DNA-based strategies for blocking HMGB1 cytokine activity: Design, synthesis and preliminary in vitro/in vivo assays of DNA and DNA-like duplexes (462 views)
Mol Biosyst (ISSN: 1742-206x, 1742-2051, 1742-2051electronic), 2011 May; 7(5): 1742-1752.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.534, 5-year impact factor: 3.705
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79954550870&partnerID=40&md5=0910849612aa81cf202011f723666191
Keywords: Circular Dna, Heteroduplex, High Mobility Group B1 Protein, Kinked Dna, Lipopolysaccharide, Peptide Nucleic Acid, Animal, Article, Bagg Albino Mouse, Binding Site, Cell Line, Cell Motion, Cell Proliferation, Chemical Structure, Chemically Induced Disorder, Chemistry, Conformation, Drug Antagonism, Drug Effect, Endotoxemia, Metabolism, Mortality, Nucleotide Sequence, Protein Binding, Protein Tertiary Structure, Survival Rate, Base Sequence, Cell Movement, Hmgb1 Protein, Inbred Balb C, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Nucleic Acid Heteroduplexes, Protein Structure, Time Factors,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini - CNR, via Mezzocannone 16, 80134 Napoli, Italy
Bionucleon Srl, via Ribes 5, 10010 Colleretto Giacosa (TO), Italy
DIBIT, San Raffaele University, via Olgettina 58, 20132 Milano, Italy
References:
Shingo, Y., Ikuro, M., HMGB1, a novel inflammatory cytokine (2007) Clin. Chim. Acta, 375, pp. 36-4
Agresti, A., Bianchi, M.E., HMGB proteins and gene expression (2003) Current Opinion in Genetics and Development, 13 (2), pp. 170-178. , DOI 10.1016/S0959-437X(03)00023-6
Degryse, B., De Virgilio, M., The nuclear protein HMGB1, a new kind of chemokine? (2003) FEBS Letters, 553 (1-2), pp. 11-17. , DOI 10.1016/S0014-5793(03)01027-5
Ishihara, K., Tsutsumi, K., Kawane, S., Nakajima, M., Kasaoka, T., The receptor for advanced glycation end-products (RAGE) directly binds to ERK by a D-domain-like docking site (2003) FEBS Letters, 550 (1-3), pp. 107-113. , DOI 10.1016/S0014-5793(03)00846-9
Huttunen, H.J., Fages, C., Rauvala, H., Receptor for advanced glycation end products (RAGE)-mediated neurite outgrowth and activation of NF-kappaB require the cytoplasmic domain of the receptor but different downstream signaling pathways (1999) J. Biol. Chem., 274, pp. 19919-19924
Huttunen, H.J., Kuja-Panula, J., Rauvala, H., Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation (2002) Journal of Biological Chemistry, 277 (41), pp. 38635-38646. , DOI 10.1074/jbc.M202515200
Lander, H.M., Tauras, J.M., Ogiste, J.S., Hori, O., Moss, R.A., Schmidt, A.M., Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress (1997) Journal of Biological Chemistry, 272 (28), pp. 17810-17814. , DOI 10.1074/jbc.272.28.17810
Li, J., Kokkola, R., Tabibzadeh, S., Yang, R., Ochani, M., Qiang, X., Harris, H.E., Yang, H., Structural basis for the proinflammatory cytokine activity of high mobility group box 1 (2003) Molecular Medicine, 9 (1-2), pp. 37-45
Ito, I., Mitsuoka, N., Sobajima, J., Uesugi, H., Ozaki, S., Ohya, K., Yoshida, M., Conformational difference in HMGB1 proteins of human neutrophils and lymphocytes revealed by epitope mapping of a monoclonal antibody (2004) Journal of Biochemistry, 136 (2), pp. 155-162. , DOI 10.1093/jb/mvh107
Yamada, S., Inoue, K., Yakabe, K., Imaizumi, H., Maruyama, I., High mobility group protein 1 (HMGB1) quantified by ELISA with a monoclonal antibody that does not cross-react with HMGB2 (2003) Clinical Chemistry, 49 (9), pp. 1535-1537. , DOI 10.1373/49.9.1535
Allain, F.H.-T., Yen, Y.-M., Masse, J.E., Schultze, P., Dieckmann, T., Johnson, R.C., Feigon, J., Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding (1999) EMBO Journal, 18 (9), pp. 2563-2579. , DOI 10.1093/emboj/18.9.2563
Bianchi, M.E., Falciola, L., Ferrari, S., Lilley, D.M., The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins (1992) EMBO J., 11, pp. 1055-1063
Cerdan, R., Payet, D., Yang, J.-C., Travers, A.A., Neuhaus, D., HMG-D complexed to a bulge DNA: An NMR model (2001) Protein Science, 10 (3), pp. 504-518. , DOI 10.1110/ps.35501
Hardman, C.H., Broadhurst, R.W., Raine, A.R.C., Grasser, K.D., Thomas, J.O., Laue, E.D., Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy (1995) Biochemistry, 34 (51), pp. 16596-16607. , DOI 10.1021/bi00051a007
Jaouen, S., De Koning, L., Gaillard, C., Muselikova-Polanska, E., Stros, M., Strauss, F., Determinants of specific binding of HMGB1 protein to hemicatenated DNA loops (2005) Journal of Molecular Biology, 353 (4), pp. 822-837. , DOI 10.1016/j.jmb.2005.08.073, PII S0022283605010533
Lorenz, M., Hillisch, A., Payet, D., Buttinelli, M., Travers, A., Diekmann, S., DNA bending induced by high mobility group proteins studied by fluorescence resonance energy transfer (1999) Biochemistry, 38, pp. 12150-12158
Payet, D., Hillisch, A., Lowe, N., Diekmann, S., Travers, A., The recognition of distorted DNA structures by HMG-D: A footprinting and molecular modelling study (1999) J. Mol. Biol., 294, pp. 79-91
Webb, M., Payet, D., Lee, K.-B., Travers, A.A., Thomas, J.O., Structural requirements for cooperative binding of HMG1 to DNA minicircles (2001) Journal of Molecular Biology, 309 (1), pp. 79-88. , DOI 10.1006/jmbi.2001.4667
Harley, V.R., Jackson, D.I., Hextall, P.J., Hawkins, J.R., Berkovitz, G.D., Sockanathan, S., Lovell-Badge, R., Goodfellow, P.N., DNA binding activity of recombinant SRY from normal males and XY females (1992) Science, 255 (5043), pp. 453-456
Dornberger, U., Hillisch, A., Gollmick, F.A., Fritzsche, H., Diekmann, S., Solution structure of a five-adenine bulge loop within a DNA duplex (1999) Biochemistry, 38, pp. 12860-12868
Weir, H.M., Kraulis, P.J., Hill, C.S., Raine, A.R.C., Laue, E.D., Thomas, J.O., Structure of the HMG box motif in the B-domain of HMG1 (1993) EMBO Journal, 12 (4), pp. 1311-1319
Isernia, C., Bucci, E., Leone, M., Zaccaro, L., Di Lello, P., Digilio, G., Esposito, S., Fattorusso, R., NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein (2003) ChemBioChem, 4 (2-3), pp. 171-180
Palumbo, R., Sampaolesi, M., De Marchis, F., Tonlorenzi, R., Colombetti, S., Mondino, A., Cossu, G., Bianchi, M.E., Extracellular HMGB1, a signal of tissue damage, induces mesoangioblast migration and proliferation (2004) Journal of Cell Biology, 164 (3), pp. 441-449. , DOI 10.1083/jcb.200304135
Nielsen, P.E., Egholm, M., Buchardt, O., Peptide nucleic acid (PNA). A DNA mimic with a peptide backbone (1994) Bioconjugate Chemistry, 5 (1), pp. 3-7
Musumeci, D., Roviello, G.N., Valente, M., Sapio, R., Pedone, C., Bucci, E.M., New synthesis of PNA-3′DNA linker monomers, useful building blocks to obtain PNA/DNA chimeras (2004) Biopolymers - Peptide Science Section, 76 (6), pp. 535-542. , DOI 10.1002/bip.20135
Musumeci, D., Valente, M., Bucci, E.M., More than antisense, targeting extracellular proteins by oligonucleotide analogues (2006) Screening, 2, pp. 32-33
Bucci, E.M., Valente, M., Musumeci, D., Sapio, R., Anro, V., Roviello, G.N., Moccia, M., ODN-based drugs for targeting of extracellular proteins (2007) Nucleosides, Nucleotides and Nucleic Acids, 26 (8-9), pp. 1047-1050. , DOI 10.1080/15257770701509602, PII 787863451
Dumitriu, I.E., Baruah, P., Manfredi, A.A., Bianchi, M.E., Rovere-Querini, P., HMGB1: Guiding immunity from within (2005) Trends in Immunology, 26 (7), pp. 381-387. , DOI 10.1016/j.it.2005.04.009, PII S1471490605001080
Lotze, M.T., Tracey, K.J., High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal (2005) Nature Reviews Immunology, 5 (4), pp. 331-342. , DOI 10.1038/nri1594
Oue, N., Phyu, P.A., Mitani, Y., Kuniyasu, H., Nakayama, H., Yasui, W., Genes involved in invasion and metastasis of gastric cancer identified by array-based hybridization and serial analysis of gene expression (2005) Oncology, 69 (SUPPL. 1), pp. 17-22. , DOI 10.1159/000086627
Sasahira, T., Akama, Y., Fujii, K., Kuniyasu, H., Expression of receptor for advanced glycation end products and HMGB1/amphoterin in colorectal adenomas (2005) Virchows Archiv, 446 (4), pp. 411-415. , DOI 10.1007/s00428-005-1210-x
Yang, H., Wang, H., Czura, C.J., Tracey, K.J., The cytokine activity of HMGB1 (2005) Journal of Leukocyte Biology, 78 (1), pp. 1-8. , DOI 10.1189/jlb.1104648
Zeh III, H.J., Lotze, M.T., Addicted to death: Invasive cancer and the immune response to unscheduled cell death (2005) Journal of Immunotherapy, 28 (1), pp. 1-9
Kokkola, R., Andersson, A., Mullins, G., Ostberg, T., Treutiger, C.-J., Arnold, B., Nawroth, P., Harris, H.E., RAGE is the major receptor for the proinflammatory activity of HMGB1 in rodent macrophages (2005) Scandinavian Journal of Immunology, 61 (1), pp. 1-9. , DOI 10.1111/j.0300-9475.2005.01534.x
Zimmermann, K., Volkel, D., Pable, S., Lindner, T., Kramberger, F., Bahrami, S., Scheiflinger, F., Native versus recombinant high-mobility group B1 proteins: Functional activity in vitro (2004) Inflammation, 28 (4), pp. 221-229. , DOI 10.1023/B:IFLA.0000049047.61014.e3
Mitola, S., Belleri, M., Urbinati, C., Coltrini, D., Sparatore, B., Pedrazzi, M., Melloni, E., Presta, M., Cutting edge: Extracellular high mobility group box-1 protein is a proangiogenic cytokine (2006) Journal of Immunology, 176 (1), pp. 12-15
Higashi, T., Sano, H., Saishoji, T., Ikeda, K., Jinnouchi, Y., Kanzaki, T., Morisaki, N., Horiuchi, S., The receptor for advanced glycation end products mediates the chemotaxis of rabbit smooth muscle cells (1997) Diabetes, 46 (3), pp. 463-472
Degryse, B., Bonaldi, T., Scaffidi, P., Muller, S., Resnati, M., Sanvito, F., Arrigoni, G., Bianchi, M.E., The high mobility group (HMG) boxes of the nuclear protein HMG1 induce chemotaxis and cytoskeleton reorganization in rat smooth muscle cells (2001) Journal of Cell Biology, 152 (6), pp. 1197-1206. , DOI 10.1083/jcb.152.6.1197
Rouhiainen, A., Kuja-Panula, J., Wilkman, E., Pakkanen, J., Stenfors, J., Tuominen, R.K., Lepantalo, M., Rauvala, H., Regulation of monocyte migration by amphoterin (HMGB1) (2004) Blood, 104 (4), pp. 1174-1182. , DOI 10.1182/blood-2003-10-3536
Schlueter, C., Weber, H., Meyer, B., Rogalla, P., Roser, K., Hauke, S., Bullerdiek, J., Angiogenetic signaling through hypoxia HMGB1: An angiogenetic switch molecule (2005) American Journal of Pathology, 166 (4), pp. 1259-1263
Borgatti, M., Lampronti, I., Romanelli, A., Pedone, C., Saviano, M., Bianchi, N., Mischiati, C., Gambari, R., Transcription factor decoy molecules based on a peptide nucleic acid (PNA)-DNA chimera mimicking Sp1 binding sites (2003) Journal of Biological Chemistry, 278 (9), pp. 7500-7509. , DOI 10.1074/jbc.M206780200
Borgatti, M., Romanelli, A., Saviano, M., Pedone, C., Lampronti, I., Breda, L., Nastruzzi, C., Gambari, R., Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum (2002) Oncology Research, 13 (5), pp. 279-287
Uhlmann, E., Peptide nucleic acids (PNA) and PNA-DNA chimeras: From high binding affinity towards biological function (1998) Biological Chemistry, 379 (8-9), pp. 1045-1052
Zannetti, A., Del Vecchio, S., Romanelli, A., Scala, S., Saviano, M., Cali, G., Stoppelli, M.P., Salvatore, M., Inhibition of Sp1 activity by a decoy PNA-DNA chimera prevents urokinase receptor expression and migration of breast cancer cells (2005) Biochemical Pharmacology, 70 (9), pp. 1277-1287. , DOI 10.1016/j.bcp.2005.07.024, PII S0006295205004971
Ma, S.-F., Garcia, J.G.N., Reuning, U., Little, S.P., Bang, N.U., Dixon, E.P., Thrombin induces thrombomodulin mRNA expression via the proteolytically activated thrombin receptor in cultured bovine smooth muscle cells (1997) Journal of Laboratory and Clinical Medicine, 129 (6), pp. 611-619
Huttunen, H. J., Fages, C., Rauvala, H., Receptor for advanced glycation end products (RAGE) -mediated neurite outgrowth and activation of NF-kappaB require the cytoplasmic domain of the receptor but different downstream signaling pathways (1999) J. Biol. Chem., 274, pp. 19919-19924
Huttunen, H. J., Kuja-Panula, J., Rauvala, H., Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation (2002) Journal of Biological Chemistry, 277 (41), pp. 38635-38646. , DOI 10. 1074/jbc. M202515200
Lander, H. M., Tauras, J. M., Ogiste, J. S., Hori, O., Moss, R. A., Schmidt, A. M., Activation of the receptor for advanced glycation end products triggers a p21 (ras) -dependent mitogen-activated protein kinase pathway regulated by oxidant stress (1997) Journal of Biological Chemistry, 272 (28), pp. 17810-17814. , DOI 10. 1074/jbc. 272. 28. 17810
Allain, F. H. -T., Yen, Y. -M., Masse, J. E., Schultze, P., Dieckmann, T., Johnson, R. C., Feigon, J., Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding (1999) EMBO Journal, 18 (9), pp. 2563-2579. , DOI 10. 1093/emboj/18. 9. 2563
Bianchi, M. E., Falciola, L., Ferrari, S., Lilley, D. M., The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins (1992) EMBO J., 11, pp. 1055-1063
Hardman, C. H., Broadhurst, R. W., Raine, A. R. C., Grasser, K. D., Thomas, J. O., Laue, E. D., Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy (1995) Biochemistry, 34 (51), pp. 16596-16607. , DOI 10. 1021/bi00051a007
Harley, V. R., Jackson, D. I., Hextall, P. J., Hawkins, J. R., Berkovitz, G. D., Sockanathan, S., Lovell-Badge, R., Goodfellow, P. N., DNA binding activity of recombinant SRY from normal males and XY females (1992) Science, 255 (5043), pp. 453-456
Weir, H. M., Kraulis, P. J., Hill, C. S., Raine, A. R. C., Laue, E. D., Thomas, J. O., Structure of the HMG box motif in the B-domain of HMG1 (1993) EMBO Journal, 12 (4), pp. 1311-1319
Nielsen, P. E., Egholm, M., Buchardt, O., Peptide nucleic acid (PNA). A DNA mimic with a peptide backbone (1994) Bioconjugate Chemistry, 5 (1), pp. 3-7
Bucci, E. M., Valente, M., Musumeci, D., Sapio, R., Anro, V., Roviello, G. N., Moccia, M., ODN-based drugs for targeting of extracellular proteins (2007) Nucleosides, Nucleotides and Nucleic Acids, 26 (8-9), pp. 1047-1050. , DOI 10. 1080/15257770701509602, PII 787863451
Dumitriu, I. E., Baruah, P., Manfredi, A. A., Bianchi, M. E., Rovere-Querini, P., HMGB1: Guiding immunity from within (2005) Trends in Immunology, 26 (7), pp. 381-387. , DOI 10. 1016/j. it. 2005. 04. 009, PII S1471490605001080
Lotze, M. T., Tracey, K. J., High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal (2005) Nature Reviews Immunology, 5 (4), pp. 331-342. , DOI 10. 1038/nri1594
Oue, N., Phyu, P. A., Mitani, Y., Kuniyasu, H., Nakayama, H., Yasui, W., Genes involved in invasion and metastasis of gastric cancer identified by array-based hybridization and serial analysis of gene expression (2005) Oncology, 69 (SUPPL. 1), pp. 17-22. , DOI 10. 1159/000086627
Zeh III, H. J., Lotze, M. T., Addicted to death: Invasive cancer and the immune response to unscheduled cell death (2005) Journal of Immunotherapy, 28 (1), pp. 1-9
Ma, S. -F., Garcia, J. G. N., Reuning, U., Little, S. P., Bang, N. U., Dixon, E. P., Thrombin induces thrombomodulin mRNA expression via the proteolytically activated thrombin receptor in cultured bovine smooth muscle cells (1997) Journal of Laboratory and Clinical Medicine, 129 (6), pp. 611-619
Mol Biosyst (ISSN: 1742-206x, 1742-2051, 1742-2051electronic), 2011 May; 7(5): 1742-1752.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.534, 5-year impact factor: 3.705
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79954550870&partnerID=40&md5=0910849612aa81cf202011f723666191
Keywords: Circular Dna, Heteroduplex, High Mobility Group B1 Protein, Kinked Dna, Lipopolysaccharide, Peptide Nucleic Acid, Animal, Article, Bagg Albino Mouse, Binding Site, Cell Line, Cell Motion, Cell Proliferation, Chemical Structure, Chemically Induced Disorder, Chemistry, Conformation, Drug Antagonism, Drug Effect, Endotoxemia, Metabolism, Mortality, Nucleotide Sequence, Protein Binding, Protein Tertiary Structure, Survival Rate, Base Sequence, Cell Movement, Hmgb1 Protein, Inbred Balb C, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Nucleic Acid Heteroduplexes, Protein Structure, Time Factors,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini - CNR, via Mezzocannone 16, 80134 Napoli, Italy
Bionucleon Srl, via Ribes 5, 10010 Colleretto Giacosa (TO), Italy
DIBIT, San Raffaele University, via Olgettina 58, 20132 Milano, Italy
References:
Shingo, Y., Ikuro, M., HMGB1, a novel inflammatory cytokine (2007) Clin. Chim. Acta, 375, pp. 36-4
Agresti, A., Bianchi, M.E., HMGB proteins and gene expression (2003) Current Opinion in Genetics and Development, 13 (2), pp. 170-178. , DOI 10.1016/S0959-437X(03)00023-6
Degryse, B., De Virgilio, M., The nuclear protein HMGB1, a new kind of chemokine? (2003) FEBS Letters, 553 (1-2), pp. 11-17. , DOI 10.1016/S0014-5793(03)01027-5
Ishihara, K., Tsutsumi, K., Kawane, S., Nakajima, M., Kasaoka, T., The receptor for advanced glycation end-products (RAGE) directly binds to ERK by a D-domain-like docking site (2003) FEBS Letters, 550 (1-3), pp. 107-113. , DOI 10.1016/S0014-5793(03)00846-9
Huttunen, H.J., Fages, C., Rauvala, H., Receptor for advanced glycation end products (RAGE)-mediated neurite outgrowth and activation of NF-kappaB require the cytoplasmic domain of the receptor but different downstream signaling pathways (1999) J. Biol. Chem., 274, pp. 19919-19924
Huttunen, H.J., Kuja-Panula, J., Rauvala, H., Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation (2002) Journal of Biological Chemistry, 277 (41), pp. 38635-38646. , DOI 10.1074/jbc.M202515200
Lander, H.M., Tauras, J.M., Ogiste, J.S., Hori, O., Moss, R.A., Schmidt, A.M., Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress (1997) Journal of Biological Chemistry, 272 (28), pp. 17810-17814. , DOI 10.1074/jbc.272.28.17810
Li, J., Kokkola, R., Tabibzadeh, S., Yang, R., Ochani, M., Qiang, X., Harris, H.E., Yang, H., Structural basis for the proinflammatory cytokine activity of high mobility group box 1 (2003) Molecular Medicine, 9 (1-2), pp. 37-45
Ito, I., Mitsuoka, N., Sobajima, J., Uesugi, H., Ozaki, S., Ohya, K., Yoshida, M., Conformational difference in HMGB1 proteins of human neutrophils and lymphocytes revealed by epitope mapping of a monoclonal antibody (2004) Journal of Biochemistry, 136 (2), pp. 155-162. , DOI 10.1093/jb/mvh107
Yamada, S., Inoue, K., Yakabe, K., Imaizumi, H., Maruyama, I., High mobility group protein 1 (HMGB1) quantified by ELISA with a monoclonal antibody that does not cross-react with HMGB2 (2003) Clinical Chemistry, 49 (9), pp. 1535-1537. , DOI 10.1373/49.9.1535
Allain, F.H.-T., Yen, Y.-M., Masse, J.E., Schultze, P., Dieckmann, T., Johnson, R.C., Feigon, J., Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding (1999) EMBO Journal, 18 (9), pp. 2563-2579. , DOI 10.1093/emboj/18.9.2563
Bianchi, M.E., Falciola, L., Ferrari, S., Lilley, D.M., The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins (1992) EMBO J., 11, pp. 1055-1063
Cerdan, R., Payet, D., Yang, J.-C., Travers, A.A., Neuhaus, D., HMG-D complexed to a bulge DNA: An NMR model (2001) Protein Science, 10 (3), pp. 504-518. , DOI 10.1110/ps.35501
Hardman, C.H., Broadhurst, R.W., Raine, A.R.C., Grasser, K.D., Thomas, J.O., Laue, E.D., Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy (1995) Biochemistry, 34 (51), pp. 16596-16607. , DOI 10.1021/bi00051a007
Jaouen, S., De Koning, L., Gaillard, C., Muselikova-Polanska, E., Stros, M., Strauss, F., Determinants of specific binding of HMGB1 protein to hemicatenated DNA loops (2005) Journal of Molecular Biology, 353 (4), pp. 822-837. , DOI 10.1016/j.jmb.2005.08.073, PII S0022283605010533
Lorenz, M., Hillisch, A., Payet, D., Buttinelli, M., Travers, A., Diekmann, S., DNA bending induced by high mobility group proteins studied by fluorescence resonance energy transfer (1999) Biochemistry, 38, pp. 12150-12158
Payet, D., Hillisch, A., Lowe, N., Diekmann, S., Travers, A., The recognition of distorted DNA structures by HMG-D: A footprinting and molecular modelling study (1999) J. Mol. Biol., 294, pp. 79-91
Webb, M., Payet, D., Lee, K.-B., Travers, A.A., Thomas, J.O., Structural requirements for cooperative binding of HMG1 to DNA minicircles (2001) Journal of Molecular Biology, 309 (1), pp. 79-88. , DOI 10.1006/jmbi.2001.4667
Harley, V.R., Jackson, D.I., Hextall, P.J., Hawkins, J.R., Berkovitz, G.D., Sockanathan, S., Lovell-Badge, R., Goodfellow, P.N., DNA binding activity of recombinant SRY from normal males and XY females (1992) Science, 255 (5043), pp. 453-456
Dornberger, U., Hillisch, A., Gollmick, F.A., Fritzsche, H., Diekmann, S., Solution structure of a five-adenine bulge loop within a DNA duplex (1999) Biochemistry, 38, pp. 12860-12868
Weir, H.M., Kraulis, P.J., Hill, C.S., Raine, A.R.C., Laue, E.D., Thomas, J.O., Structure of the HMG box motif in the B-domain of HMG1 (1993) EMBO Journal, 12 (4), pp. 1311-1319
Isernia, C., Bucci, E., Leone, M., Zaccaro, L., Di Lello, P., Digilio, G., Esposito, S., Fattorusso, R., NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein (2003) ChemBioChem, 4 (2-3), pp. 171-180
Palumbo, R., Sampaolesi, M., De Marchis, F., Tonlorenzi, R., Colombetti, S., Mondino, A., Cossu, G., Bianchi, M.E., Extracellular HMGB1, a signal of tissue damage, induces mesoangioblast migration and proliferation (2004) Journal of Cell Biology, 164 (3), pp. 441-449. , DOI 10.1083/jcb.200304135
Nielsen, P.E., Egholm, M., Buchardt, O., Peptide nucleic acid (PNA). A DNA mimic with a peptide backbone (1994) Bioconjugate Chemistry, 5 (1), pp. 3-7
Musumeci, D., Roviello, G.N., Valente, M., Sapio, R., Pedone, C., Bucci, E.M., New synthesis of PNA-3′DNA linker monomers, useful building blocks to obtain PNA/DNA chimeras (2004) Biopolymers - Peptide Science Section, 76 (6), pp. 535-542. , DOI 10.1002/bip.20135
Musumeci, D., Valente, M., Bucci, E.M., More than antisense, targeting extracellular proteins by oligonucleotide analogues (2006) Screening, 2, pp. 32-33
Bucci, E.M., Valente, M., Musumeci, D., Sapio, R., Anro, V., Roviello, G.N., Moccia, M., ODN-based drugs for targeting of extracellular proteins (2007) Nucleosides, Nucleotides and Nucleic Acids, 26 (8-9), pp. 1047-1050. , DOI 10.1080/15257770701509602, PII 787863451
Dumitriu, I.E., Baruah, P., Manfredi, A.A., Bianchi, M.E., Rovere-Querini, P., HMGB1: Guiding immunity from within (2005) Trends in Immunology, 26 (7), pp. 381-387. , DOI 10.1016/j.it.2005.04.009, PII S1471490605001080
Lotze, M.T., Tracey, K.J., High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal (2005) Nature Reviews Immunology, 5 (4), pp. 331-342. , DOI 10.1038/nri1594
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DNA-based strategies for blocking HMGB1 cytokine activity: Design, synthesis and preliminary in vitro/in vivo assays of DNA and DNA-like duplexes
In this work we report the design and synthesis of kinked oligonucleotide duplexes as potential inhibitors of HMGB1, a cytokine which triggers a broad range of immunological effects. We found that the designed ligands can interact with HMGB1, as evidenced by circular dichroism spectroscopy, and are able to block some extracellular effects induced by the protein, such as cellular proliferation and migration, as we demonstrated by in vitro biological assays. After selecting the most stable and active kinked duplex, we synthesized the corresponding PNA/DNA chimeric duplex which resulted to be more resistant to enzymatic degradation, and showed a biological activity comparable to that of the natural duplex. Preliminary in vivo assays in a mouse inflammatory model, showed a significant decrease of the mortality after administration of the PNA/DNA kinked duplex to LPS-treated mice. © The Royal Society of Chemistry 2011.
In this work we report the design and synthesis of kinked oligonucleotide duplexes as potential inhibitors of HMGB1, a cytokine which triggers a broad range of immunological effects. We found that the designed ligands can interact with HMGB1, as evidenced by circular dichroism spectroscopy, and are able to block some extracellular effects induced by the protein, such as cellular proliferation and migration, as we demonstrated by in vitro biological assays. After selecting the most stable and active kinked duplex, we synthesized the corresponding PNA/DNA chimeric duplex which resulted to be more resistant to enzymatic degradation, and showed a biological activity comparable to that of the natural duplex. Preliminary in vivo assays in a mouse inflammatory model, showed a significant decrease of the mortality after administration of the PNA/DNA kinked duplex to LPS-treated mice. © The Royal Society of Chemistry 2011.
DNA-based strategies for blocking HMGB1 cytokine activity: Design, synthesis and preliminary in vitro/in vivo assays of DNA and DNA-like duplexes
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DNA-based strategies for blocking HMGB1 cytokine activity: Design, synthesis and preliminary in vitro/in vivo assays of DNA and DNA-like duplexes
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Impact Factor: 3.829
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Scalia M, Satriano C, Greca R, Stella AM, Rizzarelli E, Spina-Purrello V
* 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.
Impact Factor: 2.551
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Sorriento D, Fusco A, Ciccarelli M, Rungi A, Anastasio A, Carillo A, Dorn II GW, Trimarco B, Iaccarino G
* Mitochondrial G protein coupled receptor kinase 2 regulates proinflammatory responses in macrophages (385 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013; 587(21): 3487-3494.
Impact Factor: 3.341
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Dolga AM, Letsche T, Gold M, Doti N, Bacher M, Chiamvimonvat N, Dodel R, Culmsee C
* Activation of KCNN3/SK3/K(Ca)2. 3 channels attenuates enhanced calcium influx and inflammatory cytokine production in activated microglia (552 views)
Glia (ISSN: 1098-1136), 2012 Dec; 60(12): 2050-2064.
Impact Factor: 5.466
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Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (478 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
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Galdiero S, Falanga A, Cantisani M, Tarallo R, della Pepa ME, D'Oriano V, Galdiero M
* Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins (615 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 843-854.
Impact Factor: 2.326
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Berisio R
* Editorial: cell processes in bacterial diseases (409 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1011-1012.
Impact Factor: 1.994
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De Simone G
* Editorial: Zinc Metallo-Enzymes As Target For Drug Design (423 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2012 Feb; 19(6): 820-1012.
Impact Factor: 4.07
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Spina-Purrello V, Giliberto S, Barresi V, Nicoletti VG, Giuffrida Stella AM, Rizzarelli E
* Modulation of PARP-1 and PARP-2 expression by L-carnosine and trehalose after LPS and INFγ-induced oxidative stress (428 views)
Neurochemical Research (ISSN: 0364-3190, 1573-6903), 2010 Dec; 35(12): 2144-2153.
Impact Factor: 2.608
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Sorriento D, Ciccarelli M, Santulli G, Campanile A, Altobelli GG, Cimini V, Galasso G, Astone D, Piscione F, Pastore L, Trimarco B, Iaccarino G
* The G-protein-coupled receptor kinase 5 inhibits NFκB transcriptional activity by inducing nuclear accumulation of IκBα (438 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2008; 105(46): 17818-17823.
Impact Factor: 9.38
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Nicoletti VG, Santoro AM, Grasso G, Vagliasindi LI, Giuffrida ML, Cuppari C, Purrello VS, Stella AMG, Rizzarelli E
* Carnosine interaction with nitric oxide and astroglial cell protection (647 views)
Journal Of Neuroscience Research (ISSN: 0360-4012), 2007 Sep 1; 85(10): 2239-2245.
Impact Factor: 3.268
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Musumeci D, Roviello GN, Moccia M, Pedone C, Bucci EM, Sapio R, Valente M, Fumero S
* Bent oligonucleotide duplexes as HMGB1 inhibitors: A comparative study (348 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1525-7770), 2007; 26(10-12): 1447-1450.
Impact Factor: 0.723
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Calabrese V, Colombrita C, Guagliano E, Sapienza M, Ravagna A, Cardile V, Scapagnini G, Santoro AM, Mangiameli A, Butterfield DA, Giuffrida Stella AM, Rizzarelli E
* Protective effect of carnosine during nitrosative stress in astroglial cell cultures (379 views)
Neurochemical Research (ISSN: 0364-3190, 1573-6903), 2005 Jun; 30(6-7): 797-807.
Impact Factor: 2.187
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Paesano N, Marzocco S, Vicidomini C, Saturnino C, Autore G, De Martino G, Sbardella G
* Synthesis and biological evaluation of 3-benzyl-1-methyl- and 1-methyl-3-phenyl-isothioureas as potential inhibitors of iNOS (433 views)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2005 Feb 1; 15(3): 539-543.
Impact Factor: 2.478
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Menchise V, De Simone G, Tedeschi T, Corradini R, Sforza S, Marchelli R, Capasso D, Saviano M, Pedone C
* Insights into peptide nucleic acid (PNA) structural features: The crystal structure of a D-lysine-based chiral PNA-DNA duplex (504 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2003 Oct 14; 100(21): 12021-12026.
Impact Factor: 10.272
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Galdiero M, Vitiello M, Galdiero S
* Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (443 views)
Fems Microbiology Letters (ISSN: 0378-1097), 2003 Sep 12; 226(1): 57-64.
Impact Factor: 1.932
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Ogawa R, Pacelli R, Espey MG, Miranda KM, Friedman N, Kim SM, Cox G, Mitchell JB, Wink DA, Russo A
* Comparison of control of Listeria by nitric oxide redox chemistry from murine macrophages and no donors: Insights into listeriocidal activity of oxidative and nitrosative stress (688 views)
Free Radic Biol Med (ISSN: 0891-5849, 0891-5849linking, 1873-4596electronic), 2001 Feb 1; 30(3): 268-276.
Impact Factor: 5.082
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27 Records (27 excluding Abstracts).
Total impact factor: 109.907 (109.907 excluding Abstracts).
Total 5 year impact factor: 111.414 (111.414 excluding Abstracts).
Total impact factor: 109.907 (109.907 excluding Abstracts).
Total 5 year impact factor: 111.414 (111.414 excluding Abstracts).
462 views. Last view on Friday 10 March 2023, 13:19:28
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