Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation

Wnt/β-Catenin Signaling: Components, Mechanisms, and Diseases

MacDonald, B. T., Tamai, K., & He, X. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.016 · Cited by 5,583 · see citing works

The unfolded protein response: controlling cell fate decisions under ER stress and beyond

Hetz, C. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3270 · Cited by 4,118 · see citing works

Poly(ADP-ribose): novel functions for an old molecule

Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,917 · see citing works

Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family

Filippakopoulos, P., Picaud, S., Mangos, M., Keates, T., Lambert, J., Baršytė-Lovejoy, D., Felletár, I., Volkmer, R., Müller, S., Pawson, T. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.013 · Cited by 1,719 · see citing works

New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs

Gibson, B. A., & Kraus, W. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3376 · Cited by 1,226 · see citing works

Role of poly(ADP-ribose) formation in DNA repair

Satoh, M. S., & Lindahl, T. L. (1992) · Nature · doi:10.1038/356356a0 · Cited by 1,181 · see citing works

GSK3: a multifaceted kinase in Wnt signaling

Wu, D., & Pan, W. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.10.002 · Cited by 862 · see citing works

Toward a unified nomenclature for mammalian ADP-ribosyltransferases

Hottiger, M. O., Hassa, P. O., Lüscher, B., Schuler, H., & Koch‐Nolte, F. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.12.003 · Cited by 814 · see citing works

Poly(ADP-ribose)–Dependent Regulation of DNA Repair by the Chromatin Remodeling Enzyme ALC1

Ahel, D., Hořejší, Z., Wiechens, N., Polo, S. E., Garcia-Wilson, E., Ahel, I., Flynn, H., Skehel, M., West, S. C., Jackson, S. P., et al. (2009) · Science · doi:10.1126/science.1177321 · Cited by 588 · see citing works

Comparative genomics and evolution of proteins involved in RNA metabolism

Anantharaman, V. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.7.1427 · Cited by 541 · see citing works

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 536 · see citing works

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 502 · see citing works

Poly(ADP-ribose) (PAR) binding to apoptosis-inducing factor is critical for PAR polymerase-1-dependent cell death (parthanatos)

Wang, Y., Kim, N. S., Haince, J.-F., Kang, H. C., David, K. K., Andrabi, S. A., Poirier, G. G., Dawson, V. L., & Dawson, T. M. (2011) · Science Signaling · doi:10.1126/scisignal.2000902 · Cited by 476 · see citing works

RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling

Zhang, Y., Liu, S., Mickanin, C., Feng, Y., Charlat, O., Michaud, G. A., Schirle, M., Shi, X., Hild, M., Bauer, A., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2222 · Cited by 431 · see citing works

Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins

Ahel, I., Ahel, D., Matsusaka, T., Clark, A. J., Pines, J., Boulton, S. J., & West, S. C. (2008) · Nature · doi:10.1038/nature06420 · Cited by 429 · see citing works

Ubiquitination in signaling to and activation of IKK

Chen, Z. J. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01108.x · Cited by 419 · see citing works

A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation

Timinszky, G., Till, S., Hassa, P. O., Hothorn, M., Kustatscher, G., Nijmeijer, B., Colombelli, J., Altmeyer, M., Stelzer, E. H. K., Scheffzek, K., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1664 · Cited by 416 · see citing works

Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes

Gagné, J., Isabelle, M., Lo, K. S., Bourassa, S., Hendzel, M. J., Dawson, V. L., Dawson, T. M., & Poirier, G. G. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn771 · Cited by 416 · see citing works

The histone variant macroH2A suppresses melanoma progression through regulation of CDK8

Kapoor, A., Goldberg, M. S., Cumberland, L., Ratnakumar, K., Segura, M. F., Emanuel, P. O., Menéndez, S., Vardabasso, C., LeRoy, G., Vidal, C. I., et al. (2010) · Nature · doi:10.1038/nature09590 · Cited by 401 · see citing works

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

Slade, D., Dunstan, M. S., Barkauskaite, E., Weston, R., Lafite, P., Dixon, N., Ahel, M., Leys, D., & Ahel, I. (2011) · Nature · doi:10.1038/nature10404 · Cited by 385 · see citing works

Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler

Gottschalk, A. J., Timinszky, G., Kong, S. E., Jin, J., Cai, Y., Swanson, S. K., Washburn, M. P., Florens, L. A., Ladurner, A. G., Conaway, J. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906920106 · Cited by 358 · see citing works

MacroH2A, a Core Histone Containing a Large Nonhistone Region

Pehrson, J. R., & Fried, V. A. (1992) · Science · doi:10.1126/science.1529340 · Cited by 343 · see citing works

Substrate-Assisted Catalysis by PARP10 Limits Its Activity to Mono-ADP-Ribosylation

Kleine, H., Poręba, E., Leśniewicz, K., Hassa, P. O., Hottiger, M. O., Litchfield, D. W., Shilton, B. H., & Lüscher, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.009 · Cited by 340 · see citing works

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation

Jankevicius, G., Hassler, M., Golia, B., Rybin, V., Zacharias, M., Timinszky, G., & Ladurner, A. G. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2523 · Cited by 330 · see citing works

Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

Altmeyer, M., Messner, S., Hassa, P. O., Fey, M., & Hottiger, M. O. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp229 · Cited by 325 · see citing works

Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases

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) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2521 · Cited by 317 · see citing works

Deficiency of terminal ADP‐ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease

Sharifi, R., Morra, R., Appel, C. D., Tallis, M., Chioza, B. A., Jankevicius, G., Simpson, M. A., Matić, I., Sackey, E., Golia, B., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.51 · Cited by 306 · see citing works

Splicing regulates NAD metabolite binding to histone macroH2A

Kustatscher, G., Hothorn, M., Pugieux, C., Scheffzek, K., & Ladurner, A. G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb956 · Cited by 300 · see citing works

Functional aspects of protein mono‐ADP‐ribosylation

Corda, D., & Girolamo, M. D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg209 · Cited by 294 · see citing works

Identification and Characterization of a Mammalian 39-kDa Poly(ADP-ribose) Glycohydrolase

Oka, S., Kato, J., & Moss, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510290200 · Cited by 290 · see citing works

PARP1 ADP-ribosylates lysine residues of the core histone tails

Messner, S., Altmeyer, M., Zhao, H., Pozivil, A., Roschitzki, B., Gehrig, P., Rutishauser, D., Danzhi Huang, A., Caflisch, A., & Hottiger, M. O. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq463 · Cited by 264 · see citing works

In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)

Otto, H., Reche, P. A., Bazán, F., Dittmar, K., Haag, F., & Koch‐Nolte, F. (2005) · BMC Genomics · doi:10.1186/1471-2164-6-139 · Cited by 259 · see citing works

PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1

Pines, A., Vrouwe, M. G., Marteijn, J. A. F., Typas, D., Luijsterburg, M. S., Cansoy, M., Hensbergen, P. J., Deelder, A. M., de Groot, A., Matsumoto, S., et al. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201112132 · Cited by 255 · see citing works

Tankyrase function at telomeres, spindle poles, and beyond

Hsiao, S. J., & Smith, S. H. (2007) · Biochimie · doi:10.1016/j.biochi.2007.07.012 · Cited by 249 · see citing works

Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains

Egloff, M. P., Malet, H., Putics, Á., 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 · see citing works

The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation

Aravind, L. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01787-x · Cited by 232 · see citing works

Ubiquitin Ligase RNF146 Regulates Tankyrase and Axin to Promote Wnt Signaling

Callow, M. G., Tran, H., Phu, L., Lau, T., Lee, J., Sandoval, W. N., Liu, P. S., Bheddah, S., Tao, J., Lill, J. R., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022595 · Cited by 217 · see citing works

Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3

Saikatendu, K. S., Joseph, J. S., Subramanian, V., Clayton, T., Griffith, M. T., 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 201 · see citing works

PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response

Jwa, M., & Chang, P. (2012) · Nature Cell Biology · doi:10.1038/ncb2593 · Cited by 191 · see citing works

Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II

Yang, J., Aittomäki, S., Pesu, M., Carter, K. L., Saarinen, J., Kalkkinen, N., Kieff, E. D., & Silvennoinen, O. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf463 · Cited by 191 · see citing works

Differential Activities of Cellular and Viral Macro Domain Proteins in Binding of ADP-Ribose Metabolites

Neuvonen, M., & Ahola, T. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.045 · Cited by 191 · see citing works

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

MacPherson, L., Tamblyn, L., Rajendra, S., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1337 · Cited by 179 · see citing works

Histone macroH2A isoforms predict the risk of lung cancer recurrence

Sporn, J. C., Kustatscher, G., Hothorn, T., Collado, M., Serrano, M., Muley, T., Schnabel, P. A., & Ladurner, A. G. (2009) · Oncogene · doi:10.1038/onc.2009.26 · Cited by 176 · see citing works

Reprogramming cellular events by poly(ADP-ribose)-binding proteins

Krietsch, J., Rouleau, M., Pic, É., Ethier, C., Dawson, T. M., Dawson, V. L., Masson, J., Poirier, G. G., & Gagné, J. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.005 · Cited by 171 · see citing works

Identification of Macrodomain Proteins as Novel O-Acetyl-ADP-ribose Deacetylases

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) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.206771 · Cited by 170 · see citing works

Identification of the ADP-Ribosylation Sites in the PARP-1 Automodification Domain: Analysis and Implications

Tao, Z., Gao, P., & Liu, H. (2009) · Journal of the American Chemical Society · doi:10.1021/ja906135d · Cited by 166 · see citing works

Quantitative proteomics profiling of the poly(ADP-ribose)-related response to genotoxic stress

Gagné, J., Pic, É., Isabelle, M., Krietsch, J., Éthier, C., Paquet, É. R., Kelly, I., Boutin, M., Moon, K., Foster, L. J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks486 · Cited by 165 · see citing works

B-aggressive Lymphoma Family Proteins Have Unique Domains That Modulate Transcription and Exhibit Poly(ADP-ribose) Polymerase Activity

Aguiar, R. C. T., Takeyama, K., He, C., Kreinbrink, K., & Shipp, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505408200 · Cited by 161 · see citing works

Regulation of NF-κB signalling by the mono-ADP-ribosyltransferase ARTD10

Verheugd, P., Forst, A. H., Milke, L., Herzog, N., Feijs, K. L. H., Kremmer, E., Kleine, H. O., & Lüscher, B. (2013) · Nature Communications · doi:10.1038/ncomms2672 · Cited by 160 · see citing works

ADP-Ribose-1"-Monophosphatase: a Conserved Coronavirus Enzyme That Is Dispensable for Viral Replication in Tissue Culture

Putics, Á., Filipowicz, W., Hall, J., Gorbalenya, A. E., & Ziebuhr, J. (2005) · Journal of Virology · doi:10.1128/jvi.79.20.12721-12731.2005 · Cited by 160 · see citing works

PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

Yu, M., Schreek, S., Cerni, C., Schamberger, C. J., Leśniewicz, K., Poręba, E., Vervoorts, J., Walsemann, G., Grötzinger, J., Kremmer, E., et al. (2005) · Oncogene · doi:10.1038/sj.onc.1208410 · Cited by 156 · see citing works

The BAL-binding Protein BBAP and Related Deltex Family Members Exhibit Ubiquitin-Protein Isopeptide Ligase Activity

Takeyama, K., Aguiar, R. C. T., Gu, L., He, C., Freeman, G. J., Kutok, J. L., Aster, J. C., & Shipp, M. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301157200 · Cited by 152 · see citing works

Isolation and characterization of a novel oncogene, amplified in liver cancer 1, within a commonly amplified region at 1q21 in hepatocellular carcinoma

Ma, N., Hu, L., Fung, J. M.-W., Xie, D., Zheng, B., Chen, L., Tang, D., Fu, L., Wu, Z., Chen, M., et al. (2007) · Hepatology · doi:10.1002/hep.22072 · Cited by 151 · see citing works

A family of killer toxins

Holbourn, K. P., Shone, C. C., & Acharya, K. R. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05442.x · Cited by 147 · see citing works

PARP-14 Functions as a Transcriptional Switch for Stat6-dependent Gene Activation

Mehrotra, P., Riley, J. P., Patel, R. J., Li, F., Voss, L., & Goenka, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157768 · Cited by 146 · see citing works

Viral manipulation of DNA repair and cell cycle checkpoints

Chaurushiya, M. S., & Weitzman, M. (2009) · DNA Repair · doi:10.1016/j.dnarep.2009.04.016 · Cited by 137 · see citing works

BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration

Aguiar, R. C. T., Yakushijin, Y., Kharbanda, S., Salgia, R., Fletcher, J. A., & Shipp, M. A. (2000) · Blood · doi:10.1182/blood.v96.13.4328 · Cited by 133 · see citing works

The Crystal Structure of AF1521 a Protein from Archaeoglobus fulgidus with Homology to the Non-histone Domain of MacroH2A

Allen, M. D., Buckle, A. M., Cordell, S. C., Löwe, J., & Bycroft, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00473-x · Cited by 130 · see citing works

Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains

Forst, A. H., Karlberg, T., Herzog, N., Thorsell, A. G., Groß, A., Feijs, K. L. H., Verheugd, P., Kursula, P., Nijmeijer, B., Kremmer, E., et al. (2013) · Structure · doi:10.1016/j.str.2012.12.019 · Cited by 129 · see citing works

The macro domain protein family: Structure, functions, and their potential therapeutic implications

Han, W., Li, X., & Fu, X. (2011) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2011.03.001 · Cited by 125 · see citing works

BAL1 and Its Partner E3 Ligase, BBAP, Link Poly(ADP-Ribose) Activation, Ubiquitylation, and Double-Strand DNA Repair Independent of ATM, MDC1, and RNF8

Yan, Q., Xu, R., Zhu, L., Cheng, X., Wang, Z., Manis, J. P., & Shipp, M. A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00990-12 · Cited by 122 · see citing works

ARTD10 substrate identification on protein microarrays: regulation of GSK3β by mono-ADP-ribosylation

Feijs, K. L. H., Kleine, H. O., Braczynski, A. K., Forst, A. H., Herzog, N., Verheugd, P., Linzen, U., Kremmer, E., & Lüscher, B. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-5 · Cited by 121 · see citing works

The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice

Park, E., & Griffin, D. E. (2009) · Virology · doi:10.1016/j.virol.2009.03.031 · Cited by 116 · see citing works

Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose

Tong, L., & Denu, J. M. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.02.007 · Cited by 115 · see citing works

The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O- acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases

Ono, T., Kasamatsu, A., Oka, S., & Moss, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607911103 · Cited by 112 · see citing works

Stealth and mimicry by deadly bacterial toxins

Yates, S. P., Jørgensen, R., Andersen, G. R., et al. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.12.007 · Cited by 112 · see citing works

The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation

Mueller‐Dieckmann, C., Kernstock, S., Lisurek, M., von Kries, J. P., Haag, F., Weiss, M. S., & Koch‐Nolte, F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606762103 · Cited by 112 · see citing works

Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome

Dani, N., Stilla, A., Marchegiani, A., Tamburro, A., Till, S., Ladurner, A. G., Corda, D., & Girolamo, M. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900066106 · Cited by 108 · see citing works

Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor

Goenka, S., & Boothby, M. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506981103 · Cited by 108 · see citing works

PARP-14, a member of the B aggressive lymphoma family, transduces survival signals in primary B cells

Cho, S. H., Goenka, S., Henttinen, T. A., Gudapati, P., Reinikainen, A., Eischen, C. M., Lahesmaa, R., & Boothby, M. R. (2009) · Blood · doi:10.1182/blood-2008-03-144121 · Cited by 106 · see citing works

Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase

Dunstan, M. S., Barkauskaite, E., Lafite, P., Knezevic, C. E., Brassington, A., Ahel, M., Hergenrother, P. J., Leys, D., & Ahel, I. (2012) · Nature Communications · doi:10.1038/ncomms1889 · Cited by 94 · see citing works

Collaborator of Stat6 (CoaSt6)-associated Poly(ADP-ribose) Polymerase Activity Modulates Stat6-dependent Gene Transcription

Goenka, S., Cho, S. H., & Boothby, M. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611283200 · Cited by 93 · see citing works

Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response

Li, G., McCulloch, R. D., Fenton, A. L., Cheung, M., Meng, L., Ikura, M., & Koch, C. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000556107 · Cited by 93 · see citing works

Poly (ADP-ribose) polymerase 14 and its enzyme activity regulates TH2 differentiation and allergic airway disease

Mehrotra, P., Hollenbeck, A. N., Riley, J. P., Li, F., Patel, R. J., Akhtar, N., & Goenka, S. (2012) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2012.06.015 · Cited by 85 · see citing works

Mapping PARP-1 Auto-ADP-ribosylation Sites by Liquid Chromatography–Tandem Mass Spectrometry

Chapman, J. D., Gagné, J., Poirier, G. G., & Goodlett, D. R. (2013) · Journal of Proteome Research · doi:10.1021/pr301219h · Cited by 85 · see citing works

PARP16/ARTD15 Is a Novel Endoplasmic-Reticulum-Associated Mono-ADP-Ribosyltransferase That Interacts with, and Modifies Karyopherin-ß1

Paola, S. D., Micaroni, M., Tullio, G. D., Buccione, R., & Girolamo, M. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037352 · Cited by 84 · see citing works

New readers and interpretations of poly(ADP-ribosyl)ation

Kalisch, T., Amé, J., Dantzer, F., & Schreiber, V. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.06.001 · Cited by 83 · see citing works

Orphan Macrodomain Protein (Human C6orf130) Is an O-Acyl-ADP-ribose Deacylase

Peterson, F. C., Chen, D., Lytle, B. L., Rossi, M. N., Ahel, I., Denu, J. M., & Volkman, B. F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276238 · Cited by 80 · see citing works

Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain

Patel, C. N., Koh, D. W., Jacobson, M. K., et al. (2005) · Biochemical Journal · doi:10.1042/bj20040942 · Cited by 77 · see citing works

Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes

Moss, J., Oppenheimer, N. J., West, R. E., et al. (1986) · Biochemistry · doi:10.1021/bi00367a010 · Cited by 77 · see citing works

Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element

Kim, I., Kiefer, J. R., Ho, C. M. W., Stegeman, R. A., Classen, S., Tainer, J. A., & Ellenberger, T. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2305 · Cited by 68 · see citing works

Sensing NAD metabolites through macro domains

Till, S. (2009) · Frontiers in bioscience · doi:10.2741/3448 · Cited by 61 · see citing works

Double-stranded DNA Binding Domain of Poly(ADP-ribose) Polymerase-1 and Molecular Insight into the Regulation of Its Activity

Huambachano, O., Herrera, F., Rancourt, A., & Satoh, M. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175190 · Cited by 61 · see citing works

Dynamic subcellular localization of the mono-ADP-ribosyltransferase ARTD10 and interaction with the ubiquitin receptor p62

Kleine, H. O., Herrmann, A., Lamark, T., Forst, A. H., Verheugd, P., Lüscher‐Firzlaff, J., Lippok, B. E., Feijs, K. L. H., Herzog, N., Kremmer, E., et al. (2012) · Cell Communication and Signaling · doi:10.1186/1478-811x-10-28 · Cited by 61 · see citing works

Caspase‐dependent cleavage of the mono‐ ADP ‐ribosyltransferase ARTD 10 interferes with its pro‐apoptotic function

Herzog, N., Hartkamp, J., Verheugd, P., et al. (2013) · FEBS Journal · doi:10.1111/febs.12124 · Cited by 58 · see citing works

A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae

Shull, N. P. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki211 · Cited by 58 · see citing works

Structures of the Human Poly (ADP-Ribose) Glycohydrolase Catalytic Domain Confirm Catalytic Mechanism and Explain Inhibition by ADP-HPD Derivatives

Tucker, J. A., Bennett, N. J., Brassington, C., Durant, S. T., Hassall, G., Holdgate, G. A., McAlister, M. S. B., Nissink, J. W. M., Truman, C., & Watson, M. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050889 · Cited by 56 · see citing works

Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation

Haenni, S. S., Hassa, P. O., Altmeyer, M., Fey, M., Imhof, R., & Hottiger, M. O. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.03.008 · Cited by 54 · see citing works

Molecular Insights into Poly(ADP-ribose) Recognition and Processing

Žaja, R., Mikoč, A., Barkauskaite, E., & Ahel, I. (2012) · Biomolecules · doi:10.3390/biom3010001 · Cited by 53 · see citing works

Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage

Haince, J.-F., Ouellet, M. ‐., McDonald, D., Hendzel, M. J., & Poirier, G. G. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.11.015 · Cited by 51 · see citing works

Learning How to Read ADP-Ribosylation

Kleine, H. O., & Lüscher, B. (2009) · Cell · doi:10.1016/j.cell.2009.09.018 · Cited by 50 · see citing works

CHD1L: a new candidate gene for congenital anomalies of the kidneys and urinary tract (CAKUT)

Brockschmidt, A., Chung, B. H., Weber, S., Fischer, D., Kolatsi‐Joannou, M., Christ, L., Heimbach, A., Shtiza, D., Klaus, G., Simonetti, G., et al. (2011) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfr649 · Cited by 46 · see citing works

Glutamyl ribose 5-phosphate storage disease. A hereditary defect in the degradation of poly(ADP-ribosylated) proteins.

Williams, J., Chambers, J. P., & Liehr, J. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43562-9 · Cited by 42 · see citing works

Progress in the Function and Regulation of ADP-RibosylationA report on the 18th International Conference on ADP-Ribosylation, Zurich, Switzerland, 18 to 21 August 2010.

Hottiger, M. O., Boothby, M. R., Koch‐Nolte, F., et al. (2011) · Science Signaling · doi:10.1126/scisignal.2001645 · Cited by 33 · see citing works

Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain

Karlberg, T., Thorsell, A. G., Kallas, Å., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.379289 · Cited by 25 · see citing works

Progressive Neurologic Deterioration and Renal Failure Due to Storage of Glutamyl Ribose-5-Phosphate

Williams, J. C., Butler, I. J., Rosenberg, H. S., et al. (1984) · New England Journal of Medicine · doi:10.1056/nejm198407193110305 · Cited by 16 · see citing works

Identification of common genetic risk variants for autism spectrum disorder

Autism Spectrum Disorder Working Group of the Psychiatric Genomics Consortium, Grove, J., BUPGEN, Major Depressive Disorder Working Group of the Psychiatric Genomics Consortium, 23andMe Research Team, Ripke, S., Als, T. D., Mattheisen, M., Walters, R. K., Won, H., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0344-8 · Cited by 2,421 · see citing works

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes

Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681 · see citing works

NAD+ homeostasis in health and disease

Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works

PARPs

Leung, A. K. L. (2017) · Current Biology · doi:10.1016/j.cub.2017.09.054 · Cited by 44 · see citing works

Labile intracellular zinc is associated with 3T3 cell growth

Paski, S., & Xu, Z. (2001) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(01)00188-7 · Cited by 33 · see citing works

Intracellular pH of the turtle bladder assessed with fluorescent probes.

Arruda, J. A. L., Wheeler, R. P., Dytko, G. M., et al. (1987) · PubMed · Cited by 1 · see citing works

Intracellular Na+ and Ca2+ activities in aortic smooth muscle cells from spontaneously hypertensive rats

Zidek, W., Losse, H., Grünwald, J., et al. (1982) · Research in Experimental Medicine · doi:10.1007/bf01851193 · Cited by 7 · see citing works

Radiosensitizer-DNA interactions in relation to intracellular uptake

Stratford, M. R. L., Dennis, M. F., Watts, M. E., et al. (1989) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/0360-3016(89)90904-8 · Cited by 21 · see citing works

Possible coexistence of two independent mechanisms contributing to anthracycline resistance in leukaemia P388 cells

Soto, F., Planells‐Cases, R., Cánaves, J. M., et al. (1993) · European Journal of Cancer · doi:10.1016/0959-8049(93)90050-p · Cited by 15 · see citing works