PARP-1 activation in the ERK signaling pathway

COHENARMON, M

doi:10.1016/j.tips.2007.08.005

Cited by 137Protein Kinase Regulation and GTPase SignalingDNA Repair MechanismsPARP inhibition in cancer therapy

PARP-1 activation in the ERK signaling pathway

COHENARMON, M·2007·Trends in Pharmacological Sciences

DOI 10.1016/j.tips.2007.08.005

Open this paper in CoChat — free account

Abstract

PARP-1 is a highly conserved DNA-binding protein, the most abundant member of the polyADP-ribose polymerases (PARP) family, which catalyzes post-translational modification of proteins by polyADP-ribosylation. This modification affects protein-protein and protein-DNA interactions. Binding of PARP-1 to breakages in damaged DNA causes its activation and auto-polyADP-ribosylation in a process that is pivotal for DNA repair. Our recent findings outlined an alternative mechanism of PARP-1 activation via a direct interaction with phosphorylated ERK2 (externally regulated kinase), which is unrelated to DNA damage and does not involve PARP-1 binding to DNA. Furthermore, ERK2-induced PARP-1 activation dramatically amplifies ERK-signals, enhancing ERK-induced phosphorylation of the transcription factor Elk1 and enhancing core histone acetylation and expression of the Elk1 target gene, c-fos. Thus, PARP-1 activation in the ERK signaling pathway mediates epigenetic mechanisms promoting growth, proliferation and differentiation regulated by the Raf-MEK-ERK phosphorylation cascade.

Integrity signals

Registry

Crossref · 10.1016/j.tips.2007.08.005

Cites

37 of 37 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

PARP1 activation can be induced by stress responses other than DNA damage, including ERK-1, Notch/HES-1, and intracellular calcium overload.
“In addition, as reviewed by Weaver and Yang 94, PARP1 activation can be induced by stress responses other than DNA damage, including the ERK-1 95, 96 and Notch/HES-1 97 signaling pathways and intracellular calcium overload 98.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [95]

The molecular biology of memory storage: a dialogue between genes and synapses
Kandel, E. R. (2001) · Science · doi:10.1126/science.1067020 · Cited by 3,917 · see citing works
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 · see citing works
Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543 · see citing works
The PARP superfamily
Amé, J., Spenlehauer, C., & de MURCIA, G. (2004) · BioEssays · doi:10.1002/bies.20085 · Cited by 1,463 · see citing works
Inducible and constitutive transcription factors in the mammalian nervous system: control of gene expression by Jun, Fos and Krox, and CREB/ATF proteins
Herdegen, T., & Leah, J. D. (1998) · Brain Research Reviews · doi:10.1016/s0165-0173(98)00018-6 · Cited by 1,352 · see citing works
The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions
Yoon, S., & Seger, R. (2006) · Growth Factors · doi:10.1080/02699050500284218 · Cited by 1,278 · see citing works
Patterned stimulation at the theta frequency is optimal for the induction of hippocampal long-term potentiation
Larson, J., Wong, D., & Lynch, G. (1986) · Brain Research · doi:10.1016/0006-8993(86)90579-2 · Cited by 1,037 · see citing works
XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage
Masson, M., Niedergang, C., Schreiber, V., Muller, S., Murcia, J. M., & de MURCIA, G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3563 · Cited by 910 · see citing works
CBP Histone Acetyltransferase Activity Is a Critical Component of Memory Consolidation
Korzus, E., Rosenfeld, M. G., & Mayford, M. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.002 · Cited by 823 · see citing works
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD + into a nuclear signalPreprint
Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 803 · see citing works
DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite.
Szabó, C., Zingarelli, B., O’Connor, M. P., & Salzman, A. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.1753 · Cited by 622 · see citing works
The Fos family of transcription factors and their role in tumourigenesis
Milde-Langosch, K. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2005.08.008 · Cited by 583 · see citing works
PARP Goes Transcription
Kraus, W. L., & Lis, J. T. (2003) · Cell · doi:10.1016/s0092-8674(03)00433-1 · Cited by 547 · see citing works
Base Excision Repair Is Impaired in Mammalian Cells Lacking Poly(ADP-ribose) Polymerase-1
Dantzer, F., de la Rubia, G., Murcia, J. M., Hostomský, Z., de MURCIA, G., & Schreiber, V. (2000) · Biochemistry · doi:10.1021/bi0003442 · Cited by 505 · see citing works
Prediction and validation of the distinct dynamics of transient and sustained ERK activation
Sasagawa, S., Ozaki, Y.-I., Fujita, K. A., & Kuroda, S. (2005) · Nature Cell Biology · doi:10.1038/ncb1233 · Cited by 451 · see citing works
Chromatin Loosening by Poly(ADP)-Ribose Polymerase (PARP) at Drosophila Puff Loci
Tulin, A. V., & Spradling, A. C. (2003) · Science · doi:10.1126/science.1078764 · Cited by 443 · see citing works
Ets ternary complex transcription factors
Buchwalter, G., Gross, C., & Wasylyk, B. (2004) · Gene · doi:10.1016/j.gene.2003.09.028 · Cited by 336 · see citing works
DNA-Independent PARP-1 Activation by Phosphorylated ERK2 Increases Elk1 Activity: A Link to Histone Acetylation
Cohen-Armon, M., Visochek, L., Rozensal, D., Kalal, A., Geistrikh, I., Klein, R., Bendetz-Nezer, S., Yao, Z., & Seger, R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.012 · Cited by 329 · see citing works
Self-citation
Molecular and biochemical features of poly (ADP-ribose) metabolism
Lautier, D., Lagueux, J., Thibodeau, J., M�nard, L., & Poirier, G. G. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076101 · Cited by 301 · see citing works
Spatial and Temporal Cellular Responses to Single-Strand Breaks in Human Cells
Okano, S., Lan, L., Caldecott, K. W., Mori, T., & Yasui, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5472.2003 · Cited by 297 · see citing works
Activating the PARP-1 sensor component of the groucho/ TLE1 corepressor complex mediates a CaMKinase IIdelta-dependent neurogenic gene activation pathway.
Ju, B., Solum, D., Song, E. J., Lee, K.-J., Rose, D., Glass, C., & Rosenfeld, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.017 · Cited by 285 · see citing works
Transcriptional Coactivation of Nuclear Factor-κB-dependent Gene Expression by p300 Is Regulated by Poly(ADP)-ribose Polymerase-1
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 · see citing works
Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular.
Mendoza‐Alvarez, H., & Álvarez-González, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41568-2 · Cited by 227 · see citing works
Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2
Kauppinen, T. M., Chan, W., 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 208 · see citing works
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 · see citing works
Growth Factor–induced p42/p44 MAPK Nuclear Translocation and Retention Requires Both MAPK Activation and Neosynthesis of Nuclear Anchoring Proteins
Lenormand, P., Brondello, J., Brunet, A., & Pouysségur, J. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.3.625 · Cited by 207 · see citing works
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 · see citing works
Long-Term Memory Requires PolyADP-ribosylation
Cohen‐Armon, M., Visochek, L., Katzoff, A., Levitan, D., Susswein, A. J., Klein, R., Valbrun, M., & Schwartz, J. H. (2004) · Science · doi:10.1126/science.1096775 · Cited by 159 · see citing works
Self-citation
MAP kinase phosphorylation‐dependent activation of Elk‐1 leads to activation of the co‐activator p300
Li, Q., Yang, S., Maeda, Y., Sladek, F. M., Sharrocks, A. D., & Martins‐Green, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg028 · Cited by 158 · see citing works
A Fast Signal–Induced Activation of Poly(Adp-Ribose) Polymerase
Homburg, S., Visochek, L., Moran, N., Dantzer, F., Priel, E., Asculai, E., Schwartz, D., Rotter, V., Dekel, N., & Cohen‐Armon, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.2.293 · Cited by 141 · see citing works
Self-citation
A dual role for poly‐ADP‐ribosylation in spatial memory acquisition after traumatic brain injury in mice involving NAD+ depletion and ribosylation of 14‐3‐3γ
Satchell, M. A., Zhang, X., Kochanek, P. M., Dixon, C. E., Jenkins, L. W., Melick, J. A., Szabó, C., & Clark, R. S. B. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01707.x · Cited by 99 · see citing works
PolyADP-Ribosylation Is Involved in Neurotrophic Activity
Visochek, L., Steingart, R. A., Vulih-Shultzman, I., Klein, R., Priel, E., Gozes, I., & Cohen‐Armon, M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0333-05.2005 · Cited by 82 · see citing works
Self-citation
A Tale of Early Response Genes
Sng, J., Taniura, H., & Yoneda, Y. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.606 · Cited by 77 · see citing works
Novel modulators of poly(ADP-ribose) polymerase
Szabó, C., Pacher, P., & Swanson, R. A. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.10.003 · Cited by 70 · see citing works
Sustained activation of extracellular signal‐regulated kinase by nerve growth factor regulates c‐fos protein stabilization and transactivation in PC12 cells
Pellegrino, M. J., & Stork, P. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04250.x · Cited by 59 · see citing works
Inhibition of poly (ADP-ribose) polymerase and caspase-3, but not caspase-1, prevents apoptosis and improves spatial memory of rats with twice-repeated cerebral ischemia
Hatip‐Al‐Khatib, I., Iwasaki, K., Chung, E.-H., Egashira, N., Mishima, K., & Fujiwara, M. (2004) · Life Sciences · doi:10.1016/j.lfs.2004.05.014 · Cited by 29 · see citing works
Early administration of nicotinamide prevents learning and memory impairment in mice induced by 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine
Yang, J., He, L., Wang, J., & Adams, J. D., Jr. (2004) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2004.03.007 · Cited by 28 · see citing works

Flagged first, then by citations

Sorted by citations

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
PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration
Chaitanya, G. V., Alexander, J. S., & Babu, P. P. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-31 · Cited by 929 · see citing works
Role of the Peroxynitrite-Poly(ADP-Ribose) Polymerase Pathway in Human Disease
Pacher, P., & Szabó, C. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080019 · Cited by 364 · see citing works
Functional Aspects of PARP1 in DNA Repair and Transcription
Ko, H. L., & Ren, E. C. (2012) · Biomolecules · doi:10.3390/biom2040524 · Cited by 207 · see citing works
Radiation-induced signaling pathways that promote cancer cell survival (Review)
HEIN, A. L., OUELLETTE, M. M., & YAN, Y. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2614 · Cited by 201 · see citing works
Poly(ADP-ribose): PARadigms and PARadoxes
Bürkle, A., & Virág, L. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.010 · Cited by 197 · see citing works
Beyond DNA repair, the immunological role of PARP ‐1 and its siblings
Rosado, M. M., Bennici, E., Novelli, F., & Pioli, C. (2013) · Immunology · doi:10.1111/imm.12099 · Cited by 178 · see citing works
Catastrophic NAD+ Depletion in Activated T Lymphocytes through Nampt Inhibition Reduces Demyelination and Disability in EAE
Bruzzone, S., Fruscione, F., Morando, S., Ferrando, T., Poggi, A. D., Garuti, A., D’Urso, A., Selmo, M., Benvenuto, F., Cea, M., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007897 · Cited by 171 · see citing works
Post-translational modifications in mitochondria: protein signaling in the powerhouse
Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149 · see citing works
QKI-Mediated Alternative Splicing of the Histone Variant MacroH2A1 Regulates Cancer Cell Proliferation
Novikov, L., Park, J. W., Chen, H., Klerman, H., Jalloh, A. S., & Gamble, M. J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05244-11 · Cited by 146 · see citing works
Hormonal effects on partitioning of nutrients for tissue growth: role of growth hormone and prolactin.
Bauman, D. E., Eisemann, J. H., & Currie, W. B. (1982) · PubMed · Cited by 140 · see citing works
Radiation-induced mitotic catastrophe in PARG-deficient cells
Amé, J., Fouquerel, E., Gauthier, L., Biard, D. S. F., Boussin, F. D., Dantzer, F., de MURCIA, G., & Schreiber, V. (2009) · Journal of Cell Science · doi:10.1242/jcs.039115 · Cited by 129 · see citing works
The PARP family: insights into functional aspects of poly ( ADP ‐ribose) polymerase‐1 in cell growth and survival
Jubin, T., Kadam, A. A., Jariwala, M., Bhatt, S., Sutariya, S., Gani, A. R., Gautam, S., & Begum, R. (2016) · Cell Proliferation · doi:10.1111/cpr.12268 · Cited by 130 · see citing works
PARP-1 Inhibition Attenuates Neuronal Loss, Microglia Activation and Neurological Deficits after Traumatic Brain Injury
Stoica, B. A., Loane, D. J., Zhao, Z., Kabadi, S. V., Hanscom, M., Byrnes, K. R., & Faden, A. I. (2013) · Journal of Neurotrauma · doi:10.1089/neu.2013.3194 · Cited by 122 · see citing works
RETRACTED ARTICLE: Exopolysaccharides from Lactobacillus plantarum NCU116 induce c-Jun dependent Fas/Fasl-mediated apoptosis via TLR2 in mouse intestinal epithelial cancer cells
Zhou, X., Hong, T., Yu, Q., Nie, S., Gong, D., Xiong, T., & Xie, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-14178-2 · Cited by 117 · see citing works
Retracted
PARP-1 Mediates LPS-Induced HMGB1 Release by Macrophages through Regulation of HMGB1 Acetylation
Yang, Z., Li, L., Chen, L., Yuan, W., Dong, L., Zhang, Y., Wu, H., & Wang, C. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400359 · Cited by 114 · see citing works
PARP inhibition protects mitochondria and reduces ROS production via PARP-1-ATF4-MKP-1-MAPK retrograde pathway
Hocsák, E., Szabó, V., Kálmán, N., Antus, C., Cseh, A. M., Sümegi, K., Erős, K., Hegedüs, Z., Gallyas, F., Sümegi, B., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.018 · Cited by 110 · see citing works
Poly(ADP-ribose) Polymerase-1 in Amyloid Beta Toxicity and Alzheimer's Disease
Strosznajder, J. B., Czapski, G. A., Adamczyk, A., & Strosznajder, R. P. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8258-9 · Cited by 109 · see citing works
Regulation of chromatin structure by poly(ADP-ribosyl)ation
Beneke, S. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00169 · Cited by 98 · see citing works
The role of poly(ADP-ribosyl)ation in epigenetic events
Quénet, D., Ramy, R. E., Schreiber, V., & Dantzer, F. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.07.023 · Cited by 94 · see citing works
Mitogen-Activated Protein (MAP) Kinase Scaffolding Proteins: A Recount
Meister, M., Tomasovic, A., Banning, A., & Tikkanen, R. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14034854 · Cited by 87 · see citing works
How to kill tumor cells with inhibitors of poly(ADP‐ribosyl)ation
Mangerich, A., & Bürkle, A. (2010) · International Journal of Cancer · doi:10.1002/ijc.25683 · Cited by 83 · see citing works
PolyADP‐ribosylation is required for long‐term memory formation in mammals
Goldberg, S., Visochek, L., Giladi, E., Gozes, I., & Cohen‐Armon, M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06296.x · Cited by 79 · see citing works
Self-citation
Androgen and PARP-1 Regulation of TRPM2 Channels after Ischemic Injury
Shimizu, T., Macey, T. A., Quillinan, N., Klawitter, J., Perraud, A., Traystman, R. J., & Herson, P. S. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.105 · Cited by 78 · see citing works
The role of PARP activation in glutamate-induced necroptosis in HT-22 cells
Xu, X., Chua, C. C., Zhang, M., Geng, D., Liu, C., Hamdy, R. C., & Chua, B. H. L. (2010) · Brain Research · doi:10.1016/j.brainres.2010.04.080 · Cited by 74 · see citing works
Prostatic α1‐adrenoceptors: New concepts of function, regulation, and intracellular signaling
Hennenberg, M., Stief, C. G., & Gratzke, C. (2013) · Neurourology and Urodynamics · doi:10.1002/nau.22467 · Cited by 74 · see citing works
The PARP Enzyme Family and the Hallmarks of Cancer Part 1. Cell Intrinsic Hallmarks
Demény, M. Á., & Virág, L. (2021) · Cancers · doi:10.3390/cancers13092042 · Cited by 70 · see citing works
Cell Signaling Pathways That Promote Radioresistance of Cancer Cells
Ouellette, M. M., Zhou, S., & Yan, Y. (2022) · Diagnostics · doi:10.3390/diagnostics12030656 · Cited by 69 · see citing works
Enhanced repair of UV-induced DNA damage by 1,25-dihydroxyvitamin D3 in skin is linked to pathways that control cellular energy
Rybchyn, M. S., De Silva, W. G. M., Sequeira, V. B., McCarthy, B. Y., Dilley, A. V., Dixon, K. M., Halliday, G. M., & Mason, R. S. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.11.037 · Cited by 63 · see citing works
Inputs and outputs of poly(ADP-ribosyl)ation: Relevance to oxidative stress
Hegedűs, C., & Virág, L. (2014) · Redox Biology · doi:10.1016/j.redox.2014.08.003 · Cited by 63 · see citing works
Teratoma: from spontaneous tumors to the pluripotency/malignancy assay
Bulić‐Jakuš, F., Bojanac, A. K., Jurić‐Lekić, G., Vlahović, M., & Sinčić, N. (2015) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.219 · Cited by 60 · see citing works
Neuronal NOS and cyclooxygenase-2 contribute to DNA damage in a mouse model of Parkinson disease
Hoang, T., Choi, D., Nagai, M., Wu, D. C., Nagata, T., Prou, D., Wilson, G. L., Vila, M., Jackson-Lewis, V. R., Dawson, V. L., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.013 · Cited by 59 · see citing works
A selective eradication of human nonhereditary breast cancer cells by phenanthridine-derived polyADP-ribose polymerase inhibitors
Inbar-Rozensal, D., Castiel, A., Visochek, L., Castel, D., Dantzer, F., Izraeli, S., & Cohen‐Armon, M. (2009) · Breast Cancer Research · doi:10.1186/bcr2445 · Cited by 58 · see citing works
Self-citation
Poly(ADP-Ribose) Metabolism in Brain and Its Role in Ischemia Pathology
Strosznajder, R. P., Czubowicz, K., Jęśko, H. M., & Strosznajder, J. B. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8124-6 · Cited by 55 · see citing works
Perinatal asphyxia: current status and approaches towards neuroprotective strategies, with focus on sentinel proteins
Herrera‐Marschitz, M., Morales, P., Leyton, L., Bustamante, D., Klawitter, V., Espina-Marchant, P., Allende-Castro, C., Lisboa, F., Cunich, G., Jara-Cavieres, A., et al. (2010) · Neurotoxicity Research · doi:10.1007/s12640-010-9208-9 · Cited by 54 · see citing works
Poly(ADP-ribose) polymerase-1 modulates Nrf2-dependent transcription
Wu, T., Wang, X. J., Tian, W., Jaramillo, M. C., Lau, A., & Zhang, D. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.806 · Cited by 53 · see citing works
Bisphenol A induces DNA damage in cells exerting immune surveillance functions at peripheral and central level
Pietro, P. D., D’Auria, R., Viggiano, A., Ciaglia, E., Meccariello, R., Russo, R. D., Puca, A. A., Vecchione, C., Nori, S. L., & Santoro, A. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.126819 · Cited by 54 · see citing works
Regulation of the MicroRNA 200b (miRNA-200b) by Transcriptional Regulators PEA3 and ELK-1 Protein Affects Expression of Pin1 Protein to Control Anoikis
Zhang, X., Zhang, B., Gao, J., Wang, X., & Liu, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.478016 · Cited by 52 · see citing works
The Multifactorial Role of PARP-1 in Tumor Microenvironment
Martí, J. M., Fernández‐Cortés, M., Serrano-Sáenz, S., Zamudio-Martínez, E., Delgado‐Bellido, D., García-Díaz, Á., & Oliver, F. J. (2020) · Cancers · doi:10.3390/cancers12030739 · Cited by 51 · see citing works
Perinatal asphyxia: CNS development and deficits with delayed onset
Herrera‐Marschitz, M., Neira-Peña, T., Rojas-Mancilla, E., Espina-Marchant, P., Esmar, D., Perez, R. S., MuÃ±oz, V., Gutierrez-Hernandez, M., Rivera, B., Simola, N., et al. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00047 · Cited by 50 · see citing works
Synergic pro-apoptotic effects of Ferulic Acid and nanostructured lipid carrier in glioblastoma cells assessed through molecular and Delayed Luminescence studies
Grasso, R., Dell’Albani, P., Carbone, C., Spatuzza, M., Bonfanti, R., Sposito, G., Puglisi, G., Musumeci, F., Scordino, A., & Campisi, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-61670-3 · Cited by 47 · see citing works
SETBP1 accumulation induces P53 inhibition and genotoxic stress in neural progenitors underlying neurodegeneration in Schinzel-Giedion syndrome
Banfi, F., Rubio, A., Zaghi, M., Massimino, L., Fagnocchi, G., Bellini, E. N., Luoni, M., Cancellieri, C., Bagliani, A., Resta, C. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24391-3 · Cited by 40 · see citing works
Proteomic Dissection of Cell Type-Specific H2AX-Interacting Protein Complex Associated with Hepatocellular Carcinoma
Yang, X., Zou, P., Yao, J., Yun, D., Bao, H., Du, R., Long, J., & Chen, X. (2009) · Journal of Proteome Research · doi:10.1021/pr900932y · Cited by 41 · see citing works
Low Shear Stress Induced HMGB1 Translocation and Release via PECAM-1/PARP-1 Pathway to Induce Inflammation Response
Qin, W., Mi, S.-H., Li, C., Wang, G., Zhang, J., Wang, H., Zhang, F., Ma, Y., Wu, D., & Zhang, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120586 · Cited by 43 · see citing works
Fibroblast Growth Factor Regulates Human Neuroectoderm Specification Through ERK1/2-PARP-1 Pathway
Yoo, Y. D., Huang, C. T.-L., Zhang, X., LaVaute, T. M., & Zhang, S. (2011) · Stem Cells · doi:10.1002/stem.758 · Cited by 42 · see citing works
Inducible Major Vault Protein Plays a Pivotal Role in Double-Stranded RNA– or Virus-Induced Proinflammatory Response
Peng, N., Liu, S., Xia, Z., Ren, S., Feng, J. J., Jing, M.-Z., Gao, X., Wiemer, E. A. C., & Zhu, Y. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501481 · Cited by 42 · see citing works
Sam68 Is Required for DNA Damage Responses via Regulating Poly(ADP-ribosyl)ation
Sun, X., Fu, K., Hodgson, A., Wier, E. M., Wen, M. G., Kamenyeva, O., Xia, X., Koo, L. Y., & Wan, F. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002543 · Cited by 42 · see citing works
Interplay between ADP-ribosyltransferases and essential cell signaling pathways controls cellular responses
Böhi, F., Manetsch, P., & Hottiger, M. O. (2021) · Cell Discovery · doi:10.1038/s41421-021-00323-9 · Cited by 40 · see citing works
HMGN1 Protein Regulates Poly(ADP-ribose) Polymerase-1 (PARP-1) Self-PARylation in Mouse Fibroblasts
Masaoka, A., Gassman, N. R., Kedar, P. S., Prasad, R., Hou, E. W., Horton, J. K., Bustin, M., & Wilson, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.370759 · Cited by 40 · see citing works
cAMP-independent non-pigmentary actions of variant melanocortin 1 receptor: AKT-mediated activation of protective responses to oxidative DNA damage
Castejón-Griñán, M., Herráiz, C., Olivares, C., Jiménez‐Cervantes, C., & García-Borrón, J. C. (2018) · Oncogene · doi:10.1038/s41388-018-0216-1 · Cited by 39 · see citing works
Poly-(ADP-Ribose) Polymerase-1 Is Necessary for Long-Term Facilitation inAplysia
Hernandez, A. I., Wolk, J., Hu, J., Liu, J., Kurosu, T., Schwartz, J. H., & Schacher, S. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1512-09.2009 · Cited by 39 · see citing works
Poly(ADP-ribosyl)ation polymerases: mechanism and new target of anticancer therapy
Heitz, F., Harter, P., Ewald-Riegler, N., Papsdorf, M., Kommoss, S., & du Bois, A. (2010) · Expert Review of Anticancer Therapy · doi:10.1586/era.10.53 · Cited by 39 · see citing works
Zn2+‐induced ERK activation mediates PARP‐1‐dependent ischemic‐reoxygenation damage to oligodendrocytes
Domercq, M., Mato, S., Soria, F. N., Sánchez‐Gómez, M. V., Alberdi, E. M., & Matute, C. (2012) · Glia · doi:10.1002/glia.22441 · Cited by 38 · see citing works
Immune Cell Regulatory Pathways Unexplored as Host-Directed Therapeutic Targets for Mycobacterium tuberculosis : An Opportunity to Apply Precision Medicine Innovations to Infectious Diseases
Mahon, R. N., & Hafner, R. (2015) · Clinical Infectious Diseases · doi:10.1093/cid/civ621 · Cited by 36 · see citing works
CXXC finger protein 4 inhibits the CDK18‐ERK1/2 axis to suppress the immune escape of gastric cancer cells with involvement of ELK1/MIR100HG pathway
Li, P., Ge, D., Li, P., Hu, F., Chu, J., Chen, X., Song, W., Wang, A., Tian, G., & Gu, X. Q. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15625 · Cited by 35 · see citing works
Antiproliferative Effects of GnRH Agonists: Prospects and Problems for Cancer Therapy
White, C. D., Stewart, A. J., Lu, Z.-L., Millar, R. P., & Morgan, K. (2008) · Neuroendocrinology · doi:10.1159/000119093 · Cited by 34 · see citing works
Protection from Ultraviolet Damage and Photocarcinogenesis by Vitamin D Compounds
Gordon‐Thomson, C., Tongkao‐on, W., Song, E. J., Carter, S. E., Dixon, K. M., & Mason, R. S. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0437-2_17 · Cited by 32 · see citing works
Role of PARP-1 in prostate cancer.
Deshmukh, D., & Qiu, Y. (2015) · Europe PMC (PubMed Central) · Cited by 33 · see citing works
Knockdown of PARP-1 Inhibits Proliferation and ERK Signals, Increasing Drug Sensitivity in Osteosarcoma U2OS Cells
Li, S., Cui, Z., & Meng, X. (2016) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504016x14666990347554 · Cited by 28 · see citing works
Enhancement of Soft Tissue Sarcoma Cell Radiosensitivity by Poly(ADP-ribose) Polymerase-1 Inhibitors
Mangoni, M., Sottili, M., Salvatore, G., Meattini, I., Desideri, I., Greto, D., Loi, M., Becherini, C., Garlatti, P., Paoli, C. D., et al. (2018) · Radiation Research · doi:10.1667/rr15035.1 · Cited by 28 · see citing works
Poly (ADP-ribose) polymerase: An Overview of Mechanistic Approaches and Therapeutic Opportunities in the Management of Stroke
Tiwari, P., Khan, H., Singh, T. G., & Grewal, A. K. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03595-z · Cited by 27 · see citing works
Antitumor and anticancer stem cell activity of a poly ADP-ribose polymerase inhibitor olaparib in breast cancer cells
Shimo, T., Kurebayashi, J., Kanomata, N., Yamashita, T., Kozuka, Y., Moriya, T., & Sonoo, H. (2012) · Breast Cancer · doi:10.1007/s12282-012-0356-z · Cited by 27 · see citing works
Targeting TRAF3 Downstream Signaling Pathways in B cell Neoplasms
Moore, C. R. (2015) · Journal of Cancer Science & Therapy · doi:10.4172/1948-5956.1000327 · Cited by 27 · see citing works
Catalpol Protects Pre-myelinating Oligodendrocytes against Ischemia-Induced Oxidative Injury through ERK1/2 Signaling Pathway
Cai, Q., Ma, T., Li, C., Tian, Y., & Li, H. (2016) · International Journal of Biological Sciences · doi:10.7150/ijbs.16823 · Cited by 26 · see citing works
The interplay of mitophagy, autophagy, and apoptosis in cisplatin-induced kidney injury: involvement of ERK signaling pathway
Suman, I., Šimić, L., Jurešić, G. Č., Buljević, S., Klepac, D., & Domitrović, R. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01872-0 · Cited by 26 · see citing works
ADP‐ribosylation in evasion, promotion and exacerbation of immune responses
Rosado, M. M., & Pioli, C. (2021) · Immunology · doi:10.1111/imm.13332 · Cited by 24 · see citing works
Further Studies on the Hypothesis of PARP-1 Inhibition as a Strategy for Lessening the Long-Term Effects Produced by Perinatal Asphyxia: Effects of Nicotinamide and Theophylline on PARP-1 Activity in Brain and Peripheral Tissue
Allende-Castro, C., Espina-Marchant, P., Bustamante, D., Rojas-Mancilla, E., Neira-Peña, T., Gutierrez-Hernandez, M., Esmar, D., Valdés, J. L., Morales, P., Gebicke‐Haerter, P. J., et al. (2012) · Neurotoxicity Research · doi:10.1007/s12640-012-9310-2 · Cited by 24 · see citing works
Inhibition of poly (ADP-ribose) polymerase and inducible nitric oxide synthase protects against ischemic myocardial damage by reduction of apoptosis
Wang, J., Lin, H., Wang, Y., Qin, W., Wang, X., Zhao, T., Liu, Y., Lin, S., Du, Y., Zhang, M., et al. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2977 · Cited by 24 · see citing works
Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation
Musich, P. R., Li, Z., & Zou, Y. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-56017-5_4 · Cited by 23 · see citing works
Ca2+-induced PARP-1 activation and <i>ANF</i> expression are coupled events in cardiomyocytes
Geistrikh, I., Visochek, L., Klein, R., Miller, L., Mittelman, L., Shainberg, A., & Cohen-Armon, M. (2011) · Biochemical Journal · doi:10.1042/bj20101484 · Cited by 23 · see citing works
Self-citation
Array comparative genomic hybridization analysis of adult acute leukemia patients
Yasar, D., Karadoǧan, Ì., Alanoğlu, G., Akkaya, B., Lüleci, G., Salim, O., Timurağaoğlu, A., Törüner, G., & Berker-Karaüzüm, S. (2010) · Cancer Genetics and Cytogenetics · doi:10.1016/j.cancergencyto.2009.11.018 · Cited by 23 · see citing works
The development of PARP as a successful target for cancer therapy
Ferrara, R., Simionato, F., Ciccarese, C., Grego, E., Cingarlini, S., Iacovelli, R., Bria, E., Tortora, G., & Melisi, D. (2017) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2018.1419870 · Cited by 23 · see citing works
Mutated in colorectal cancer (MCC) is a novel oncogene in B lymphocytes
Edwards, S. K. E., Baron, J. E., Moore, C. R., Liu, Y., Perlman, D. H., Hart, R. P., & Xie, P. (2014) · Journal of Hematology & Oncology · doi:10.1186/s13045-014-0056-6 · Cited by 22 · see citing works
Characterization of nuclear factors modulating the apolipoprotein D promoter during growth arrest: Implication of PARP-1, APEX-1 and ERK1/2 catalytic activities
Levros, L.-C., Carmo, S. D., Edouard, E., Legault, P., Charfi, C., & Rassart, É. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.04.011 · Cited by 21 · see citing works
Epigallocatechin gallate attenuates cardiopulmonary bypass–associated lung injury
Kasper, B., Salameh, A., Krausch, M., Kiefer, P., Kostelka, M., Mohr, F. W., & Dhein, S. (2015) · Journal of Surgical Research · doi:10.1016/j.jss.2015.11.007 · Cited by 21 · see citing works
Parp and Cell Death or Protection in Rat Primary Astroglial Cell Cultures Under LPS/IFNγ Induced Proinflammatory Conditions
Spina-Purrello, V., Patti, D., Giuffrida‐Stella, A. M., & Nicoletti, V. G. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9835-1 · Cited by 21 · see citing works
Increased ERK and JNK activation and decreased ERK/JNK ratio are associated with long-term organ damage in patients with systemic lupus erythematosus
Bloch, O., Amit-Vazina, M., Yona, E., Molad, Y., & Rapoport, M. J. (2014) · Lara D. Veeken · doi:10.1093/rheumatology/ket482 · Cited by 21 · see citing works
Açai Berry Administration Promotes Wound Healing through Wnt/β-Catenin Pathway
Interdonato, L., Marino, Y., Franco, G. A., Arangia, A., D’Amico, R., Siracusa, R., Cordaro, M., Impellizzeri, D., Fusco, R., Cuzzocrea, S., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010834 · Cited by 19 · see citing works
Hydrogen sulfide supplementation as a potential treatment for primary mitochondrial diseases
Slade, L., Deane, C. S., Szewczyk, N. J., Etheridge, T., & Whiteman, M. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107180 · Cited by 21 · see citing works
PJ-34 inhibits PARP-1 expression and ERK phosphorylation in glioma-conditioned brain microvascular endothelial cells
Motta, C., D’Angeli, F., Scalia, M., Satriano, C., Barbagallo, D., Николаевна, Н. И., Anfuso, C. D., Lupo, G., & Spina-Purrello, V. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.04.026 · Cited by 19 · see citing works
Catalpol Inhibits Ischemia-Induced Premyelinating Oligodendrocyte Damage through Regulation of Intercellular Calcium Homeostasis via Na+/Ca2+ Exchanger 3
Cai, Q., Ma, T., Tian, Y., Li, C., & Li, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071925 · Cited by 19 · see citing works
The effect of poly(ADP-ribosyl)ation inhibition on the porcine cumulus-oocyte complex during in vitro maturation
Kim, D. H., Lee, H. R., Kim, M. G., Lee, J. S., Jin, S. J., & Lee, H. T. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.070 · Cited by 18 · see citing works
Signal-induced PARP1-Erk synergism mediates IEG expression
Cohen-Armon, M., Yeheskel, A., & Pascal, J. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0042-0 · Cited by 18 · see citing works
Self-citation
An Interaction with PARP-1 and Inhibition of Parylation Contribute to Attenuation of DNA Damage Signaling by the Adenovirus E4orf4 Protein
Nebenzahl-Sharon, K., Sharf, R., Amer, J., Shalata, H., Khoury-Haddad, H., Sohn, S., Ayoub, N., Hearing, P., & Kleinberger, T. (2019) · Journal of Virology · doi:10.1128/jvi.02253-18 · Cited by 18 · see citing works
PKCα and HMGB1 antagonistically control hydrogen peroxide-induced poly-ADP-ribose formation
Andersson, A., Bluwstein, A., Kumar, N., Teloni, F., Traenkle, J., Baudis, M., Altmeyer, M., & Hottiger, M. O. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw442 · Cited by 18 · see citing works
Protection from Ultraviolet Damage and Photocarcinogenesis by Vitamin D Compounds
Silva, W. G. M. D., Abboud, M., Yang, C., Dixon, K. M., Rybchyn, M. S., & Mason, R. S. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-46227-7_12 · Cited by 18 · see citing works
Short- and Long-Term Consequences of Perinatal Asphyxia: Looking for Neuroprotective Strategies
Herrera‐Marschitz, M., Neira-Peña, T., Leyton, L., Gebicke‐Haerter, P. J., Rojas-Mancilla, E., Morales, P., & Bustamante, D. (2014) · Advances in neurobiology · doi:10.1007/978-1-4939-1372-5_9 · Cited by 16 · see citing works
ELK1 suppresses SYTL1 expression by recruiting HDAC2 in bladder cancer progression
Wang, J., Luo, J., Wu, X., & Li, Z. (2022) · Human Cell · doi:10.1007/s13577-022-00789-z · Cited by 15 · see citing works
Nanoparticulate drug combination inhibits DNA damage repair and PD-L1 expression in BRCA-mutant and wild type triple-negative breast cancer
Alradwan, I. A., Zhi, P., Zhang, T., Lip, H., Zetrini, A., He, C., Henderson, J. T., Rauth, A. M., & Wu, X. Y. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.11.061 · Cited by 15 · see citing works
Acyl-CoA-binding domain containing 3 modulates NAD+ metabolism through activating poly(ADP-ribose) polymerase 1
Chen, Y., Bang, S., Park, S.-H., Shi, H., & Kim, S. F. (2015) · Biochemical Journal · doi:10.1042/bj20141487 · Cited by 15 · see citing works
PARP1 Activation Controls Stress Granule Assembly after Oxidative Stress and DNA Damage
Singatulina, A. S., Sukhanova, M. V., Desforges, B., Joshi, V., Pastré, D., & Lavrik, O. I. (2022) · Cells · doi:10.3390/cells11233932 · Cited by 14 · see citing works
Quantitative proteomics unveiled: Regulation of DNA double strand break repair by EGFR involves PARP1
Myllynen, L., Kwiatkowski, M., Gleißner, L., Riepen, B., Hoffer, K., Wurlitzer, M., Petersen, C., Dikomey, E., Rothkamm, K., Schlüter, H., et al. (2015) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2015.09.018 · Cited by 14 · see citing works
Erythropoietin-driven signalling and cell migration mediated by polyADP-ribosylation
Inbar, D., Cohen‐Armon, M., & Neumann, D. (2012) · British Journal of Cancer · doi:10.1038/bjc.2012.395 · Cited by 14 · see citing works
Self-citation
Computational analysis of data from a genome-wide screening identifies new PARP1 functional interactors as potential therapeutic targets
Lodovichi, S., Mercatanti, A., Cervelli, T., & Galli, A. (2019) · Oncotarget · doi:10.18632/oncotarget.26812 · Cited by 13 · see citing works
Posttranslational Modification of Proteins
Green, K., & Garneau-Tsodikova, S. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00662-6 · Cited by 2 · see citing works
Silodosin Inhibits Noradrenaline-Activated Transcription Factors Elk1 and SRF in Human Prostate Smooth Muscle
Hennenberg, M., Strittmatter, F., Beckmann, C., Rutz, B., Füllhase, C., Waidelich, R. M., Montorsi, F., Hedlund, P., Andersson, K., Stief, C. G., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050904 · Cited by 12 · see citing works
The TAS1R2 G-protein-coupled receptor is an ambient glucose sensor in skeletal muscle that regulates NAD homeostasis and mitochondrial capacity
Serrano, J., Boyd, J., Brown, I. S., Mason, C., Smith, K. R., Károlyi, K., Maurya, S. K., Meshram, N. N., Serna, V. A., Link, G. M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49100-8 · Cited by 11 · see citing works
Paclitaxel Induce Apoptosis of Giant Cells Tumor of Bone via TP53INP1 Signaling
Xiao, W., Zong, Z., Qiu, M., Chen, X., Shen, H., & Lao, L. (2018) · Orthopaedic Surgery · doi:10.1111/os.12414 · Cited by 11 · see citing works
DDI2 promotes tumor metastasis and resists antineoplastic drugs-induced apoptosis in colorectal cancer
Lei, L., Cao, Q., An, G., Lv, Y., Tang, J., & Yang, J. (2022) · APOPTOSIS · doi:10.1007/s10495-022-01796-z · Cited by 11 · see citing works
Radiation‐activated prosurvival signaling pathways in cancer cells
Ouellette, M. M., & Yan, Y. (2019) · Precision Radiation Oncology · doi:10.1002/pro6.1076 · Cited by 10 · see citing works

DNA-Independent PARP-1 Activation by Phosphorylated ERK2 Increases Elk1 Activity: A Link to Histone Acetylation
Cohen-Armon, M., Visochek, L., Rozensal, D., Kalal, A., Geistrikh, I., Klein, R., Bendetz-Nezer, S., Yao, Z., & Seger, R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.012 · Cited by 329 · see citing works
Self-citation
Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2
Kauppinen, T. M., Chan, W., 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 208 · see citing works
A Fast Signal–Induced Activation of Poly(Adp-Ribose) Polymerase
Homburg, S., Visochek, L., Moran, N., Dantzer, F., Priel, E., Asculai, E., Schwartz, D., Rotter, V., Dekel, N., & Cohen‐Armon, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.2.293 · Cited by 141 · see citing works
Self-citation
Poly(ADP-ribose)polymerase-1 regulates activation of AP-1 by DNA damage
Lonskaya, I., & Soldatenkov, V. A. (2006) · Cancer Research
Interaction of PARP-2 with DNA structures mimicking DNA repair intermediates and consequences on activity of base excision repair proteins
Kutuzov, M. M., Khodyreva, S. N., Amé, J., Ilina, E. S., Sukhanova, M. V., Schreiber, V., & Lavrik, O. I. (2013) · Biochimie · doi:10.1016/j.biochi.2013.01.007 · Cited by 73 · see citing works

Authors: COHENARMON, M.
Venue: Trends in Pharmacological Sciences
Publisher: Elsevier BV
Published: 2007-11
Volume: 28
Issue: 11
Pages: 556-560
ISSN: 0165-6147 (ISSN-L)
DOI: 10.1016/j.tips.2007.08.005
OpenAlex: W2013220294
Cited by: 137
References: 37
Citations by year: 2026: 4 · 2025: 1 · 2024: 6 · 2023: 3 · 2022: 9 · 2021: 9 · 2020: 6 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 9 · 2015: 12 · 2014: 10 · 2013: 11 · 2012: 12
FWCI: 3.04
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Pharmacological Sciences (publishedVersion)
PubMed (publishedVersion)
Funders: Israel Science Foundation
Ministry of Health, State of Israel
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
Keywords: PARP1, ERK signaling, ERK2 phosphorylation, poly(ADP-ribosyl)ation, histone acetylation, Fos expression, epigenetic regulation, cell proliferation and differentiation
MeSH terms: Poly (ADP-Ribose) Polymerase-1, Animals, Enzyme Activation, Humans, Models, Biological, Poly(ADP-ribose) Polymerases, Signal Transduction, Protein Serine-Threonine Kinases

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.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

PARP-1 activation in the ERK signaling pathway

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks