PARPs

PARP inhibitors: Synthetic lethality in the clinic

Lord, C. J., & Ashworth, A. (2017) · Science · doi:10.1126/science.aam7344 · Cited by 2,932 · 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

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

Family-wide analysis of poly(ADP-ribose) polymerase activity

Vyas, S., Matić, I., Uchima, L., Rood, J., Žaja, R., Hay, R. T., Ahel, I., & Chang, P. (2014) · Nature Communications · doi:10.1038/ncomms5426 · Cited by 503 · see citing works

Biosensor reveals multiple sources for mitochondrial NAD ⁺

Cambronne, X. A., Stewart, M. L., Kim, D., Jones-Brunette, A. M., Morgan, R. K., Farrens, D. L., Cohen, M. S., & Goodman, R. H. (2016) · Science · doi:10.1126/science.aad5168 · Cited by 407 · see citing works

Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors

Thorsell, A. G., Ekblad, T., Karlberg, T., Löw, M., Pinto, A. F., Tresaugues, L., Moche, M., Cohen, M. S., & Schuler, H. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00990 · Cited by 369 · see citing works

Opportunities for the repurposing of PARP inhibitors for the therapy of non‐oncological diseases

Berger, N. A., Besson, V. C., Boulares, A. H., Bürkle, A., Chiarugi, A., Clark, R. S. B., Curtin, N. J., Cuzzocrea, S., Dawson, T. M., Dawson, V. L., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13748 · Cited by 212 · see citing works

Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9

Yang, C., Jividen, K., Spencer, A., Dworak, N. M., Li, N., Oostdyk, L. T., Chatterjee, M., Kuśmider, B., Reon, B. J., Parlak, M., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.028 · Cited by 205 · see citing works

The Promise of Proteomics for the Study of ADP-Ribosylation

Daniels, C. M., Ong, S., & Leung, A. K. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.012 · Cited by 196 · see citing works

Rapid Evolution of PARP Genes Suggests a Broad Role for ADP-Ribosylation in Host-Virus Conflicts

Daugherty, M. D., Young, J. M., Kerns, J. A., & Malik, H. S. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004403 · Cited by 176 · see citing works

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

Feijs, K. L. H., Forst, A. H., Verheugd, P., & Lüscher, B. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3601 · Cited by 154 · see citing works

ADP ‐ribosylation: new facets of an ancient modification

Palazzo, L., Mikoč, A., & Ahel, I. (2017) · FEBS Journal · doi:10.1111/febs.14078 · Cited by 145 · see citing works

The recognition and removal of cellular poly( ADP ‐ribose) signals

Barkauskaite, E., Jankevicius, G., Ladurner, A. G., Ahel, I., & Timinszky, G. (2013) · FEBS Journal · doi:10.1111/febs.12358 · Cited by 124 · see citing works

ADPriboDB: The database of ADP-ribosylated proteins

Vivelo, C. A., Wat, R., Agrawal, C., Tee, H. Y., & Leung, A. K. L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw706 · Cited by 67 · see citing works

NAD+ in Brain Aging and Neurodegenerative Disorders

Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790 · see citing works

Biological Properties of Vitamins of the B-Complex, Part 1: Vitamins B1, B2, B3, and B5

Hrubša, M., Siatka, T., Najmanová, I., Vopršalová, M., Krčmová, L. K., Matoušová, K., Javorská, L., Macáková, K., Mercolini, L., Remião, F., et al. (2022) · Nutrients · doi:10.3390/nu14030484 · Cited by 277 · see citing works

NAD+ homeostasis in human health and disease

Perez, R. Z., Wanders, R. J. A., van Karnebeek, C., & Houtkooper, R. H. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202113943 · Cited by 238 · see citing works

Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation

Buch-Larsen, S. C., Hendriks, I. A., Lyon, D. B., Jensen, L. J., & Nielsen, M. L. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.083 · Cited by 179 · see citing works

Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation

O’Sullivan, J. A., Ferreira, M. T., Gagné, J., Sharma, A. K., Hendzel, M. J., Masson, J., & Poirier, G. G. (2019) · Nature Communications · doi:10.1038/s41467-019-08859-x · Cited by 161 · see citing works

Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation

Leung, A. K. L. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.02.002 · Cited by 153 · see citing works

PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasisPreprint

Kim, D.-S., Challa, S., Jones, A., & Kraus, W. L. (2020) · Genes & Development · doi:10.1101/gad.334433.119 · Cited by 143 · see citing works

Preclinical and clinical evidence of NAD+ precursors in health, disease, and ageing

Reiten, O. K., Wilvang, M. A., Mitchell, S. J., Hu, Z., & Fang, E. F. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111567 · Cited by 133 · see citing works

A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules

Millar, S. R., Huang, J. Q., Schreiber, K. J., Tsai, Y.-C., Won, J., Zhang, J., Moses, A. M., & Youn, J. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00608 · Cited by 120 · see citing works

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

Hopp, A.-K., Grüter, P., & Hottiger, M. O. (2019) · Cells · doi:10.3390/cells8080890 · Cited by 107 · see citing works

The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome

Hendriks, I. A., Buch-Larsen, S. C., Prokhorova, E. A., Elsborg, J. D., Rebak, A. K. L. F. S., Zhu, K., Ahel, D., Lukas, C., Ahel, I., & Nielsen, M. L. (2021) · Nature Communications · doi:10.1038/s41467-021-26172-4 · Cited by 97 · see citing works

Poly(ADP-ribosylation) of P-TEFb by PARP1 disrupts phase separation to inhibit global transcription after DNA damage

Fu, H., Liu, R., Jia, Z., Li, R., Zhu, F., Zhu, W., Shao, Y., Jin, Y., Xue, Y., Huang, J., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00872-5 · Cited by 83 · see citing works

Reduced nicotinamide mononucleotide is a new and potent NAD + precursor in mammalian cells and mice

Perez, R. Z., Tammaro, A., Schomakers, B. V., Scantlebery, A. M. L., Denis, S. W., Elfrink, H. L., Giroud‐Gerbetant, J., Cantó, C., López‐Leonardo, C., McIntyre, R. L., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202001826r · Cited by 75 · see citing works

PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response

Aberle, L., Krüger, A., Reber, J. M., Lippmann, M., Hufnagel, M., Schmalz, M. F., Trussina, I. R. E. A., Schlesiger, S., Zubel, T., Schütz, K., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa590 · Cited by 72 · see citing works

The therapeutic perspective of NAD+ precursors in age-related diseases

Iqbal, T., & Nakagawa, T. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.149590 · Cited by 65 · see citing works

PGC-1α, Sirtuins and PARPs in Huntington’s Disease and Other Neurodegenerative Conditions: NAD+ to Rule Them All

Lloret, A., & Beal, M. F. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02809-1 · Cited by 52 · see citing works

Enabling drug discovery for the PARP protein family through the detection of mono-ADP-ribosylation

Lu, A. Z., Abo, R., Ren, Y., Gui, B., Mo, J.-R., Blackwell, D. J., Wigle, T. J., Keilhack, H., & Niepel, M. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.05.007 · Cited by 50 · see citing works

Roles of NAD+ in Acute and Chronic Kidney Diseases

Morevati, M., Fang, E. F., Mace, M. L., Kanbay, M., Gravesen, E., Nordholm, A., Egstrand, S., & Hornum, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010137 · Cited by 49 · see citing works

Neuroprotective Effects of PARP Inhibitors in Drosophila Models of Alzheimer’s Disease

Maggiore, A., Casale, A. M., Toscanelli, W., Cappucci, U., Rotili, D., Grieco, M., Gagné, J.-P., Poirier, G. G., d’Erme, M., & Piacentini, L. (2022) · Cells · doi:10.3390/cells11081284 · Cited by 40 · see citing works

NAD+ centric mechanisms and molecular determinants of skeletal muscle disease and aging

Wagner, S., Manickam, R., Brotto, M. A. P., & Tipparaju, S. M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04408-1 · Cited by 39 · see citing works

PARP1 regulates DNA damage-induced nucleolar-nucleoplasmic shuttling of WRN and XRCC1 in a toxicant and protein-specific manner

Veith, S., Schink, A., Engbrecht, M., Mack, M., Rank, L., Rossatti, P., Hakobyan, M., Goly, D., Hefele, T., Frensch, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-46358-7 · Cited by 36 · see citing works

Sirtuins and Resveratrol in Cardiorenal Diseases: A Narrative Review of Mechanisms and Therapeutic Potential

Carollo, C., Sorce, A., Cirafici, E., Mulè, G., & Caimi, G. (2025) · Nutrients · doi:10.3390/nu17071212 · Cited by 27 · see citing works

Temporal and Site-Specific ADP-Ribosylation Dynamics upon Different Genotoxic Stresses

Buch-Larsen, S. C., Rebak, A. K. L. F. S., Hendriks, I. A., & Nielsen, M. L. (2021) · Cells · doi:10.3390/cells10112927 · Cited by 24 · see citing works

Influence of chain length and branching on poly(ADP-ribose)–protein interactions

Löffler, T., Krüger, A., Zirak, P., Winterhalder, M., Müller, A.-L., Fischbach, A., Mangerich, A., & Zumbusch, A. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1235 · Cited by 23 · see citing works

Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation

Bashyal, A., & Brodbelt, J. S. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21811 · Cited by 22 · see citing works

Functional Roles of Poly(ADP-Ribose) in Stress Granule Formation and Dynamics

Jin, X., Cao, X., Liu, S., & Liu, B. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.671780 · Cited by 17 · see citing works

Structural analyses of NudT16–ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins

Thirawatananond, P., McPherson, R. L., Malhi, J. K., Nathan, S., Lambrecht, M. J., Brichacek, M. P., Hergenrother, P. J., Leung, A. K. L., & Gabelli, S. B. (2019) · Scientific Reports · doi:10.1038/s41598-019-39491-w · Cited by 16 · see citing works

Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases

Vainonen, J. P., Gossens, R., Krasensky-Wrzaczek, J., Masi, R. D., Danciu, I., Puukko, T., Battchikova, N., Jonak, C., Wirthmueller, L., Wrzaczek, M., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04794-2 · Cited by 15 · see citing works

The dynamic process of covalent and non-covalent PARylation in the maintenance of genome integrity: a focus on PARP inhibitors

Beneyton, A., Nonfoux, L., Gagné, J., Rodrigue, A., Kothari, C., Atalay, N., Hendzel, M. J., Poirier, G. G., & Masson, J. (2023) · NAR Cancer · doi:10.1093/narcan/zcad043 · Cited by 13 · see citing works

Poly (ADP-ribose) polymerase 1 promotes HuR/ELAVL1 cytoplasmic localization and inflammatory gene expression by regulating p38 MAPK activity

Fu, X., Zhang, J., Sun, K., Zhang, M., Wang, S., Yuan, M., Liu, W., Zeng, X., Ba, X., & Ke, Y. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05292-2 · Cited by 12 · see citing works

Targeting selective inhibitors of PARPs in drug discovery and development

Duan, M., Gao, J., Li, J., Huang, X., Ren, Y., Li, Y., Liao, M., & Zhang, Y. (2024) · Medicinal Chemistry Research · doi:10.1007/s00044-024-03282-4 · Cited by 9 · see citing works

Assay technologies facilitating drug discovery for ADP‐ribosyl writers, readers and erasers

Glumoff, T., Sowa, S. T., & Lehtiö, L. (2021) · BioEssays · doi:10.1002/bies.202100240 · Cited by 9 · see citing works

Arabidopsis poly(ADP-ribose)-binding protein RCD1 interacts with Photoregulatory Protein Kinases in nuclear bodiesPreprint

Vainonen, J. P., Shapiguzov, A., Krasensky-Wrzaczek, J., Gossens, R., Masi, R. D., Danciu, I., Puukko, T., Battchikova, N., Jonak, C., Wirthmueller, L., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.02.184937 · Cited by 9 · see citing works

PARP12 regulates mouse oocyte meiotic maturation

Cao, G., Guo, R., Chen, M., Sun, C., & Wang, J. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.31037 · Cited by 8 · see citing works

Poly (ADP-ribose) polymerase (PARP) inhibition in cancer: Potential impact in cancer stem cells and therapeutic implications

Rizvi, A., Merlin, M. A., & Shah, G. M. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174546 · Cited by 8 · see citing works

The poly(ADP-ribosyl)ation system in the crustacean copepod Temora stylifera (Dana, 1853–1855) from a coastal area of the Mediterranean Sea: a new biomarker of the health status

Bianchi, A. R., Capua, I. D., Guerretti, V., Guagliardi, A., Carotenuto, Y., & Maio, A. D. (2024) · Euro-Mediterranean Journal for Environmental Integration · doi:10.1007/s41207-024-00625-w · Cited by 3 · see citing works

Decoding PARP roles in breast cancer therapy resistance

Abohassan, M., Altalbawy, F. M. A., Jabir, M. S., Hasan, T. F., Kyada, A., Nathiya, D., Kaur, P., Kumar, M. R., Abosaoda, M. K., & Iqbal, M. S. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12223-w · Cited by 2 · see citing works

SPERT gene silencing inhibits the growth of human colon cancer xenograft tumor in nude mice via p38MAPK/HSP27 signaling pathway

Si-zeng, C. H. E. N., & Zheng, L. (2021) · Biomedical Research · doi:10.2220/biomedres.42.247 · Cited by 2 · see citing works

The molecular complexity of deep vein thrombosis was preliminarily explored based on the ceRNA network, scRNA-seq and AlphaFold 2

Pan, B.-Z., Luo, Q.-Y., Jiang, M., Ning, D., Deng, L., Dai, X., Wu, Z., Deng, Z., Luo, D.-Y., Wang, Y.-Y.-J., et al. (2025) · BMC Medical Genomics · doi:10.1186/s12920-025-02239-9 · Cited by 1 · see citing works

Nicotinamide Adenine Dinucleotide and Signaling Transduction

Xu, H., Zhang, D., Sun, M., & Qin, Z.-H. (2025) · Springer eBooks · doi:10.1007/978-981-97-9877-3_17

PARP inhibitors elicit distinct transcriptional programs in homologous recombination competent castration‐resistant prostate cancer

Cunningham, M. L., Vasquez‐Gonzalez, J., Barnada, S. M., Tchotorlishvili, S., Jones, L., Maguire, R., Lewis, G., Rizwan, K., Deng, J., Koachar, S., et al. (2025) · Molecular Oncology · doi:10.1002/1878-0261.70098

Rôles du NAD dans la plasticité cellulaire cancéreuse

Gouasmi, R. (2025) · doi:10.70675/4c8cef97z8e4fz4245z8588z8d740f2b17fe

Regulation of chromatin structure and function by adenosine diphosphate (ADP)-ribosylation

Huang, D., Edwards, A. D., & Kraus, W. L. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-19001-8.00007-6

Structural and evolutionary insights into chicken ADP-ribosyl transferases (ARTs)

Bandi, J. P., Rohaim, M. A., Atasoy, M. O., Naggar, R. F. E., Copeland, N. A., & Munir, M. (2026) · Gene Reports · doi:10.1016/j.genrep.2026.102672

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

ADP-Ribosylation: Activation, Recognition, and Removal

Li, N., & Chen, J. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.2245 · Cited by 53 · see citing works

Poli-ADP-ribosilación de proteínas y función en procesos biológicos

Borja Guachamín, R. F. (2022) · Deposito de Investigacion Universidad de Sevilla (University of Seville)

ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes

Grimaldi, G., & Corda, D. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180416 · Cited by 30 · see citing works

Chemical genetic methodologies for identifying protein substrates of PARPs

Rodriguez, K. M., & Cohen, M. S. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.07.002 · Cited by 15 · see citing works