PARP-1 inhibitors DPQ and PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells (422 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2013 Jan; 38(1): 50-58.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.551, 5-year impact factor: 2.377
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84871615066&partnerID=40&md5=59dfcbceb79264b039d02a22b17aa383
Keywords: Anti-Inflammatory Agents, Biological Markers Metabolism, Brain Neoplasms Pathology, Carnosine Pharmacology, Cell Line, Tumor, Cell Survival Drug Effects, Coloring Agents, Down-Regulation Drug Effects, Fluorescent Antibody Technique, Glioblastoma Pathology, Humans, Isoquinolines Pharmacology, L-Lactate Dehydrogenase Biosynthesis, Microscopy, Confocal, Nitrites Metabolism, Phenanthrenes Pharmacology, Piperidines Pharmacology, Poly(adp-Ribose) Polymerases Antagonists, Inhibitors, Tetrazolium Salts, Thiazoles, Trehalose Pharmacology, Parp-1, Pj-34, 4 Dihydro 5 [4 (1 Piperidinyl)butoxy] 1(2h) Isoquinoline, Arginine Derivative, Enzyme Inhibitor, Gamma Interferon, Lipopolysaccharide, 6 Dihydro 6 Oxo 2 Phenanthridinyl) 2 Dimethylaminoacetamide, N Monomethylarginine, Nicotinamide Adenine Dinucleotide Adenosine Diphosphate Ribosyltransferase 1, Nitric Oxide Synthase Inhibitor, Unclassified Drug, Antiinflammatory Activity, Article, Cell Viability, Confocal Microscopy, Controlled Study, Down Regulation, Enzyme Release, Human Cell, Immunofluorescence, Priority Journal, Protein Expression, 4 Dihydro 5 [4 (1 Piperidinyl) Butoxy] 1 (2h) Isoquinoline, Poly (adp-Ribose) Polymerases, Poly (adp-Ribose) Polymerases Antagonists,
Affiliations:
*** IBB - CNR ***
Dipartimento Gian Filippo Ingrassia, Sezione di Biologia, Genetica, Genomica Cellulare e Molecolare, Unita di BioMedicina Molecolare Genomica e dei Sistemi Complessi, Genetica, Biologia Computazionale, Universita di Catania, Via Santa Sofia 87, 95123 Catania, Italy.
Department of Chemical Sciences, University of Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Istituto Biostrutture e Bioimmagini CNR, Sez. di Catania, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
References:
D'Amours, D., Desnoyers, S., Da Silva, I., Poirier, G.G., Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions (1999) Biochem J, 342 (PART 2), pp. 249-268. , 1045500
Hassa, P.O., Hottiger, M.O., The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases (2008) Front Biosci, 13, pp. 3046-3082. , 17981777 1:CAS:528:DC%2BD1cXhs1Cntrk%3D
Hottiger, M.O., Hassa, P.O., Luscher, B., Toward a unified nomenclature for mammalian ADP-ribosyltransferases (2010) Trends Biochem Sci, 35 (4), pp. 208-219. , 20106667 1:CAS:528:DC%2BC3cXksVegs70%3D
Ame, J.C., Spenlehauer, C., De Murcia, G., The PARP superfamily (2004) BioEssays, 26, pp. 882-893. , 15273990 1:CAS:528:DC%2BD2cXnt1CqtLk%3D
Citarelli, M., Teotia, S., Lamb, R.S., Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes (2010) BMC Evol Biol, 10, p. 308. , 20942953
Hassa, P.O., Haenni, S.S., Elser, M., Hottiger, M.O., Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going? (2006) Microbiol Mol Biol Rev, 70, pp. 789-829. , 16959969 1:CAS:528:DC%2BD28XhtVOnsrfP
Nguewa, P.A., Fuertes, M.A., Valladares, B., Poly(ADP-ribose) polymerases: Homology, structural domains and functions. Novel therapeutical applications (2005) Prog Biophys Mol Biol, 88, pp. 143-172. , 15561303 1:CAS:528:DC%2BD2cXhtVSltbnM
Veres, B., Radnai, B., Gallyas, F., Regulation of kinase cascades and transcription factors by a poly(ADP-ribose) polymerase-1 inhibitor, 4-hydroxyquinazoline, in lipopolysaccharideinduced inflammation in mice (2004) J Pharmacol Exp Ther, 310, pp. 247-255. , 14999056 1:CAS:528:DC%2BD2cXlsVOjsLc%3D
Oliver, F.J., Menissier-De Murcia, J., De Murcia, G., Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease (1999) Am J Hum Genet, 64, pp. 1282-1288. , 10205258 1:CAS:528:DyaK1MXlt1ajtro%3D
Hassa, P.O., Covic, M., Hasan, S., The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function (2001) J Biol Chem, 276, pp. 45588-45597. , 11590148 1:CAS:528:DC%2BD3MXptVyntb0%3D
Ha, H.C., Hester, L.D., Snyder, S.H., Poly(ADP-ribose) polymerase-1 dependence of stress-induced transcription factors and associated gene expression in glia (2002) Proc Natl Acad Sci USA, 99, pp. 3270-3275. , 11854472 1:CAS:528:DC%2BD38Xit1CqsbY%3D
Hassa, P.O., Buerki, C., Lombardi, C., Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1 (2003) J Biol Chem, 278, pp. 45145-45153. , 12960163 1:CAS:528:DC%2BD3sXoslyqur0%3D
Ha, H.C., Defective transcription factor activation for proinflammatory gene expression in poly(ADPribose) polymerase 1-deficient glia (2004) Proc Natl Acad Sci USA, 101, pp. 5087-5092. , 15041747 1:CAS:528:DC%2BD2cXjsFCisbo%3D
Nakajima, H., Nagaso, H., Kakui, N., Critical role of the automodification of poly(ADP-ribose) polymerase-1 in nuclear factor-kappaB-dependent gene expression in primary cultured mouse glial cells (2004) J Biol Chem, 279, pp. 42774-42786. , 15302869 1:CAS:528:DC%2BD2cXotVOgsb0%3D
Eliasson, M.J., Sampei, K., Mandir, A.S., Hurn, P.D., Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia (1997) Nat Med, 3, pp. 1089-1095. , 9334719 1:CAS:528:DyaK2sXmsFyqtb8%3D
Burkart, V., Wang, Z.Q., Radons, J., Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin (1999) Nat Med, 5, pp. 314-319. , 10086388 1:CAS:528:DyaK1MXhsVSks7Y%3D
Jijon, H.B., Churchill, T., Malfair, D., Inhibition of poly (ADP-ribose) polymerase attenuates inflammation in a model of chronic colitis (2000) Am J Physiol Gastrointest Liver Physiol, 279, pp. 641-G651. , 10960365 1:CAS:528:DC%2BD3cXmvVGrtL4%3D
Chiarugi, A., Inhibitors of poly(ADP-ribose) polymerase-1 suppress transcriptional activation in lymphocytes and ameliorate autoimmune encephalomyelitis in rats (2002) Br J Pharmacol, 137, pp. 761-770. , 12411406 1:CAS:528:DC%2BD38XovF2gu7o%3D
Boulares, A.H., Zoltoski, A.J., Sherif, Z.A., Gene knockout or pharmacological inhibition of poly(ADP-ribose) polymerase-1 prevents lung inflammation in a murine model of asthma (2003) Am J Respir Cell Mol Biol, 28, pp. 322-329. , 12594058 1:CAS:528:DC%2BD3sXhvVOmsLk%3D
Iwashita, A., Tojo, N., Matsuura, S., A novel and potent poly(ADP-ribose) polymerase-1 inhibitor, FR247304 (5-chloro-2- [3-(4-phenyl-3,6-dihydro-1(2H)-pyridinyl)propyl]-4(3H)-quinazo linone), attenuates neuronal damage in in vitro and in vivo models of cerebral ischemia (2004) J Pharmacol Exp Ther, 310, pp. 425-436. , 15075382 1:CAS:528:DC%2BD2cXmtVyksrk%3D
Spina-Purrello, V., Patti, D., Giuffrida-Stella, A.M., Parp and cell death or protection in rat primary astroglial cell cultures under LPS/IFNγ induced proinflammatory conditions (2008) Neurochem Res, 33, pp. 2583-2592. , 18758954 1:CAS:528:DC%2BD1cXhtlOktL3E
Lange, M., Connelly, D., Traber, D.L., Time course of nitric oxide synthases, nitrosative stress, and poly(ADP ribosylation) in an ovine sepsis model (2010) Crit Care, 14, pp. R129. , http://ccforum.com/content/14/4/R129
Virag, L., Szabo, C., The therapeutic potential of poly(ADP-ribose) polymerase inhibitors (2002) Pharmacol Rev, 54, pp. 375-429
Underhill, C., Toulmonde, M., Bonnefoi, H., A review of PARP inhibitors: From bench to bedside (2011) Ann Oncol, 22, pp. 268-279. , 20643861 1:STN:280:DC%2BC3M7ltFSruw%3D%3D
Graziani, G., Szabò, C., Clinical perspectives of PARP inhibitors (2005) Pharmacol Res, 52, pp. 109-111. , 15911339 1:CAS:528:DC%2BD2MXks1Wlsbk%3D
Jagtap, P., Szabo, C., Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors (2005) Nat Rev Drug Discov, 4, pp. 421-440. , 15864271 1:CAS:528:DC%2BD2MXjs1OktL8%3D
Rouleau, M., Patel, A., Hendzel, M.J., Kaufmann, S.H., PARP inhibition: PARP1 and beyond (2010) Nat Rev Cancer, 10, pp. 293-301. , 10.1038/nrc2812 20200537 1:CAS:528:DC%2BC3cXis1yms7w%3D
Krishnakumar, R., Lee Kraus, W., The PARP Side of the nucleus: Molecular actions, physiological outcomes, and clinical targets (2010) Mol Cell, 39, pp. 8-24. , 20603072 1:CAS:528:DC%2BC3cXpsFejsr4%3D
Mazzone, G.L., Nistri, A., Effect of the PARP-1 inhibitor PJ 34 on excitotoxic damage evoked by kainate on rat spinal cord organotypic slices (2011) Cell Mol Neurobiol, 31, pp. 469-478. , 21190076 1:CAS:528:DC%2BC3MXjvFOjsbw%3D
De Murcia, J.M., Niedergang, C., Trucco, C., Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells (1997) Proc Natl Acad Sci USA, 94, pp. 7303-7307. , 9207086
Popoff, I., Jijon, H., Monia, B., Antisense oligonucleotides to poly(ADP-ribose) polymerase-2 ameliorate colitis in interleukin-10-deficient mice (2002) J Pharmacol Exp Therap, 303, pp. 1145-1154. , 1:CAS:528:DC%2BD38Xptlamur4%3D
Kofler, J., Otsuka, T., Zhang, Z., Differential effect of PARP-2 deletion on brain injury after focal and global cerebral ischemia (2006) J Cereb Blood Flow Metab, 26, pp. 135-141. , 15959455 1:CAS:528:DC%2BD28XmsFamtQ%3D%3D
Menissier De Murcia, J., Ricoul, M., Tartier, L., Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse (2003) EMBO J, 22, pp. 2255-2263. , 12727891 1:CAS:528:DC%2BD3sXjsVKmu7w%3D
Rouleau, M., McDonald, D., Gagne, P., PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery (2007) J Cell Biochem, 100, pp. 385-401. , 16924674 1:CAS:528:DC%2BD2sXpsVyksg%3D%3D
Phulwani, N.K., Poly (ADP-ribose) polymerases (PARPs) 1-3 regulate astrocyte activation (2008) J Neurochem, 106 (2), pp. 578-590. , 10.1111/j.1471-4159.2008.05403.x 18410506 1:CAS:528:DC%2BD1cXovFWgt7k%3D
Zingarelli, B., Salzman, A.L., Szabo, C., Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury (1998) Circ Res, 83, pp. 85-94. , 9670921 1:CAS:528:DyaK1cXks1Kktr8%3D
Yu, Z., Kuncewicz, T., Dubinsky, W.P., Nitric oxide dependent negative feedback of PARP-1 transactivation of the inducible nitric-oxide synthase gene (2006) J Biol Chem, 281, pp. 9101-9109. , 10.1074/jbc.M511049200 16464859 1:CAS:528:DC%2BD28XjtVSktbY%3D
Ehrlich, W., Huser, H., Kroger, H., Inhibition of the induction of collagenase by interleukin-1 beta in cultured rabbit synovial fibroblasts after treatment with the poly(ADP-ribose)-polymerase inhibitor 3-aminobenzamide (1995) Rheumatol Int, 15, pp. 171-172. , 8835300 1:CAS:528:DyaK28XhtVSmt7Y%3D
Martin-Oliva, D., Aguilar-Quesada, R., O'Valle, F., Inhibition of poly(ADP-ribose) polymerase modulates tumor related gene expression, including hypoxia-inducible factor-1 activation, during skin carcinogenesis (2006) Cancer Res, 66, pp. 5744-5756. , 16740713 1:CAS:528:DC%2BD28XltFyjtLk%3D
Andreone, T.L., O'Connor, M., Denenberg, A., Poly(ADPribose) polymerase-1 regulates activation of activator protein-1 in murine fibroblasts (2003) J Immunol, 170, pp. 2113-2120. , 12574383 1:CAS:528:DC%2BD3sXht12hsrw%3D
Bryant, H.E., Schultz, N., Thomas, H.D., Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase (2005) Nature, 434, pp. 913-917. , 15829966 1:CAS:528:DC%2BD2MXjtFOmsrY%3D
Toller, I.M., Altmeyer, M., Kohler, E., Inhibition of ADP ribosylation prevents and cures Helicobacter-induced gastric preneoplasia (2010) Cancer Res, 70, pp. 5912-5922. , 20634404 1:CAS:528:DC%2BC3cXovVanu7o%3D
Chen, S., Chiu, L.-Y., Maa, M.-C., ZVAD-induced autophagic cell death requires c-Src-dependent ERK and JNK activation and reactive oxygen species generation (2011) Autophagy, 7, pp. 217-228. , 21127402 1:CAS:528:DC%2BC3MXivVSmu7c%3D
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2013 Jan; 38(1): 50-58.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.551, 5-year impact factor: 2.377
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84871615066&partnerID=40&md5=59dfcbceb79264b039d02a22b17aa383
Keywords: Anti-Inflammatory Agents, Biological Markers Metabolism, Brain Neoplasms Pathology, Carnosine Pharmacology, Cell Line, Tumor, Cell Survival Drug Effects, Coloring Agents, Down-Regulation Drug Effects, Fluorescent Antibody Technique, Glioblastoma Pathology, Humans, Isoquinolines Pharmacology, L-Lactate Dehydrogenase Biosynthesis, Microscopy, Confocal, Nitrites Metabolism, Phenanthrenes Pharmacology, Piperidines Pharmacology, Poly(adp-Ribose) Polymerases Antagonists, Inhibitors, Tetrazolium Salts, Thiazoles, Trehalose Pharmacology, Parp-1, Pj-34, 4 Dihydro 5 [4 (1 Piperidinyl)butoxy] 1(2h) Isoquinoline, Arginine Derivative, Enzyme Inhibitor, Gamma Interferon, Lipopolysaccharide, 6 Dihydro 6 Oxo 2 Phenanthridinyl) 2 Dimethylaminoacetamide, N Monomethylarginine, Nicotinamide Adenine Dinucleotide Adenosine Diphosphate Ribosyltransferase 1, Nitric Oxide Synthase Inhibitor, Unclassified Drug, Antiinflammatory Activity, Article, Cell Viability, Confocal Microscopy, Controlled Study, Down Regulation, Enzyme Release, Human Cell, Immunofluorescence, Priority Journal, Protein Expression, 4 Dihydro 5 [4 (1 Piperidinyl) Butoxy] 1 (2h) Isoquinoline, Poly (adp-Ribose) Polymerases, Poly (adp-Ribose) Polymerases Antagonists,
Affiliations:
*** IBB - CNR ***
Dipartimento Gian Filippo Ingrassia, Sezione di Biologia, Genetica, Genomica Cellulare e Molecolare, Unita di BioMedicina Molecolare Genomica e dei Sistemi Complessi, Genetica, Biologia Computazionale, Universita di Catania, Via Santa Sofia 87, 95123 Catania, Italy.
Department of Chemical Sciences, University of Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Istituto Biostrutture e Bioimmagini CNR, Sez. di Catania, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
References:
D'Amours, D., Desnoyers, S., Da Silva, I., Poirier, G.G., Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions (1999) Biochem J, 342 (PART 2), pp. 249-268. , 1045500
Hassa, P.O., Hottiger, M.O., The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases (2008) Front Biosci, 13, pp. 3046-3082. , 17981777 1:CAS:528:DC%2BD1cXhs1Cntrk%3D
Hottiger, M.O., Hassa, P.O., Luscher, B., Toward a unified nomenclature for mammalian ADP-ribosyltransferases (2010) Trends Biochem Sci, 35 (4), pp. 208-219. , 20106667 1:CAS:528:DC%2BC3cXksVegs70%3D
Ame, J.C., Spenlehauer, C., De Murcia, G., The PARP superfamily (2004) BioEssays, 26, pp. 882-893. , 15273990 1:CAS:528:DC%2BD2cXnt1CqtLk%3D
Citarelli, M., Teotia, S., Lamb, R.S., Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes (2010) BMC Evol Biol, 10, p. 308. , 20942953
Hassa, P.O., Haenni, S.S., Elser, M., Hottiger, M.O., Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going? (2006) Microbiol Mol Biol Rev, 70, pp. 789-829. , 16959969 1:CAS:528:DC%2BD28XhtVOnsrfP
Nguewa, P.A., Fuertes, M.A., Valladares, B., Poly(ADP-ribose) polymerases: Homology, structural domains and functions. Novel therapeutical applications (2005) Prog Biophys Mol Biol, 88, pp. 143-172. , 15561303 1:CAS:528:DC%2BD2cXhtVSltbnM
Veres, B., Radnai, B., Gallyas, F., Regulation of kinase cascades and transcription factors by a poly(ADP-ribose) polymerase-1 inhibitor, 4-hydroxyquinazoline, in lipopolysaccharideinduced inflammation in mice (2004) J Pharmacol Exp Ther, 310, pp. 247-255. , 14999056 1:CAS:528:DC%2BD2cXlsVOjsLc%3D
Oliver, F.J., Menissier-De Murcia, J., De Murcia, G., Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease (1999) Am J Hum Genet, 64, pp. 1282-1288. , 10205258 1:CAS:528:DyaK1MXlt1ajtro%3D
Hassa, P.O., Covic, M., Hasan, S., The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function (2001) J Biol Chem, 276, pp. 45588-45597. , 11590148 1:CAS:528:DC%2BD3MXptVyntb0%3D
Ha, H.C., Hester, L.D., Snyder, S.H., Poly(ADP-ribose) polymerase-1 dependence of stress-induced transcription factors and associated gene expression in glia (2002) Proc Natl Acad Sci USA, 99, pp. 3270-3275. , 11854472 1:CAS:528:DC%2BD38Xit1CqsbY%3D
Hassa, P.O., Buerki, C., Lombardi, C., Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1 (2003) J Biol Chem, 278, pp. 45145-45153. , 12960163 1:CAS:528:DC%2BD3sXoslyqur0%3D
Ha, H.C., Defective transcription factor activation for proinflammatory gene expression in poly(ADPribose) polymerase 1-deficient glia (2004) Proc Natl Acad Sci USA, 101, pp. 5087-5092. , 15041747 1:CAS:528:DC%2BD2cXjsFCisbo%3D
Nakajima, H., Nagaso, H., Kakui, N., Critical role of the automodification of poly(ADP-ribose) polymerase-1 in nuclear factor-kappaB-dependent gene expression in primary cultured mouse glial cells (2004) J Biol Chem, 279, pp. 42774-42786. , 15302869 1:CAS:528:DC%2BD2cXotVOgsb0%3D
Eliasson, M.J., Sampei, K., Mandir, A.S., Hurn, P.D., Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia (1997) Nat Med, 3, pp. 1089-1095. , 9334719 1:CAS:528:DyaK2sXmsFyqtb8%3D
Burkart, V., Wang, Z.Q., Radons, J., Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin (1999) Nat Med, 5, pp. 314-319. , 10086388 1:CAS:528:DyaK1MXhsVSks7Y%3D
Jijon, H.B., Churchill, T., Malfair, D., Inhibition of poly (ADP-ribose) polymerase attenuates inflammation in a model of chronic colitis (2000) Am J Physiol Gastrointest Liver Physiol, 279, pp. 641-G651. , 10960365 1:CAS:528:DC%2BD3cXmvVGrtL4%3D
Chiarugi, A., Inhibitors of poly(ADP-ribose) polymerase-1 suppress transcriptional activation in lymphocytes and ameliorate autoimmune encephalomyelitis in rats (2002) Br J Pharmacol, 137, pp. 761-770. , 12411406 1:CAS:528:DC%2BD38XovF2gu7o%3D
Boulares, A.H., Zoltoski, A.J., Sherif, Z.A., Gene knockout or pharmacological inhibition of poly(ADP-ribose) polymerase-1 prevents lung inflammation in a murine model of asthma (2003) Am J Respir Cell Mol Biol, 28, pp. 322-329. , 12594058 1:CAS:528:DC%2BD3sXhvVOmsLk%3D
Iwashita, A., Tojo, N., Matsuura, S., A novel and potent poly(ADP-ribose) polymerase-1 inhibitor, FR247304 (5-chloro-2- [3-(4-phenyl-3,6-dihydro-1(2H)-pyridinyl)propyl]-4(3H)-quinazo linone), attenuates neuronal damage in in vitro and in vivo models of cerebral ischemia (2004) J Pharmacol Exp Ther, 310, pp. 425-436. , 15075382 1:CAS:528:DC%2BD2cXmtVyksrk%3D
Spina-Purrello, V., Patti, D., Giuffrida-Stella, A.M., Parp and cell death or protection in rat primary astroglial cell cultures under LPS/IFNγ induced proinflammatory conditions (2008) Neurochem Res, 33, pp. 2583-2592. , 18758954 1:CAS:528:DC%2BD1cXhtlOktL3E
Lange, M., Connelly, D., Traber, D.L., Time course of nitric oxide synthases, nitrosative stress, and poly(ADP ribosylation) in an ovine sepsis model (2010) Crit Care, 14, pp. R129. , http://ccforum.com/content/14/4/R129
Virag, L., Szabo, C., The therapeutic potential of poly(ADP-ribose) polymerase inhibitors (2002) Pharmacol Rev, 54, pp. 375-429
Underhill, C., Toulmonde, M., Bonnefoi, H., A review of PARP inhibitors: From bench to bedside (2011) Ann Oncol, 22, pp. 268-279. , 20643861 1:STN:280:DC%2BC3M7ltFSruw%3D%3D
Graziani, G., Szabò, C., Clinical perspectives of PARP inhibitors (2005) Pharmacol Res, 52, pp. 109-111. , 15911339 1:CAS:528:DC%2BD2MXks1Wlsbk%3D
Jagtap, P., Szabo, C., Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors (2005) Nat Rev Drug Discov, 4, pp. 421-440. , 15864271 1:CAS:528:DC%2BD2MXjs1OktL8%3D
Rouleau, M., Patel, A., Hendzel, M.J., Kaufmann, S.H., PARP inhibition: PARP1 and beyond (2010) Nat Rev Cancer, 10, pp. 293-301. , 10.1038/nrc2812 20200537 1:CAS:528:DC%2BC3cXis1yms7w%3D
Krishnakumar, R., Lee Kraus, W., The PARP Side of the nucleus: Molecular actions, physiological outcomes, and clinical targets (2010) Mol Cell, 39, pp. 8-24. , 20603072 1:CAS:528:DC%2BC3cXpsFejsr4%3D
Mazzone, G.L., Nistri, A., Effect of the PARP-1 inhibitor PJ 34 on excitotoxic damage evoked by kainate on rat spinal cord organotypic slices (2011) Cell Mol Neurobiol, 31, pp. 469-478. , 21190076 1:CAS:528:DC%2BC3MXjvFOjsbw%3D
De Murcia, J.M., Niedergang, C., Trucco, C., Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells (1997) Proc Natl Acad Sci USA, 94, pp. 7303-7307. , 9207086
Popoff, I., Jijon, H., Monia, B., Antisense oligonucleotides to poly(ADP-ribose) polymerase-2 ameliorate colitis in interleukin-10-deficient mice (2002) J Pharmacol Exp Therap, 303, pp. 1145-1154. , 1:CAS:528:DC%2BD38Xptlamur4%3D
Kofler, J., Otsuka, T., Zhang, Z., Differential effect of PARP-2 deletion on brain injury after focal and global cerebral ischemia (2006) J Cereb Blood Flow Metab, 26, pp. 135-141. , 15959455 1:CAS:528:DC%2BD28XmsFamtQ%3D%3D
Menissier De Murcia, J., Ricoul, M., Tartier, L., Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse (2003) EMBO J, 22, pp. 2255-2263. , 12727891 1:CAS:528:DC%2BD3sXjsVKmu7w%3D
Rouleau, M., McDonald, D., Gagne, P., PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery (2007) J Cell Biochem, 100, pp. 385-401. , 16924674 1:CAS:528:DC%2BD2sXpsVyksg%3D%3D
Phulwani, N.K., Poly (ADP-ribose) polymerases (PARPs) 1-3 regulate astrocyte activation (2008) J Neurochem, 106 (2), pp. 578-590. , 10.1111/j.1471-4159.2008.05403.x 18410506 1:CAS:528:DC%2BD1cXovFWgt7k%3D
Zingarelli, B., Salzman, A.L., Szabo, C., Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury (1998) Circ Res, 83, pp. 85-94. , 9670921 1:CAS:528:DyaK1cXks1Kktr8%3D
Yu, Z., Kuncewicz, T., Dubinsky, W.P., Nitric oxide dependent negative feedback of PARP-1 transactivation of the inducible nitric-oxide synthase gene (2006) J Biol Chem, 281, pp. 9101-9109. , 10.1074/jbc.M511049200 16464859 1:CAS:528:DC%2BD28XjtVSktbY%3D
Ehrlich, W., Huser, H., Kroger, H., Inhibition of the induction of collagenase by interleukin-1 beta in cultured rabbit synovial fibroblasts after treatment with the poly(ADP-ribose)-polymerase inhibitor 3-aminobenzamide (1995) Rheumatol Int, 15, pp. 171-172. , 8835300 1:CAS:528:DyaK28XhtVSmt7Y%3D
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PARP-1 inhibitors DPQ and PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells
Poly(ADP-ribose) polymerases (PARPs) are recognized as key regulators of cell survival or death. PARP-1 is essential to the repair of DNA single-strand breaks via the base excision repair pathway. The enzyme may be overactivated in response to inflammatory cues, thus depleting cellular energy pools and eventually causing cell death. Accordingly, PARP-1 inhibitors, acting by competing with its physiological substrate NAD(+), have been proposed to play a protective role in a wide range of inflammatory and ischemia/reperfusion-associated diseases. Recently, it has also been reported that PARP-1 regulates proinflammatory mediators, including cytokines, chemokines, adhesion molecules, and enzymes (e.g., iNOS). Furthermore, PARP-1 has been shown to act as a coactivator of NF-kappaB- and other transcription factors implicated in stress/inflammation, as AP-1, Oct-1, SP-1, HIF, and Stat-1. To further substantiate this hypothesis, we tested the biomolecular effects of PARP-1 inhibitors DPQ and PJ-34 on human glioblastoma cells, induced to a proinflammatory state with lipopolysaccharide and Interferon-gamma. PARP-1 expression was evaluated by laser scanning confocal microscopy immunofluorescence (LSM); nitrite production, LDH release and cell viability were also determined. LSM of A-172, SNB-19 and CAS-1 cells demonstrated that DPQ and PJ-34 downregulate PARP-1 expression; they also cause a decrease of LDH release and nitrite production, while increasing cell viability. Similar effects were caused in all three cell lines by N-mono-methyl-arginine, a well known iNOS inhibitor, and by L-carnosine and trehalose, two antioxidant molecules. These results demonstrate that, similar to other well characterized drugs, DPQ and PJ-34 reduce cell inflammation and damage that follow PARP-1 overexpression, while they increase cell survival: this suggests their potential exploitation in clinical Medicine.
Poly(ADP-ribose) polymerases (PARPs) are recognized as key regulators of cell survival or death. PARP-1 is essential to the repair of DNA single-strand breaks via the base excision repair pathway. The enzyme may be overactivated in response to inflammatory cues, thus depleting cellular energy pools and eventually causing cell death. Accordingly, PARP-1 inhibitors, acting by competing with its physiological substrate NAD(+), have been proposed to play a protective role in a wide range of inflammatory and ischemia/reperfusion-associated diseases. Recently, it has also been reported that PARP-1 regulates proinflammatory mediators, including cytokines, chemokines, adhesion molecules, and enzymes (e.g., iNOS). Furthermore, PARP-1 has been shown to act as a coactivator of NF-kappaB- and other transcription factors implicated in stress/inflammation, as AP-1, Oct-1, SP-1, HIF, and Stat-1. To further substantiate this hypothesis, we tested the biomolecular effects of PARP-1 inhibitors DPQ and PJ-34 on human glioblastoma cells, induced to a proinflammatory state with lipopolysaccharide and Interferon-gamma. PARP-1 expression was evaluated by laser scanning confocal microscopy immunofluorescence (LSM); nitrite production, LDH release and cell viability were also determined. LSM of A-172, SNB-19 and CAS-1 cells demonstrated that DPQ and PJ-34 downregulate PARP-1 expression; they also cause a decrease of LDH release and nitrite production, while increasing cell viability. Similar effects were caused in all three cell lines by N-mono-methyl-arginine, a well known iNOS inhibitor, and by L-carnosine and trehalose, two antioxidant molecules. These results demonstrate that, similar to other well characterized drugs, DPQ and PJ-34 reduce cell inflammation and damage that follow PARP-1 overexpression, while they increase cell survival: this suggests their potential exploitation in clinical Medicine.
PARP-1 inhibitors DPQ and PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells
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PARP-1 inhibitors DPQ and PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells
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Bucci M, Cigliano L, Vellecco V, D'Andrea LD, Ziaco B, Rossi A, Sautebin L, Carlucci A, Abrescia P, Pedone C, Ianaro A, Cirino G
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Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
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Capparelli R, Romanelli A, Iannaccone M, Nocerino N, Ripa R, Pensato S, Pedone C, Iannelli D
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* Cyclic mimetics of kinase-inhibitory region of Suppressors of Cytokine Signaling 1: Progress toward novel anti-inflammatory therapeutics (22 views)
Eur J Med Chem (ISSN: 0223-5234linking, 1768-3254, 1768-3254electronic), 2021 Oct 5; 221: 113547-113547.
Impact Factor: 5.572
View Export to BibTeX Export to EndNote
Platella C, Gaglione R, Napolitano E, Arciello A, Pirota V, Doria F, Musumeci D, Montesarchio D
* DNA Binding Mode Analysis of a Core-Extended Naphthalene Diimide as a Conformation-Sensitive Fluorescent Probe of G-Quadruplex Structures (10 views)
Int J Mol Sci (ISSN: 1422-0067linking), 2021 Sep 30; 22 (19 ): N/D-N/D.
Impact Factor:
View Export to BibTeX Export to EndNote
Russo L, Mascanzoni F, Farina B, Dolga AM, Monti A, Caporale A, Culmsee C, Fattorusso R, Ruvo M, Doti N
* Design, Optimization, and Structural Characterization of an Apoptosis-Inducing Factor Peptide Targeting Human Cyclophilin A to Inhibit Apoptosis Inducing Factor-Mediated Cell Death (11 views)
J Med Chem (ISSN: 0022-2623linking), 2021 Aug 12; 64 (15 ): 11445-11459.
Impact Factor:
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello V, Roviello GN
* Molecular Basis of the Therapeutical Potential of Clove (Syzygium aromaticum L. ) and Clues to Its Anti-COVID-19 Utility (78 views)
Molecules (ISSN: 1420-3049linking, 1420-3049electronic), 2021 Mar 26; 26(7): 1880-1886.
Impact Factor: 4.411
View Export to BibTeX Export to EndNote
Miceli M, Cutignano A, Conte M, Ummarino R, Romanelli A, Ruvo M, Leone M, Mercurio FA, Doti N, Manzo E, Romano G, Altucci L, Ianora A
* Monoacylglycerides from the Diatom Skeletonema marinoi Induce Selective Cell Death in Cancer Cells (158 views)
Mar Drugs (ISSN: 1660-3397linking), 2019 Nov 1; 17 (11 ): N/D-N/D.
Impact Factor: 3.345
View Export to BibTeX Export to EndNote
Carella A, Roviello V, Iannitti R, Palumbo R, La Manna S, Marasco D, Trifuoggi M, Diana R, Roviello GN
* Evaluating the biological properties of synthetic 4-nitrophenyl functionalized benzofuran derivatives with telomeric DNA binding and antiproliferative activities (398 views)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Jan; 121: 77-88.
Impact Factor: 4.784
View Export to BibTeX Export to EndNote
Diaferia C, Balasco N, Sibillano T, Ghosh M, Adler-abramovich L, Giannini C, Vitagliano L, Morelli G, Accardo A
* Amyloid-Like Fibrillary Morphology Originated by Tyrosine-Containing Aromatic Hexapeptides (82 views)
Chemistry (ISSN: 0947-6539linking, 1521-3765electronic), 2018 May 7; 24 (26 ): 6804-6817.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Romano S, Staibano S, Greco A, Brunetti A, Nappo G, Ilardi G, Martinelli R, Sorrentino A, Di Pace A, Mascolo M, Bisogni R, Scalvenzi M, Alfano B, Romano M
* FK506 binding protein 51 positively regulates melanoma stemness and metastatic potential (430 views) (PDF 242 views)
Cell Death & (ISSN: 2041-4889, 2041-4889electronic), 2013 Apr 4; 4(6): e578-e578.
Impact Factor: 5.333
View Export to BibTeX Export to EndNote
Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (523 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
View Export to BibTeX Export to EndNote
Bucci M, Cigliano L, Vellecco V, D'Andrea LD, Ziaco B, Rossi A, Sautebin L, Carlucci A, Abrescia P, Pedone C, Ianaro A, Cirino G
* Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (401 views)
J Pharmacol Exp Ther (ISSN: 1521-0103, 0022-3565), 2012 Mar; 340(3): 716-722.
Impact Factor: 3.891
View Export to BibTeX Export to EndNote
Zaccaro L, Garcia-lopez Mt Gonzalez-muniz RG
* TRPV1 modulators: Structure-activity relationships using a rational combinatorial approach (392 views)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2011 Jun 15; 21(12): 3541-3545.
Impact Factor: 2.554
View Export to BibTeX Export to EndNote
Erkekoǧlu P, Rachidi W, De Rosa V, Giray B, Favier A, Hincal F
* Protective effect of selenium supplementation on the genotoxicity of di(2-ethylhexyl)phthalate and mono(2-ethylhexyl)phthalate treatment in LNCaP cells (554 views)
Free Radic Biol Med (ISSN: 0891-5849, 0891-5849linking, 1873-4596electronic), 2010 Aug 15; 49(4): 559-566.
Impact Factor: 5.707
View Export to BibTeX Export to EndNote
Lanzillo R, Orefice G, Quarantelli M, Rinaldi C, Prinster A, Ventrella G, Spitaleri D, Lus G, Vacca G, Carotenuto B, Salvatore E, Brunetti A, Tedeschi G, Brescia Morra V
* Atorvastatin combined to interferon to verify the efficacy (ACTIVE) in relapsing-remitting active multiple sclerosis patients: A longitudinal controlled trial of combination therapy (559 views)
Mult Scler (ISSN: 1352-4585, 1477-0970, 1352-4585linking), 2010 Apr; 16(4): 450-454.
Impact Factor: 4.23
View Export to BibTeX Export to EndNote
Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
* Crystal And Molecular Structure Of Beta-Cyclodextrins Functionalized With The Anti-Inflammatory Drug Etodolac (416 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1227-1235.
Impact Factor: 2.605
View Export to BibTeX Export to EndNote
Capparelli R, Romanelli A, Iannaccone M, Nocerino N, Ripa R, Pensato S, Pedone C, Iannelli D
* Synergistic antibacterial and anti-inflammatory activity of temporin A and modified temporin B in vivo (452 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 28; 4(9): e7191-e7191.
Impact Factor: 4.351
View Export to BibTeX Export to EndNote
15 Records (13 excluding Abstracts).
Total impact factor: 54.585 (44.901 excluding Abstracts).
Total 5 year impact factor: 51.302 (41.586 excluding Abstracts).
Total impact factor: 54.585 (44.901 excluding Abstracts).
Total 5 year impact factor: 51.302 (41.586 excluding Abstracts).
422 views. Last view on Saturday 14 January 2023, 20:33:46
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