes in eubacterial and archaeabacterial genomes. Six genes encoding "bona fide" PARP enzymes have been identified in mammalians: PARP1, PARP2, PARP3, PARP4/vPARP, PARP5/Tankyrases-1 and PARP6/Tankyrases-2. The best studied of these enzymes PARP1 plays a primary role in the process of poly-ADP-ribosylation. PARP1-mediated poly-ADP-ribosylation has been implicated in the pathogenesis of cancer, inflammatory and neurodegenerative disorders. This review will summarize the novel findings and concepts for PARP enzymes and their poly-ADP-ribosylation activity in the regulation of physiological and pathophysiological processes. A special focus is placed on the proposed molecular mechanisms involved in these processes, such as signaling, regulation of telomere dynamics, remodeling of chromatin structure and transcriptional regulation. A potential functional cross talk between PARP family members and other NAD+-consuming enzymes is discussed.
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1 retracted
Chung, J.-H., Ginn-Pease, M. E., & Eng, C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0124 · Cited by 164
RetractedTargeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
Farmer, H., McCabe, N., Lord, C. J., Tutt, A. N. J., Johnson, D. A., Richardson, T. B., Santarosa, M., Dillon, K. J., Hickson, I., Knights, C., et al. (2005) · Nature · doi:10.1038/nature03445 · Cited by 6,683
Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
Bryant, H. E., Schultz, N., Thomas, H. D., Parker, K. M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N. J., & Helleday, T. (2005) · Nature · doi:10.1038/nature03443 · Cited by 5,198
Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060
Purification and Characterization
(2006) · Biomacromolecules · doi:10.1002/0470080124.ch3 · Cited by 2,309
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Ame, J.-C., & de Murcia, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,915
Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor
Yu, S.-W., Wang, H., Poitras, M. F., Coombs, C., Bowers, W. J., Federoff, H. J., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2002) · Science · doi:10.1126/science.1072221 · Cited by 1,826
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
d'AMOURS, D., DESNOYERS, S., d'SILVA, I., & POIRIER, G. G. (1999) · Biochemical Journal · doi:10.1042/bj3420249 · Cited by 1,815
Telomeres and human disease: ageing, cancer and beyond
Blasco, M. A. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1656 · Cited by 1,434
The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373
Cell death by necrosis: towards a molecular definition
Golstein, P., & Kroemer, G. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.001 · Cited by 1,044
Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres
Smith, S., Giriat, I., Schmitt, A., & de Lange, T. (1998) · Science · doi:10.1126/science.282.5393.1484 · Cited by 1,012
The General Transcription Machinery and General Cofactors
Thomas, M. C., & Chiang, C.-M. (2006) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230600648736 · Cited by 925
Zong, W.-X., & Thompson, C. B. (2006) · Genes & Development · doi:10.1101/gad.1376506 · Cited by 917
Masson, M., Niedergang, C., Schreiber, V., Muller, S., Menissier-de Murcia, J., & de Murcia, G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3563 · Cited by 910
The ankyrin repeat as molecular architecture for protein recognition
Mosavi, L. K., Cammett, T. J., Desrosiers, D. C., & Peng, Z. (2004) · Protein Science · doi:10.1110/ps.03554604 · Cited by 907
Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
Jagtap, P., & Szabó, C. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1718 · Cited by 896
A Topoisomerase IIß-Mediated dsDNA Break Required for Regulated Transcription
Ju, B.-G., Lunyak, V. V., Perissi, V., Garcia-Bassets, I., Rose, D. W., Glass, C. K., & Rosenfeld, M. G. (2006) · Science · doi:10.1126/science.1127196 · Cited by 840
Mitochondrio‐nuclear translocation of AIF in apoptosis and necrosis
Daugas, E., Susin, S. A., Zamzami, N., Ferri, K. F., Irinopoulou, T., Larochette, N., Prévost, M., Leber, B., Andrews, D., Penninger, J., et al. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.5.729 · Cited by 776
Poly(ADP-Ribose) in the Cellular Response to DNA Damage
Berger, N. A. (1985) · Radiation Research · doi:10.2307/3576299 · Cited by 775
Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease.
Wang, Z. Q., Auer, B., Stingl, L., Berghammer, H., Haidacher, D., Schweiger, M., & Wagner, E. F. (1995) · Genes & Development · doi:10.1101/gad.9.5.509 · Cited by 774
PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
Amé, J.-C., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Höger, T., Murcia, J. M.-D., & de Murcia, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17860 · Cited by 745
Two Distinct Pathways Leading to Nuclear Apoptosis
Susin, S. A., Daugas, E., Ravagnan, L., Samejima, K., Zamzami, N., Loeffler, M., Costantini, P., Ferri, K. F., Irinopoulou, T., Prévost, M.-C., et al. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.4.571 · Cited by 736
Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death
Yu, S.-W., Andrabi, S. A., Wang, H., Kim, N. S., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606528103 · Cited by 718
Schreiber, V., Amé, J.-C., Dollé, P., Schultz, I., Rinaldi, B., Fraulob, V., Ménissier-de Murcia, J., & de Murcia, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202390200 · Cited by 705
Role of poly(ADP-ribose) synthetase in inflammation and ischaemia–reperfusion
Szabó, C., & Dawson, V. L. (1998) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(98)01193-6 · Cited by 685
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
Hassa, P. O., Haenni, S. S., Elser, M., & Hottiger, M. O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-05 · Cited by 682
Self-citationChambon, P., Weill, J. D., & Mandel, P. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90024-x · Cited by 654
Poly(ADP-ribose) (PAR) polymer is a death signal
Andrabi, S. A., Kim, N. S., Yu, S.-W., Wang, H., Koh, D. W., Sasaki, M., Klaus, J. A., Otsuka, T., Zhang, Z., Koehler, R. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606526103 · Cited by 643
Menissier de Murcia, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg206 · Cited by 627
AIF deficiency compromises oxidative phosphorylation
Vahsen, N., Candé, C., Brière, J., Bénit, P., Joza, N., Larochette, N., Mastroberardino, P. G., Pequignot, M. O., Casares, N., Lazar, V., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600461 · Cited by 623
Caldecott, K. W., Aoufouchi, S., Johnson, P., & Shall, S. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.22.4387 · Cited by 620
Alkylating DNA damage stimulates a regulated form of necrotic cell death
Zong, W.-X., Ditsworth, D., Bauer, D. E., Wang, Z.-Q., & Thompson, C. B. (2004) · Genes & Development · doi:10.1101/gad.1199904 · Cited by 618
The harlequin mouse mutation downregulates apoptosis-inducing factor
Klein, J. A., Longo-Guess, C. M., Rossmann, M. P., Seburn, K. L., Hurd, R. E., Frankel, W. N., Bronson, R. T., & Ackerman, S. L. (2002) · Nature · doi:10.1038/nature01034 · Cited by 605
PARP is important for genomic stability but dispensable in apoptosis
Wang, Z.-Q., Stingl, L., Morrison, C., Jantsch, M., Los, M., Schulze-Osthoff, K., & Wagner, E. F. (1997) · Genes & Development · doi:10.1101/gad.11.18.2347 · Cited by 557
Kim, M. Y., Mauro, S., Gévry, N., Lis, J. T., & Kraus, W. L. (2004) · Cell · doi:10.1016/j.cell.2004.11.002 · Cited by 550
Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins
Pleschke, J. M., Kleczkowska, H. E., Strohm, M., & Althaus, F. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006520200 · Cited by 541
Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?
Shall, S., & de Murcia, G. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00016-1 · Cited by 534
Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure.
Poirier, G. G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C., & Mandel, P. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3423 · Cited by 515
Candé, C., Cohen, I., Daugas, E., Ravagnan, L., Larochette, N., Zamzami, N., & Kroemer, G. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01374-3 · Cited by 513
SAP – a putative DNA-binding motif involved in chromosomal organization
Aravind, L., & Koonin, E. V. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01537-6 · Cited by 512
Berger, F., Lau, C., Dahlmann, M., & Ziegler, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508660200 · Cited by 508
The macro domain is an ADP‐ribose binding module
Karras, G. I., Kustatscher, G., Buhecha, H. R., Allen, M. D., Pugieux, C., Sait, F., Bycroft, M., & Ladurner, A. G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600664 · Cited by 505
Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death
Lorenzo, H. K., Susin, S. A., Penninger, J., & Kroemer, G. (1999) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400527 · Cited by 494
The new life of a centenarian: signalling functions of NAD(P)
Berger, F. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.01.007 · Cited by 489
Apoptosis‐inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis
Daugas, E., Nochy, D., Ravagnan, L., Loeffler, M., Susin, S. A., Zamzami, N., & Kroemer, G. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01731-2 · Cited by 466
Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling
Hong, S. J., Dawson, T. M., & Dawson, V. L. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.03.005 · Cited by 463
Calpain I Induces Cleavage and Release of Apoptosis-inducing Factor from Isolated Mitochondria
Polster, B. M., Basañez, G., Etxebarria, A., Hardwick, J. M., & Nicholls, D. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413269200 · Cited by 437
A Targeted DNA-PKcs-Null Mutation Reveals DNA-PK-Independent Functions for KU in V(D)J Recombination
Gao, Y., Chaudhuri, J., Zhu, C., Davidson, L., Weaver, D. T., & Alt, F. W. (1998) · Immunity · doi:10.1016/s1074-7613(00)80619-6 · Cited by 432
Hassa, P. O., & Hottiger, M. O. (2002) · Cellular and Molecular Life Sciences CMLS · doi:10.1007/s00018-002-8527-2 · Cited by 427
Self-citationThe 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
Kickhoefer, V. A., Siva, A. C., Kedersha, N. L., Inman, E. M., Ruland, C., Streuli, M., & Rome, L. H. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.917 · Cited by 405
Pillai, J. B., Isbatan, A., Imai, S.-I., & Gupta, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506162200 · Cited by 391
Alano, C. C., Ying, W., & Swanson, R. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313329200 · Cited by 374
ADP-ribosylation of proteins. Enzymology and biological significance.
Althaus, F. R., & Richter, C. (1987) · PubMed · Cited by 371
Sparago, A., Cerrato, F., Vernucci, M., Ferrero, G. B., Silengo, M. C., & Riccio, A. (2004) · Nature Genetics · doi:10.1038/ng1410 · Cited by 371
DNA binding is required for the apoptogenic action of apoptosis inducing factor
Ye, H., Cande, C., Stephanou, N. C., Jiang, S., Gurbuxani, S., Larochette, N., Daugas, E., Garrido, C., Kroemer, G., & Wu, H. (2002) · Nature Structural Biology · doi:10.1038/nsb836 · Cited by 368
Regulation of intracellular levels of NAD: A novel role for CD38
Aksoy, P., White, T. A., Thompson, M., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.042 · Cited by 351
DNA repair defect in poly(ADP-ribose) polymerase-deficient cell lines
Trucco, C. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.11.2644 · Cited by 348
Koh, D. W., Lawler, A. M., Poitras, M. F., Sasaki, M., Wattler, S., Nehls, M. C., Stöger, T., Poirier, G. G., Dawson, V. L., & Dawson, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406182101 · Cited by 339
Importance of Poly(ADP-Ribose) Glycohydrolase in the Control of Poly(ADP-Ribose) Metabolism
Davidovic, L., Vodenicharov, M., Affar, E. B., & Poirier, G. G. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5263 · Cited by 326
Moubarak, R. S., Yuste, V. J., Artus, C., Bouharrour, A., Greer, P. A., Menissier-de Murcia, J., & Susin, S. A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02141-06 · Cited by 322
Role for the Related Poly(ADP-Ribose) Polymerases Tankyrase 1 and 2 at Human Telomeres
Cook, B. D., Dynek, J. N., Chang, W., Shostak, G., & Smith, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.332-342.2002 · Cited by 316
Studies on the Polymer of Adenosine Diphosphate Ribose
Nishizuka, Y., Ueda, K., Nakazawa, K., & Hayaishi, O. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95947-8 · Cited by 308
Hassa, P. O., Haenni, S. S., Buerki, C., Meier, N. I., Lane, W. S., Owen, H., Gersbach, M., Imhof, R., & Hottiger, M. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507553200 · Cited by 306
Self-citationPoly(ADP-ribosyl)ation regulates CTCF-dependent chromatin insulation
Yu, W., Ginjala, V., Pant, V., Chernukhin, I., Whitehead, J., Docquier, F., Farrar, D., Tavoosidana, G., Mukhopadhyay, R., Kanduri, C., et al. (2004) · Nature Genetics · doi:10.1038/ng1426 · Cited by 298
A Role of Poly (ADP-Ribose) Polymerase in NF- B Transcriptional Activation
Hassa, P. O., & Hottiger, M. O. (1999) · Biological Chemistry · doi:10.1515/bc.1999.118 · Cited by 296
The Enzymatic and DNA Binding Activity of PARP-1 Are Not Required for NF-κB Coactivator Function
Hassa, P. O., Covic, M., Hasan, S., Imhof, R., & Hottiger, M. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106528200 · Cited by 296
Self-citationAlthaus, F. R., & Richter, C. (1987) · Molecular Biology Biochemistry and Biophysics · doi:10.1007/978-3-642-83077-8 · Cited by 289
New functions of a long‐known molecule: Emerging roles of NAD in cellular signaling
Ziegler, M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01187.x · Cited by 289
Identification and Characterization of a Mammalian 39-kDa Poly(ADP-ribose) Glycohydrolase
Oka, S., Kato, J., & Moss, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510290200 · Cited by 288
Enzymology of NAD+ homeostasis in man
Magni, G., Amici, A., Emanuelli, M., Orsomando, G., Raffaelli, N., & Ruggieri, S. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-3161-1 · Cited by 288
Masutani, M., Suzuki, H., Kamada, N., Watanabe, M., Ueda, O., Nozaki, T., Jishage, K.-I., Watanabe, T., Sugimoto, T., Nakagama, H., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2301 · Cited by 286
Spindle Assembly in Animal Cells
Compton, D. A. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.95 · Cited by 284
Wang, H., Yu, S.-W., Koh, D. W., Lew, J., Coombs, C., Bowers, W., Federoff, H. J., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3461-04.2004 · Cited by 282
Gradwohl, G., Ménissier de Murcia, J. M., Molinete, M., Simonin, F., Koken, M., Hoeijmakers, J. H., & de Murcia, G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.2990 · Cited by 277
Chi, N.-W., & Lodish, H. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007635200 · Cited by 277
The role of poly(ADP-ribose) in the DNA damage signaling network
Malanga, M., & Althaus, F. R. (2005) · Biochemistry and Cell Biology · doi:10.1139/o05-038 · Cited by 275
Ju, B.-G., Solum, D., Song, E. J., Lee, K.-J., Rose, D. W., Glass, C. K., & Rosenfeld, M. G. (2004) · Cell · doi:10.1016/j.cell.2004.11.017 · Cited by 274
Resolution of Sister Telomere Association Is Required for Progression Through Mitosis
Dynek, J. N., & Smith, S. (2004) · Science · doi:10.1126/science.1094754 · Cited by 273
Multisite protein modification and intramolecular signaling
Yang, X.-J. (2005) · Oncogene · doi:10.1038/sj.onc.1208173 · Cited by 266
In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
Otto, H., Reche, P. A., Bazan, F., Dittmar, K., Haag, F., & Koch-Nolte, F. (2005) · BMC Genomics · doi:10.1186/1471-2164-6-139 · Cited by 259
Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
Chang, P., Coughlin, M., & Mitchison, T. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1322 · Cited by 259
Vaults Are Up-regulated in Multidrug-resistant Cancer Cell Lines
Kickhoefer, V. A., Rajavel, K. S., Scheffer, G. L., Dalton, W. S., Scheper, R. J., & Rome, L. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8971 · Cited by 248
Barbosa, M. T. P., Soares, S. M., Novak, C. M., Sinclair, D., Levine, J. A., Aksoy, P., & Chini, E. N. (2007) · The FASEB Journal · doi:10.1096/fj.07-8290com · Cited by 248
Stimulation of the DNA-dependent Protein Kinase by Poly(ADP-Ribose) Polymerase
Ruscetti, T., Lehnert, B. E., Halbrook, J., Le Trong, H., Hoekstra, M. F., Chen, D. J., & Peterson, S. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14461 · Cited by 248
Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains
Egloff, M.-P., Malet, H., Putics, A., Heinonen, M., Dutartre, H., Frangeul, A., Gruez, A., Campanacci, V., Cambillau, C., Ziebuhr, J., et al. (2006) · Journal of Virology · doi:10.1128/jvi.00713-06 · Cited by 243
Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo
Alvarez-Gonzalez, R., & Jacobson, M. K. (1987) · Biochemistry · doi:10.1021/bi00385a042 · Cited by 242
Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
Ruf, A., Mennissier de Murcia, J., de Murcia, G., & Schulz, G. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7481 · Cited by 241
Ikejima, M., Noguchi, S., Yamashita, R., Ogura, T., Sugimura, T., Gill, D. M., & Miwa, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45824-3 · Cited by 238
Hassa, P. O., Buerki, C., Lombardi, C., Imhof, R., & Hottiger, M. O. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307957200 · Cited by 236
Self-citationStructural basis of phosphopeptide recognition by the BRCT domain of BRCA1
Williams, R. S., Lee, M. S., Hau, D. D., & Glover, J. N. M. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb776 · Cited by 230
Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents
Alvarez-Gonzalez, R., & Althaus, F. R. (1989) · Mutation Research/DNA Repair · doi:10.1016/0921-8777(89)90012-8 · Cited by 224
PARP-1 Determines Specificity in a Retinoid Signaling Pathway via Direct Modulation of Mediator
Pavri, R., Lewis, B., Kim, T.-K., Dilworth, F. J., Erdjument-Bromage, H., Tempst, P., de Murcia, G., Evans, R., Chambon, P., & Reinberg, D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.034 · Cited by 224
Poly(ADP-ribose) Binds to Specific Domains of p53 and Alters Its DNA Binding Functions
Malanga, M., Pleschke, J. M., Kleczkowska, H. E., & Althaus, F. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11839 · Cited by 220
Kaminker, P. G., Kim, S.-H., Taylor, R. D., Zebarjadian, Y., Funk, W. D., Morin, G. B., Yaswen, P., & Campisi, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105968200 · Cited by 218
Zhu, C., Wang, X., Huang, Z., Qiu, L., Xu, F., Vahsen, N., Nilsson, M., Eriksson, P. S., Hagberg, H., Culmsee, C., et al. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402053 · Cited by 212
Isolation and Characterization of the cDNA Encoding Bovine Poly(ADP-ribose) Glycohydrolase
Lin, W., Amé, J.-C., Aboul-Ela, N., Jacobson, E. L., & Jacobson, M. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.18.11895 · Cited by 211
Interactions between BRCT repeats and phosphoproteins: tangled up in two
Glover, J. N. M., Williams, R. S., & Lee, M. S. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.09.010 · Cited by 211
TAZ Interacts with TTF-1 and Regulates Expression of Surfactant Protein-C
Park, K.-S., Whitsett, J. A., Di Palma, T., Hong, J.-H., Yaffe, M. B., & Zannini, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312569200 · Cited by 210
Meyer-Ficca, M. L., Meyer, R. G., Coyle, D. L., Jacobson, E. L., & Jacobson, M. K. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.03.050 · Cited by 209
Ditsworth, D., Zong, W.-X., & Thompson, C. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701465200 · Cited by 208
Poly(ADP-ribose) is required for spindle assembly and structure
Chang, P., Jacobson, M. K., & Mitchison, T. J. (2004) · Nature · doi:10.1038/nature03061 · Cited by 208
Kauppinen, T. M., Chan, W. Y., Suh, S. W., Wiggins, A. K., Huang, E. J., & Swanson, R. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508606103 · Cited by 207
Saikatendu, K. S., Joseph, J. S., Subramanian, V., Clayton, T., Griffith, M., Moy, K., Velasquez, J., Neuman, B. W., Buchmeier, M. J., Stevens, R. C., et al. (2005) · Structure · doi:10.1016/j.str.2005.07.022 · Cited by 204
Kolthur-Seetharam, U., Dantzer, F., McBurney, M. W., Murcia1, G. D., & Sassone-Corsi, P. (2006) · Cell Cycle · doi:10.4161/cc.5.8.2690 · Cited by 203
Smith, S., & de Lange, T. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.21.3649 · Cited by 202
Modulation of chromatin superstructure induced by poly(ADP-ribose) synthesis and degradation.
de Murcia, G., Huletsky, A., Lamarre, D., Gaudreau, A., Pouyet, J., Daune, M., & Poirier, G. G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62715-8 · Cited by 201
Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei.
Ogata, N., Ueda, K., Kawaichi, M., & Hayaishi, O. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69404-4 · Cited by 200
Ruf, A., de Murcia, G., & Schulz, G. E. (1998) · Biochemistry · doi:10.1021/bi972383s · Cited by 199
Gu, Y., Sekiguchi, J., Gao, Y., Dikkes, P., Frank, K., Ferguson, D., Hasty, P., Chun, J., & Alt, F. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.6.2668 · Cited by 198
TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex
Ye, J. Z.-S., & de Lange, T. (2004) · Nature Genetics · doi:10.1038/ng1360 · Cited by 197
Hanai, S., Kanai, M., Ohashi, S., Okamoto, K., Yamada, M., Takahashi, H., & Miwa, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2237114100 · Cited by 195
Poly(ADP-ribosyl)ated chromatin domains: access granted
Rouleau, M., Aubin, R. A., & Poirier, G. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01080 · Cited by 194
Ménissier-de Murcia, J., Molinete, M., Gradwohl, G., Simonin, F., & de Murcia, G. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90302-1 · Cited by 193
Vaults: a ribonucleoprotein particle involved in drug resistance?
Mossink, M. H., van Zon, A., Scheper, R. J., Sonneveld, P., & Wiemer, E. A. (2003) · Oncogene · doi:10.1038/sj.onc.1206947 · Cited by 187
Regulation of Poly(ADP-ribose) Polymerase-1 by DNA Structure-specific Binding
Lonskaya, I., Potaman, V. N., Shlyakhtenko, L. S., Oussatcheva, E. A., Lyubchenko, Y. L., & Soldatenkov, V. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413483200 · Cited by 186
Dantzer, F., Giraud-Panis, M.-J., Jaco, I., Amé, J.-C., Schultz, I., Blasco, M., Koering, C.-E., Gilson, E., Ménissier-de Murcia, J., de Murcia, G., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.4.1595-1607.2004 · Cited by 186
Poly(ADP-ribose) Polymerase (PARP-1) in Homologous Recombination and as a Target for Cancer Therapy
Helleday, T., Bryant, H. E., & Schultz, N. (2005) · Cell Cycle · doi:10.4161/cc.4.9.2031 · Cited by 184
A Shuttle Mechanism for DNA‐Protein Interactions: The Regulation of Poly(ADP‐ribose) Polymerase
ZAHRADKA, P., & EBISUZAKI, K. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06912.x · Cited by 182
Cherney, B. W., McBride, O. W., Chen, D. F., Alkhatib, H., Bhatia, K., Hensley, P., & Smulson, M. E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8370 · Cited by 180
Dueling Activities of AIF in Cell Death versus Survival
Lipton, S. A., & Bossy-Wetzel, E. (2002) · Cell · doi:10.1016/s0092-8674(02)01046-2 · Cited by 180
Role of Topoisomerase IIβ in the Expression of Developmentally Regulated Genes
Lyu, Y. L., Lin, C.-P., Azarova, A. M., Cai, L., Wang, J. C., & Liu, L. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00617-06 · Cited by 179
Rho-modifying C3-like ADP-ribosyltransferases
Aktories, K., Wilde, C., & Vogelsgesang, M. (2004) · Reviews of Physiology, Biochemistry and Pharmacology · doi:10.1007/s10254-004-0034-4 · Cited by 178
Lung resistance-related protein/major vault protein and vaults in multidrug-resistant cancer
Scheffer, G. L., Schroeijers, A. B., Izquierdo, M. A., Wiemer, E. A. C., & Scheper, R. J. (2000) · Current Opinion in Oncology · doi:10.1097/00001622-200011000-00007 · Cited by 176
Cortes, U., Tong, W.-M., Coyle, D. L., Meyer-Ficca, M. L., Meyer, R. G., Petrilli, V., Herceg, Z., Jacobson, E. L., Jacobson, M. K., & Wang, Z.-Q. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7163-7178.2004 · Cited by 175
Aksoy, P., Escande, C., White, T. A., Thompson, M., Soares, S., Benech, J. C., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.066 · Cited by 173
Histone shuttling by poly ADP-ribosylation
Althaus, F. R., Höfferer, L., Kleczkowska, H. E., Malanga, M., Naegeli, H., Panzeter, P. L., & Realini, C. A. (1994) · ADP-Ribosylation: Metabolic Effects and Regulatory Functions · doi:10.1007/978-1-4615-2614-8_7 · Cited by 172
Ouararhni, K., Hadj-Slimane, R., Ait-Si-Ali, S., Robin, P., Mietton, F., Harel-Bellan, A., Dimitrov, S., & Hamiche, A. (2006) · Genes & Development · doi:10.1101/gad.396106 · Cited by 172
Meder, V. S., Boeglin, M., de Murcia, G., & Schreiber, V. (2005) · Journal of Cell Science · doi:10.1242/jcs.01606 · Cited by 171
The family of toxin‐related ecto‐ADP‐ribosyltransferases in humans and the mouse
Glowacki, G., Braren, R., Firner, K., Nissen, M., Kühl, M., Reche, P., Bazan, F., Cetkovic‐Cvrlje, M., Leiter, E., Haag, F., et al. (2002) · Protein Science · doi:10.1110/ps.0200602 · Cited by 171
Role of Glutamic Acid 988 of Human Poly-ADP-ribose Polymerase in Polymer Formation
Marsischky, G. T., Wilson, B. A., & Collier, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3247 · Cited by 169
Huletsky, A., de MURCIA, G., Muller, S., Hengartner, M. O., Ménard, L., Lamarre, D., & Poirier, G. G. (1989) · PubMed · Cited by 168
Ruf, A., Rolli, V., de Murcia, G., & Schulz, G. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1673 · Cited by 164
Sbodio, J. I., & Chi, N.-W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203916200 · Cited by 162
Histone shuttling by poly(ADP-ribosylation).
Realini, C. A., & Althaus, F. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37040-1 · Cited by 160
Bonicalzi, M.-È., Haince, J.-F., Droit, A., & Poirier, G. G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4505-1 · Cited by 158
Miwa, M., Saikawa, N., Yamaizumi, Z., Nishimura, S., & Sugimura, T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.2.595 · Cited by 158
Augustin, A., Spenlehauer, C., Dumond, H., Ménissier-de Murcia, J., Piel, M., Schmit, A.-C., Apiou, F., Vonesch, J.-L., Kock, M., Bornens, M., et al. (2003) · Journal of Cell Science · doi:10.1242/jcs.00341 · Cited by 158
Domenighini, M., & Rappuoli, R. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.321396.x · Cited by 155
Kanai, M., Tong, W., Sugihara, E., Wang, Z., Fukasawa, K., & Miwa, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.7.2451-2462.2003 · Cited by 154
Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism.
Ferro, A. M., & Olivera, B. M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34453-3 · Cited by 153
Mice with bad ends: mouse models for the study of telomeres and telomerase in cancer and aging
Blasco, M. A. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600598 · Cited by 153
NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis
Chang, W., Dynek, J. N., & Smith, S. H. (2005) · Biochemical Journal · doi:10.1042/bj20050885 · Cited by 152
Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase
Uchida, K., Morita, T., Sato, T., Ogura, T., Yamashita, R., Noguchi, S., Suzuki, H., Nyunoya, H., Miwa, M., & Sügimura, T. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90921-1 · Cited by 150
Wielckens, K., Schmidt, A., George, E., Bredehorst, R., & Hilz, H. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33596-8 · Cited by 148
Nuclear Poly(ADP-ribose) Polymerase-1 Rapidly Triggers Mitochondrial Dysfunction
Cipriani, G., Rapizzi, E., Vannacci, A., Rizzuto, R., Moroni, F., & Chiarugi, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414526200 · Cited by 148
Rolli, V., O'Farrell, M. K., Murcia, J. M., & de MURCIA, G. (1997) · Biochemistry · doi:10.1021/bi971055p · Cited by 148
Seimiya, H., & Smith, S. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112266200 · Cited by 147
Host Resistance to Lung Infection Mediated by Major Vault Protein in Epithelial Cells
Kowalski, M. P., Dubouix-Bourandy, A., Bajmoczi, M., et al. (2007) · Science · doi:10.1126/science.1142311 · Cited by 147
Johansson, M. (1999) · Genomics · doi:10.1006/geno.1999.5799 · Cited by 147
AIF suppresses chemical stress‐induced apoptosis and maintains the transformed state of tumor cells
Urbano, A., Lakshmanan, U., Choo, P. H., Kwan, J., Ng, P. Y., Guo, K., Dhakshinamoorthy, S., & Porter, A. G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600746 · Cited by 139
Poly ADP-ribosylation: a histone shuttle mechanism in DNA excision repair
Us, F. R. A. (1992) · Journal of Cell Science · doi:10.1242/jcs.102.4.663 · Cited by 139
Kreimeyer, A., Wielckens, K., Adamietz, P., & Hilz, H. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43540-x · Cited by 138
Han, S., Arvai, A. S., Clancy, S., & Tainer, J. A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4292 · Cited by 138
Detection of Protein Folding Defects Caused by BRCA1-BRCT Truncation and Missense Mutations
Williams, R. S., Chasman, D. I., Hau, D., Hui, B., Lau, A. Y., & Glover, J. N. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310182200 · Cited by 138
Sbodio, J. I., Lodish, H. F., & Chi, N. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610451 · Cited by 137
Iwasaki, T., Chin, W. W., & Ko, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101517200 · Cited by 136
PARP-1, PARP-2, and the cellular response to low doses of ionizing radiation
Chalmers, A. J., Johnston, P. J., Woodcock, M., Joiner, M. C., & Marples, B. (2004) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2003.09.053 · Cited by 134
Mode of action of poly(ADP-ribose) glycohydrolase
Brochu, G., Duchaine, C., Thibeault, L., Lagueux, J., Shah, G. M., & Poirier, G. G. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90058-2 · Cited by 134
Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase
Yeh, T.-Y. J., Sbodio, J. I., Tsun, Z.-Y., Luo, B., & Chi, N. (2007) · Biochemical Journal · doi:10.1042/bj20060793 · Cited by 133
PARP‐2 deficiency affects the survival of CD4+CD8+ double‐positive thymocytes
Yélamos, J., Monreal, Y., Saenz, L., Aguado, E., Schreiber, V., Mota, R., Fuente, T., Minguela, A., Parrilla, P., de MURCIA, G., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601301 · Cited by 133
PARP‐3 associates with polycomb group bodies and with components of the DNA damage repair machinery
Rouleau, M., McDonald, D., Gagné, P., Ouellet, M. ‐., Droit, A., Hunter, J. M., Dutertre, S., Prigent, C., Hendzel, M. J., & Poirier, G. G. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21051 · Cited by 133
PolyADP-ribose polymerase is a coactivator for AP-2-mediated transcriptional activation
Kannan, P., Yu, Y., Wankhade, S., & Tainsky, M. A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.3.866 · Cited by 131
Misregulation of gene expression in primary fibroblasts lacking poly(ADP-ribose) polymerase
Simbulan-Rosenthal, C. M., Ly, D. H., Rosenthal, D. S., Konopka, G., Luo, R., Wang, Z., Schultz, P. G., & Smulson, M. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200285797 · Cited by 130
Poly(ADP-Ribose) Polymerase Impairs Early and Long-Term Experimental Stroke Recovery
Goto, S., Xue, R., Sugo, N., Sawada, M., Blizzard, K. K., Poitras, M. F., Johns, D. C., Dawson, T. M., Dawson, V. L., Crain, B. J., et al. (2002) · Stroke · doi:10.1161/01.str.0000014203.65693.1e · Cited by 129
Noncovalent interactions of poly(adenosine diphosphate ribose) with histones
Panzeter, P. L., Realini, C. A., & Althaus, F. R. (1992) · Biochemistry · doi:10.1021/bi00120a014 · Cited by 128
Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2
Oliver, A. W. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh215 · Cited by 127
Function of poly(ADP-ribose) polymerase in response to DNA damage: Gene-disruption study in mice
Masutani, M., Nozaki, T., Nishiyama, E., Shimokawa, T., Tachi, Y., Suzuki, H. I., Nakagama, H., Wakabayashi, K., & Sügimura, T. (1999) · Springer eBooks · doi:10.1007/978-1-4419-8740-2_21 · Cited by 127
Exotoxin A–eEF2 complex structure indicates ADP ribosylation by ribosome mimicry
Jørgensen, R., Merrill, A. R., Yates, S. P., Marquez, V. E., Schwan, A. L., Boesen, T., & Andersen, G. R. (2005) · Nature · doi:10.1038/nature03871 · Cited by 127
Distinct hsp70 Domains Mediate Apoptosis-inducing Factor Release and Nuclear Accumulation
Ruchalski, K. L., Mao, H., Li, Z., Wang, Z., Gillers, S., Wang, Y., Mosser, D. D., Gabai, V. L., Schwartz, J. H., & Borkan, S. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513728200 · Cited by 126
Identification of a Novel Human Tankyrase through Its Interaction with the Adaptor Protein Grb14
Lyons, R. J., Deane, R., Lynch, D. K., Ye, Z.-S. J., Sanderson, G. M., Eyre, H. J., Sutherland, G. R., & Daly, R. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009756200 · Cited by 125
Poly(ADP-ribose) polymerase-1 mediated caspase-independent cell death after ischemia/reperfusion
van Wijk, S. J. L., & Hageman, G. J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.021 · Cited by 124
van Empel, V. P. M., Bertrand, A., van der Nagel, R., Sawa Kostin, D., Doevendans, P. A., Crijns, H. J. G. M., de Wit, E., Sluiter, W. J., Ackerman, S. L., & Windt, L. J. D. (2005) · Circulation Research · doi:10.1161/01.res.0000172081.30327.28 · Cited by 121
Oei, S. L., Griesenbeck, J., Schweiger, M., & Ziegler, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31644 · Cited by 121
Developmental Changes in Histone macroH2A1-Mediated Gene Regulation
Changolkar, L. N., Costanzi, C., Leu, N. A., Chen, D., McLaughlin, K. J., & Pehrson, J. R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02334-06 · Cited by 121
Polymerization of the adenosine 5′-diphosphate ribose moiety of NAD by rat liver nuclear enzyme
Sügimura, T., Fujimura, S., Hasegawa, S., & Kawamura, Y. (1967) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(67)90507-2 · Cited by 120
ADP-ribosyltransferase from hen liver nuclei. Purification and characterization.
Tanigawa, Y., Tsuchiya, M., Imai, Y., & Shimoyama, M. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43510-1 · Cited by 119
Thorslund, T., von Kobbe, C., Harrigan, J. A., Indig, F. E., Christiansen, M., Stevnsner, T., & Bohr, V. A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.17.7625-7636.2005 · Cited by 118
Transcriptional Repression by Binding of Poly(ADP-ribose) Polymerase to Promoter Sequences
Soldatenkov, V. A., Chasovskikh, S., Potaman, V. N., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108551200 · Cited by 117
Zhang, S., Lin, Y., Kim, Y., Hande, M. P., Liu, Z., & Shen, H.-M. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402088 · Cited by 117
Zon, A., Mossink, M. H., Scheper, R. J., Sonneveld, P., & Wiemer, E. A. C. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3030-y · Cited by 117
Nusinow, D. A., Hernández‐Muñoz, I., Fazzio, T. G., Shah, G. M., Kraus, W. L., & Panning, B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610502200 · Cited by 116
Simbulan-Rosenthal, C. M., Rosenthal, D. S., Luo, R., Samara, R. N., Espinoza, L. A., Hassa, P. O., Hottiger, M. O., & Smulson, M. E. (2003) · Oncogene · doi:10.1038/sj.onc.1206897 · Cited by 115
Self-citationPillai, J. B., Gupta, M., Rajamohan, S. B., Lang, R. M., Raman, J., & Gupta, M. P. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01124.2005 · Cited by 114
Relation between carcinogenesis, chromatin structure and poly(ADP-ribosylation) (review).
Boulikas, T. (1991) · PubMed · Cited by 114
Schreiber, V., Molinete, M., Bœuf, H., de MURCIA, G., & Murcia, J. M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05404.x · Cited by 113
Ladurner, A. G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00284-3 · Cited by 113
Gagné, J., Hunter, J. M., Labrecque, B., Chabot, B., & Poirier, G. G. (2003) · Biochemical Journal · doi:10.1042/bj20021675 · Cited by 113
Saxena, A., Saffery, R., Wong, L. H., Kalitsis, P., & Choo, K. H. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200620200 · Cited by 113
Tong, W., Cortes, U., Hande, M. P., Ohgaki, H., Cavalli, L. R., Lansdorp, P. M., Haddad, B. R., & Wang, Z. (2002) · PubMed · Cited by 112
Purification and properties of poly(adenosine diphosphate ribose) synthetase.
Okayama, H., Edson, C. M., Fukushima, M., Ueda, K., & Hayaishi, O. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)66926-7 · Cited by 111
Magnitude and significance of NAD turnover in human cell line D98/AH2
Rechsteiner, M., Hillyard, D. R., & Olivera, B. M. (1976) · Nature · doi:10.1038/259695a0 · Cited by 111
Berger, F., Lau, C., & Ziegler, M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609211104 · Cited by 111
C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins
Vogelsgesang, M., Pautsch, A., & Aktories, K. (2006) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-006-0113-y · Cited by 111
Panda, S., Poirier, G. G., & Kay, S. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00200-9 · Cited by 107
Noncleavable poly(ADP-ribose) polymerase-1 regulates the inflammation response in mice
Pétrilli, V., Herceg, Z., Hassa, P. O., Patel, N. S. A., Paola, R. D., Cortes, U., Dugo, L., Mota‐Filipe, H., Thiemermann, C., Hottiger, M. O., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200421854 · Cited by 107
Self-citationOgino, H., Nozaki, T., Gunji, A., Miho, M., Suzuki, H., Ohta, T., Murakami, Y., Nakagama, H., Sügimura, T., & Masutani, M. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-227 · Cited by 105
Studies on the Polymer of Adenosine Diphosphate Ribose
Reeder, R. H., Ueda, K., Honjo, T., Nishizuka, Y., & Hayaishi, O. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95948-x · Cited by 104
The effect of gamma radiation and neocarzinostatin of NAD and ATP levels in mouse leukaemia cells
Goodwin, P. M., Lewis, P. J., DAVIES, M. I., SKIDMORE, C. J., & Shall, S. (1978) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(78)90312-4 · Cited by 104
Desmarais, Y., Ménard, L., Lagueux, J., & Poirier, G. G. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)99007-f · Cited by 103
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Metadata
- Authors
- Hassa, P.
- Venue
- Frontiers in Bioscience
- Publisher
- IMR Press
- Published
- 2008
- Volume
- 13
- Issue
- 13
- Pages
- 3046
- ISSN
- 1093-4715 (ISSN-L)
- 1093-9946
- DOI
- 10.2741/2909
- OpenAlex
- W1825629489
- Cited by
- 584
- References
- 314
- FWCI
- 14.34
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.