Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation (508 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2011 Oct 10; 6(10): e25888-e25888.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.092, 5-year impact factor: 4.537
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-80053912078&partnerID=40&md5=0eb793207aa83ba1368c2b008d25af04
Keywords: Acylamino Acid Releasing Enzyme, Caspase, Immunoglobulin Enhancer Binding Protein, Linoleic Acid, Proteasome, Protein P21, Small Interfering Rna, Transmembrane Conductance Regulator, Ubiquitin, Acylaminoacyl Peptidase, Acylaminoacyl-Peptidase, Archaeal Protein, Conjugated Linoleic Acid, Oligopeptide, Peptide Hydrolase, Proteinase Inhibitor, Article, Cancer Growth, Cell Assay, Concentration Response, Conjugation, Controlled Study, Cytoplasm, Down Regulation, Enzyme Activation, Enzyme Activity, Enzyme Inhibition, Epithelium Cell, Genetic Transfection, Isomer, Protein Degradation, Signal Transduction, Ubiquitination, Animal, Apoptosis, Binding Site, Cell Strain Caco 2, Chemical Structure, Chemistry, Drug Design, Drug Effect, Drug Interaction, Enzyme Specificity, Human, Isomerism, Metabolism, Mutation, Protein Conformation, Sulfolobus Solfataricus, Caco-2 Cells, Cystic Fibrosis Transmembrane Conductance Regulator, Down-Regulation, Models, Molecular, Protease Inhibitors, Proteasome Endopeptidase Complex, Proteolysis, Substrate Specificity, Time Factors, Pharmacology, Deficiency,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, National Research Council (CNR-IBP), Napoli, Italy
Institute of Food Sciences, National Research Council (CNR-ISA), Avellino, Italy
Institute of Biostructure and Bioimaging, National Research Council (CNR-IBB), Napoli, Italy
Institute of Crystallography, National Council of Research of Italy (CNR-IC), Bari, Italy
Telethon Institute of Genetics and Medicine (TIGEM), Napoli, Italy
References:
Ciechanover, A., Proteolysis: from the lysosome to ubiquitin and the proteasome (2005) Nat Rev Mol Cell Biol, 6, pp. 79-8
Schwartz, A.L., Ciechanover, A., Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology (2009) Annu Rev Pharmacol Toxicol, 49, pp. 73-96
Shah, I.M., Di Napoli, M., The ubiquitin-proteasome system and proteasome inhibitors in central nervous system diseases (2007) Cardiovasc Hematol Disord Drug Targets, 7, pp. 250-273
Rajkumar, S.V., Richardson, P.G., Hideshima, T., Anderson, K.C., Proteasome inhibition as a novel therapeutic target in human cancer (2005) J Clin Oncol, 23, pp. 630-639
Naujokat, C., Sezer, O., Zinke, H., Leclere, A., Hauptmann, S., Proteasome inhibitors induced caspase-dependent apoptosis and accumulation of p21WAF1/Cip1 in human immature leukemic cells (2000) Eur J Haematol, 65, pp. 221-236
Drexler, H.C.A., Activation of the cell death program by inhibition of proteasome function (1997) Proc Natl Acad Sci USA, 94, pp. 855-860
Palombella, V.J., Rando, O.J., Goldberg, A.L., Maniatis, T., The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB (1994) Cell, 78, pp. 773-785
Nencioni, A., Grunebach, F., Patrone, F., Ballestrero, A., Brossart, P., Proteasome inhibitors: antitumor effects and beyond (2007) Leukemia, 21, pp. 30-36
Vlahakis, S.R., Badley, A.D., Influence of proteasome inhibitors on apoptosis (2006) Curr Opin Clin Nutr Metab Care, 9, pp. 42-47
Orlowski, R.Z., Kuhn, D.J., Proteasome Inhibitors in Cancer Therapy: Lessons from the First Decade (2008) Clin Cancer Res, 14, pp. 1649-1657
Landis-Piwowar, K.R., Milacic, V., Chen, D., Yang, H., Zhao, Y., The proteasome as a potential target for novel anticancer drugs and chemosensitizers (2006) Drug Resist Updat, 9, pp. 263-273
Serini, S., Piccioni, E., Merendino, N., Calviello, G., Dietary polyunsaturated fatty acids as inducers of apoptosis: implications for cancer (2009) Apoptosis, 14, pp. 135-152
Park, Y., Conjugated linoleic acid (CLA): Good or bad trans fat? (2009) J Food Compos Anal, 22 S, pp. S4-S12
Hamel, F.G., Preliminary report: inhibition of cellular proteasome activity by free fatty acids (2009) Metabolism, 58, pp. 1047-1049
Shimizu, K., Kiuchi, Y., Ando, K., Hayakawa, M., Kikugawa, K., Coordination of oxidized protein hydrolase and the proteasome in the clearance of cytotoxic denatured proteins (2004) Biochem Biophys Res Commun, 324, pp. 140-146
Scaloni, A., Jones, W., Pospischil, M., Sassa, S., Schneewind, O., Deficiency of acylpeptide hydrolase in small-cell lung carcinoma cell lines (1992) J Lab Clin Med, 120, pp. 546-552
Palmieri, G., Langella, E., Gogliettino, M., Saviano, M., Pocsfalvi, G., A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): a study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus (2010) Mol Biosyst, 6, pp. 2498-2507
Palmieri, G., Catara, G., Saviano, M., Langella, E., Gogliettino, M., First Archaeal PEPB-Serine Protease Inhibitor from Sulfolobus solfataricus with Noncanonical Amino Acid Sequence in the Reactive-Site Loop (2009) J Proteome Res, 8, pp. 327-334
Ponticelli, S., Marasco, D., Tarallo, V., Albuquerque, R.J., Mitola, S., Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1 (2008) J Biol Chem, 283, pp. 34250-34259
Cheng, S.H., Gregory, R.J., Marshall, J., Paul, S., Souza, D.W., Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis (1990) Cell, 63, pp. 827-834
Ward, C.L., Omura, S., Kopito, R.R., Degradation of CFTR by the ubiquitin-proteasome pathway (1995) Cell, 83, pp. 121-127
Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., Multiple proteolytic systems, including the proteasome, contribute to CFTR processing (1995) Cell, 83, pp. 129-135
Busse, A., Kraus, M., Na, I.K., Rietz, A., Scheibenbogen, C., Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits (2008) Cancer, 112, pp. 659-670
Chou, T.C., Talalay, P., Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors (1984) Adv Enzyme Regul, 22, pp. 27-55
Suzuki, Y., Nakabayashi, Y., Takahashi, R., Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death (2001) Proc Natl Acad Sci USA, 98, pp. 8662-8667
Hideshima, T., Chauhan, D., Richardson, P., Mitsiades, C., Mitsiades, N., NF-kappa B as a therapeutic target in multiple myeloma (2002) J Biol Chem, 277, pp. 16639-16647
Wertz, I.E., Dixit, V.M., Signaling to NF-kappaB: regulation by ubiquitination (2010) Cold Spring Harb Perspect Biol 2010 Mar, 2 (3), pp. a003350. , (Ed. Louis M. Staudt and Michael Karin)
Bloom, J., Amador, V., Bartolini, F., DeMartino, G., Pagano, M., Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation (2003) Cell, 115, pp. 71-82
Moore, H.E., Davenport, E.L., Smith, E.M., Muralikrishnan, S., Dunlop, A.S., Aminopeptidase inhibition as a targeted treatment strategy in myeloma (2009) Mol Cancer Ther, 8, pp. 762-770
Wahle, K.W.J., Heys, S.D., Rotondo, D., Conjugated linoleic acids: are they beneficial or detrimental to health? (2004) Progr Lipid Res, 43, pp. 553-587
Reynolds, C.M., Roche, H.M., Conjugated linoleic acid and inflammatory cell signalling (2010) Prostaglandins Leukot Essent Fatty Acids, 82, pp. 199-204
Bartlam, M., Wang, G., Yang, H., Gao, R., Zhao, X., Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (2004) Structure, 12, pp. 1481-1488
Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Automated docking using Lamarckian genetic algorithm and an empirical binding free energy function (1998) J Comput Chem, 19, pp. 1639-1662
Sacchinettini, J.C., Scapin, G., Gopaul, D., Gordon, J.I., Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75-A resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate (1992) J Biol Chem, 267, pp. 23534-23545
Hamilton, J.A., Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us (2004) Progr Lipid Res, 43, pp. 177-199
Nencioni, A., Grünebach, F., Patrone, F., Ballestrero, A., Brossart, P., Proteasome inhibitors: antitumor effects and beyond (2007) Leukemia, 21, pp. 30-36
Saric, T., Graef, C.I., Goldberg, A.L., Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases (2004) J Biol Chem, 279, pp. 46723-46732
Ichinose, Y., Genka, K., Koike, T., Kato, H., Watanabe, Y., Randomized double-blind placebo controlled trial of bestatin in patients with resected stage I squamous-cell carcinoma (2003) J Natl Cancer Inst, 95, pp. 605-610
Perrier, J., Durand, A., Giardina, T., Puigserver, A., Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase (2005) Biochimie, 87, pp. 673-685
Arnesen, T., van Damme, P., Polevoda, B., Helsens, K., Evjenth, R., Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans (2009) Proc Natl Acad Sci U S A, 106, pp. 8157-8162
Goetze, S., Qeli, E., Mosimann, C., Staes, A., Gerrits, B., Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster (2009) PLoS Biol, 7, pp. e1000236
Boissel, J.P., Kasper, T.J., Bunn, H.F., Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin (1988) J Biol Chem, 263, pp. 8443-8449
Kouzarides, T., Acetylation: a regulatory modification to rival phosphorylation? (2000) EMBO J, 19, pp. 1176-1179
Shimizu, K., Fujino, T., Ando, K., Hayakawa, M., Yasuda, H., Overexpression of oxidized protein hydrolase protect COS-7 cells from oxidative stress-induced inhibition of cell growth and survival (2003) Biochem Biophys Res Commun, 304, pp. 766-771
Ben Saadon, R., Fajerman, I., Ziv, T., Hellman, U., Schwartz, A.L., The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue (2004) J Biol Chem, 279, pp. 41414-41421
Hwang, C.S., Shemorry, A., Varshavsky, A., N-terminal acetylation of cellular proteins creates specific degradation signals (2010) Science, 327, pp. 973-977
Fields, G.B., Noble, R.L., Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids (1990) Int J Pept Protein Res, 35, pp. 161-214
Decker, T., Lohmann-Matthes, M.L., A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity (1988) J Immunol Methods, 115, pp. 61-69
Koradi, R., Billeter, M., Wüthrich, K., MOLMOL: a program for display and analysis of macromolecular structures (1996) J Mol Graph, 14, pp. 51-55+29-32
Schwartz, A. L., Ciechanover, A., Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology (2009) Annu Rev Pharmacol Toxicol, 49, pp. 73-96
Shah, I. M., Di Napoli, M., The ubiquitin-proteasome system and proteasome inhibitors in central nervous system diseases (2007) Cardiovasc Hematol Disord Drug Targets, 7, pp. 250-273
Rajkumar, S. V., Richardson, P. G., Hideshima, T., Anderson, K. C., Proteasome inhibition as a novel therapeutic target in human cancer (2005) J Clin Oncol, 23, pp. 630-639
Drexler, H. C. A., Activation of the cell death program by inhibition of proteasome function (1997) Proc Natl Acad Sci USA, 94, pp. 855-860
Palombella, V. J., Rando, O. J., Goldberg, A. L., Maniatis, T., The ubiquitinproteasome pathway is required for processing the NF- B1 precursor protein and the activation of NF- B (1994) Cell, 78, pp. 773-785
Vlahakis, S. R., Badley, A. D., Influence of proteasome inhibitors on apoptosis (2006) Curr Opin Clin Nutr Metab Care, 9, pp. 42-47
Orlowski, R. Z., Kuhn, D. J., Proteasome Inhibitors in Cancer Therapy: Lessons from the First Decade (2008) Clin Cancer Res, 14, pp. 1649-1657
Landis-Piwowar, K. R., Milacic, V., Chen, D., Yang, H., Zhao, Y., The proteasome as a potential target for novel anticancer drugs and chemosensitizers (2006) Drug Resist Updat, 9, pp. 263-273
Hamel, F. G., Preliminary report: inhibition of cellular proteasome activity by free fatty acids (2009) Metabolism, 58, pp. 1047-1049
Cheng, S. H., Gregory, R. J., Marshall, J., Paul, S., Souza, D. W., Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis (1990) Cell, 63, pp. 827-834
Ward, C. L., Omura, S., Kopito, R. R., Degradation of CFTR by the ubiquitin-proteasome pathway (1995) Cell, 83, pp. 121-127
Jensen, T. J., Loo, M. A., Pind, S., Williams, D. B., Goldberg, A. L., Multiple proteolytic systems, including the proteasome, contribute to CFTR processing (1995) Cell, 83, pp. 129-135
Chou, T. C., Talalay, P., Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors (1984) Adv Enzyme Regul, 22, pp. 27-55
Wertz, I. E., Dixit, V. M., Signaling to NF-kappaB: regulation by ubiquitination (2010) Cold Spring Harb Perspect Biol 2010 Mar, 2 (3), pp. a003350. , (Ed. Louis M. Staudt and Michael Karin)
Moore, H. E., Davenport, E. L., Smith, E. M., Muralikrishnan, S., Dunlop, A. S., Aminopeptidase inhibition as a targeted treatment strategy in myeloma (2009) Mol Cancer Ther, 8, pp. 762-770
Wahle, K. W. J., Heys, S. D., Rotondo, D., Conjugated linoleic acids: are they beneficial or detrimental to health? (2004) Progr Lipid Res, 43, pp. 553-587
Reynolds, C. M., Roche, H. M., Conjugated linoleic acid and inflammatory cell signalling (2010) Prostaglandins Leukot Essent Fatty Acids, 82, pp. 199-204
Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Automated docking using Lamarckian genetic algorithm and an empirical binding free energy function (1998) J Comput Chem, 19, pp. 1639-1662
Sacchinettini, J. C., Scapin, G., Gopaul, D., Gordon, J. I., Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1. 75-A resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate (1992) J Biol Chem, 267, pp. 23534-23545
Hamilton, J. A., Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us (2004) Progr Lipid Res, 43, pp. 177-199
Nencioni, A., Gr nebach, F., Patrone, F., Ballestrero, A., Brossart, P., Proteasome inhibitors: antitumor effects and beyond (2007) Leukemia, 21, pp. 30-36
Boissel, J. P., Kasper, T. J., Bunn, H. F., Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin (1988) J Biol Chem, 263, pp. 8443-8449
Hwang, C. S., Shemorry, A., Varshavsky, A., N-terminal acetylation of cellular proteins creates specific degradation signals (2010) Science, 327, pp. 973-977
Fields, G. B., Noble, R. L., Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids (1990) Int J Pept Protein Res, 35, pp. 161-214
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2011 Oct 10; 6(10): e25888-e25888.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.092, 5-year impact factor: 4.537
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-80053912078&partnerID=40&md5=0eb793207aa83ba1368c2b008d25af04
Keywords: Acylamino Acid Releasing Enzyme, Caspase, Immunoglobulin Enhancer Binding Protein, Linoleic Acid, Proteasome, Protein P21, Small Interfering Rna, Transmembrane Conductance Regulator, Ubiquitin, Acylaminoacyl Peptidase, Acylaminoacyl-Peptidase, Archaeal Protein, Conjugated Linoleic Acid, Oligopeptide, Peptide Hydrolase, Proteinase Inhibitor, Article, Cancer Growth, Cell Assay, Concentration Response, Conjugation, Controlled Study, Cytoplasm, Down Regulation, Enzyme Activation, Enzyme Activity, Enzyme Inhibition, Epithelium Cell, Genetic Transfection, Isomer, Protein Degradation, Signal Transduction, Ubiquitination, Animal, Apoptosis, Binding Site, Cell Strain Caco 2, Chemical Structure, Chemistry, Drug Design, Drug Effect, Drug Interaction, Enzyme Specificity, Human, Isomerism, Metabolism, Mutation, Protein Conformation, Sulfolobus Solfataricus, Caco-2 Cells, Cystic Fibrosis Transmembrane Conductance Regulator, Down-Regulation, Models, Molecular, Protease Inhibitors, Proteasome Endopeptidase Complex, Proteolysis, Substrate Specificity, Time Factors, Pharmacology, Deficiency,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, National Research Council (CNR-IBP), Napoli, Italy
Institute of Food Sciences, National Research Council (CNR-ISA), Avellino, Italy
Institute of Biostructure and Bioimaging, National Research Council (CNR-IBB), Napoli, Italy
Institute of Crystallography, National Council of Research of Italy (CNR-IC), Bari, Italy
Telethon Institute of Genetics and Medicine (TIGEM), Napoli, Italy
References:
Ciechanover, A., Proteolysis: from the lysosome to ubiquitin and the proteasome (2005) Nat Rev Mol Cell Biol, 6, pp. 79-8
Schwartz, A.L., Ciechanover, A., Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology (2009) Annu Rev Pharmacol Toxicol, 49, pp. 73-96
Shah, I.M., Di Napoli, M., The ubiquitin-proteasome system and proteasome inhibitors in central nervous system diseases (2007) Cardiovasc Hematol Disord Drug Targets, 7, pp. 250-273
Rajkumar, S.V., Richardson, P.G., Hideshima, T., Anderson, K.C., Proteasome inhibition as a novel therapeutic target in human cancer (2005) J Clin Oncol, 23, pp. 630-639
Naujokat, C., Sezer, O., Zinke, H., Leclere, A., Hauptmann, S., Proteasome inhibitors induced caspase-dependent apoptosis and accumulation of p21WAF1/Cip1 in human immature leukemic cells (2000) Eur J Haematol, 65, pp. 221-236
Drexler, H.C.A., Activation of the cell death program by inhibition of proteasome function (1997) Proc Natl Acad Sci USA, 94, pp. 855-860
Palombella, V.J., Rando, O.J., Goldberg, A.L., Maniatis, T., The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB (1994) Cell, 78, pp. 773-785
Nencioni, A., Grunebach, F., Patrone, F., Ballestrero, A., Brossart, P., Proteasome inhibitors: antitumor effects and beyond (2007) Leukemia, 21, pp. 30-36
Vlahakis, S.R., Badley, A.D., Influence of proteasome inhibitors on apoptosis (2006) Curr Opin Clin Nutr Metab Care, 9, pp. 42-47
Orlowski, R.Z., Kuhn, D.J., Proteasome Inhibitors in Cancer Therapy: Lessons from the First Decade (2008) Clin Cancer Res, 14, pp. 1649-1657
Landis-Piwowar, K.R., Milacic, V., Chen, D., Yang, H., Zhao, Y., The proteasome as a potential target for novel anticancer drugs and chemosensitizers (2006) Drug Resist Updat, 9, pp. 263-273
Serini, S., Piccioni, E., Merendino, N., Calviello, G., Dietary polyunsaturated fatty acids as inducers of apoptosis: implications for cancer (2009) Apoptosis, 14, pp. 135-152
Park, Y., Conjugated linoleic acid (CLA): Good or bad trans fat? (2009) J Food Compos Anal, 22 S, pp. S4-S12
Hamel, F.G., Preliminary report: inhibition of cellular proteasome activity by free fatty acids (2009) Metabolism, 58, pp. 1047-1049
Shimizu, K., Kiuchi, Y., Ando, K., Hayakawa, M., Kikugawa, K., Coordination of oxidized protein hydrolase and the proteasome in the clearance of cytotoxic denatured proteins (2004) Biochem Biophys Res Commun, 324, pp. 140-146
Scaloni, A., Jones, W., Pospischil, M., Sassa, S., Schneewind, O., Deficiency of acylpeptide hydrolase in small-cell lung carcinoma cell lines (1992) J Lab Clin Med, 120, pp. 546-552
Palmieri, G., Langella, E., Gogliettino, M., Saviano, M., Pocsfalvi, G., A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): a study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus (2010) Mol Biosyst, 6, pp. 2498-2507
Palmieri, G., Catara, G., Saviano, M., Langella, E., Gogliettino, M., First Archaeal PEPB-Serine Protease Inhibitor from Sulfolobus solfataricus with Noncanonical Amino Acid Sequence in the Reactive-Site Loop (2009) J Proteome Res, 8, pp. 327-334
Ponticelli, S., Marasco, D., Tarallo, V., Albuquerque, R.J., Mitola, S., Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1 (2008) J Biol Chem, 283, pp. 34250-34259
Cheng, S.H., Gregory, R.J., Marshall, J., Paul, S., Souza, D.W., Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis (1990) Cell, 63, pp. 827-834
Ward, C.L., Omura, S., Kopito, R.R., Degradation of CFTR by the ubiquitin-proteasome pathway (1995) Cell, 83, pp. 121-127
Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., Multiple proteolytic systems, including the proteasome, contribute to CFTR processing (1995) Cell, 83, pp. 129-135
Busse, A., Kraus, M., Na, I.K., Rietz, A., Scheibenbogen, C., Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits (2008) Cancer, 112, pp. 659-670
Chou, T.C., Talalay, P., Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors (1984) Adv Enzyme Regul, 22, pp. 27-55
Suzuki, Y., Nakabayashi, Y., Takahashi, R., Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death (2001) Proc Natl Acad Sci USA, 98, pp. 8662-8667
Hideshima, T., Chauhan, D., Richardson, P., Mitsiades, C., Mitsiades, N., NF-kappa B as a therapeutic target in multiple myeloma (2002) J Biol Chem, 277, pp. 16639-16647
Wertz, I.E., Dixit, V.M., Signaling to NF-kappaB: regulation by ubiquitination (2010) Cold Spring Harb Perspect Biol 2010 Mar, 2 (3), pp. a003350. , (Ed. Louis M. Staudt and Michael Karin)
Bloom, J., Amador, V., Bartolini, F., DeMartino, G., Pagano, M., Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation (2003) Cell, 115, pp. 71-82
Moore, H.E., Davenport, E.L., Smith, E.M., Muralikrishnan, S., Dunlop, A.S., Aminopeptidase inhibition as a targeted treatment strategy in myeloma (2009) Mol Cancer Ther, 8, pp. 762-770
Wahle, K.W.J., Heys, S.D., Rotondo, D., Conjugated linoleic acids: are they beneficial or detrimental to health? (2004) Progr Lipid Res, 43, pp. 553-587
Reynolds, C.M., Roche, H.M., Conjugated linoleic acid and inflammatory cell signalling (2010) Prostaglandins Leukot Essent Fatty Acids, 82, pp. 199-204
Bartlam, M., Wang, G., Yang, H., Gao, R., Zhao, X., Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (2004) Structure, 12, pp. 1481-1488
Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Automated docking using Lamarckian genetic algorithm and an empirical binding free energy function (1998) J Comput Chem, 19, pp. 1639-1662
Sacchinettini, J.C., Scapin, G., Gopaul, D., Gordon, J.I., Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75-A resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate (1992) J Biol Chem, 267, pp. 23534-23545
Hamilton, J.A., Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us (2004) Progr Lipid Res, 43, pp. 177-199
Nencioni, A., Grünebach, F., Patrone, F., Ballestrero, A., Brossart, P., Proteasome inhibitors: antitumor effects and beyond (2007) Leukemia, 21, pp. 30-36
Saric, T., Graef, C.I., Goldberg, A.L., Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases (2004) J Biol Chem, 279, pp. 46723-46732
Ichinose, Y., Genka, K., Koike, T., Kato, H., Watanabe, Y., Randomized double-blind placebo controlled trial of bestatin in patients with resected stage I squamous-cell carcinoma (2003) J Natl Cancer Inst, 95, pp. 605-610
Perrier, J., Durand, A., Giardina, T., Puigserver, A., Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase (2005) Biochimie, 87, pp. 673-685
Arnesen, T., van Damme, P., Polevoda, B., Helsens, K., Evjenth, R., Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans (2009) Proc Natl Acad Sci U S A, 106, pp. 8157-8162
Goetze, S., Qeli, E., Mosimann, C., Staes, A., Gerrits, B., Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster (2009) PLoS Biol, 7, pp. e1000236
Boissel, J.P., Kasper, T.J., Bunn, H.F., Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin (1988) J Biol Chem, 263, pp. 8443-8449
Kouzarides, T., Acetylation: a regulatory modification to rival phosphorylation? (2000) EMBO J, 19, pp. 1176-1179
Shimizu, K., Fujino, T., Ando, K., Hayakawa, M., Yasuda, H., Overexpression of oxidized protein hydrolase protect COS-7 cells from oxidative stress-induced inhibition of cell growth and survival (2003) Biochem Biophys Res Commun, 304, pp. 766-771
Ben Saadon, R., Fajerman, I., Ziv, T., Hellman, U., Schwartz, A.L., The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue (2004) J Biol Chem, 279, pp. 41414-41421
Hwang, C.S., Shemorry, A., Varshavsky, A., N-terminal acetylation of cellular proteins creates specific degradation signals (2010) Science, 327, pp. 973-977
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Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation
Acylpeptide hydrolase (APEH), one of the four members of the prolyl oligopeptidase class, catalyses the removal of N-acylated amino acids from acetylated peptides and it has been postulated to play a key role in protein degradation machinery. Disruption of protein turnover has been established as an effective strategy to down-regulate the ubiquitin-proteasome system (UPS) and as a promising approach in anticancer therapy. Here, we illustrate a new pathway modulating UPS and proteasome activity through inhibition of APEH. To find novel molecules able to down-regulate APEH activity, we screened a set of synthetic peptides, reproducing the reactive-site loop of a known archaeal inhibitor of APEH (SsCEI), and the conjugated linoleic acid (CLA) isomers. A 12-mer SsCEI peptide and the trans10-cis12 isomer of CLA, were identified as specific APEH inhibitors and their effects on cell-based assays were paralleled by a dose-dependent reduction of proteasome activity and the activation of the pro-apoptotic caspase cascade. Moreover, cell treatment with the individual compounds increased the cytoplasm levels of several classic hallmarks of proteasome inhibition, such as NFkappaB, p21, and misfolded or polyubiquitinylated proteins, and additive effects were observed in cells exposed to a combination of both inhibitors without any cytotoxicity. Remarkably, transfection of human bronchial epithelial cells with APEH siRNA, promoted a marked accumulation of a mutant of the cystic fibrosis transmembrane conductance regulator (CFTR), herein used as a model of misfolded protein typically degraded by UPS. Finally, molecular modeling studies, to gain insights into the APEH inhibition by the trans10-cis12 CLA isomer, were performed. Our study supports a previously unrecognized role of APEH as a negative effector of proteasome activity by an unknown mechanism and opens new perspectives for the development of strategies aimed at modulation of cancer progression. © 2011 Palmieri et al.
Acylpeptide hydrolase (APEH), one of the four members of the prolyl oligopeptidase class, catalyses the removal of N-acylated amino acids from acetylated peptides and it has been postulated to play a key role in protein degradation machinery. Disruption of protein turnover has been established as an effective strategy to down-regulate the ubiquitin-proteasome system (UPS) and as a promising approach in anticancer therapy. Here, we illustrate a new pathway modulating UPS and proteasome activity through inhibition of APEH. To find novel molecules able to down-regulate APEH activity, we screened a set of synthetic peptides, reproducing the reactive-site loop of a known archaeal inhibitor of APEH (SsCEI), and the conjugated linoleic acid (CLA) isomers. A 12-mer SsCEI peptide and the trans10-cis12 isomer of CLA, were identified as specific APEH inhibitors and their effects on cell-based assays were paralleled by a dose-dependent reduction of proteasome activity and the activation of the pro-apoptotic caspase cascade. Moreover, cell treatment with the individual compounds increased the cytoplasm levels of several classic hallmarks of proteasome inhibition, such as NFkappaB, p21, and misfolded or polyubiquitinylated proteins, and additive effects were observed in cells exposed to a combination of both inhibitors without any cytotoxicity. Remarkably, transfection of human bronchial epithelial cells with APEH siRNA, promoted a marked accumulation of a mutant of the cystic fibrosis transmembrane conductance regulator (CFTR), herein used as a model of misfolded protein typically degraded by UPS. Finally, molecular modeling studies, to gain insights into the APEH inhibition by the trans10-cis12 CLA isomer, were performed. Our study supports a previously unrecognized role of APEH as a negative effector of proteasome activity by an unknown mechanism and opens new perspectives for the development of strategies aimed at modulation of cancer progression. © 2011 Palmieri et al.
Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation
| ▼ Structural characterization of the porphyrins/proteasome interaction |
Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation
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Sciacca MFM, Milardi D, Pappalardo M, La Rosa C, Grasso DM
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Borgatti M, Finotti A, Romanelli A, Saviano M, Bianchi N, Lampronti I, Lambertini E, Penolazzi L, Nastruzzi C, Mischiati C, Piva R, Pedone C, Gambari R
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Mischiati C, Sereni A, Finotti A, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Pedone C, Borgatti M, Gambari R
* Complexation to cationic microspheres of double-stranded peptide nucleic acid-DNA chimeras exhibiting decoy activity (378 views)
Journal Of Biomedical Science (ISSN: 1021-7770), 2004 Sep; 11(5): 697-704.
Impact Factor: 1.567
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Penolazzi L, Borgatti M, Lambertini E, Mischiati C, Finotti A, Romanelli A, Saviano M, Pedone C, Piva R, Gambari R
* Peptide nucleic acid-DNA decoy chimeras targeting NF-kappa B transcription factors: Induction of apoptosis in human primary osteoclasts (312 views)
International Journal Of Molecular Medicine (ISSN: 1107-3756), 2004 Sep; 14(2): 145-152.
Impact Factor: 3.19
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Galdiero M, Vitiello M, Galdiero S
* Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (549 views)
Fems Microbiology Letters (ISSN: 0378-1097), 2003 Sep 12; 226(1): 57-64.
Impact Factor: 1.932
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Borgatti M, Romanelli A, Saviano M, Pedone C, Lampronti I, Breda L, Nastruzzi C, Bianchi N, Mischiati C, Gambari R
* Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum (430 views)
Oncology Research (ISSN: 0965-0407), 2003; 13(5): 279-287.
Impact Factor: 1.794
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Borgatti M, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Mischiati C, Pedone C, Gambari R
* Cationic Liposomes As Delivery Systems For Double-Stranded Pna-Dna Chimeras Exhibiting Decoy Activity Against Nf-Kappab Transcription Factors (431 views)
Biochem Pharmacol Biochemical Pharmacology (ISSN: 1873-2968, 0006-2952), 2002 Sep 15; 64(4): 609-616.
Impact Factor: 3.542
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Romanelli A, Pedone C, Saviano M, Bianchi N, Borgatti M, Mischiati C, Gambari R
* Molecular interactions between nuclear factor κB (NF-κB) transcription factors and a PNA-DNA chimera mimicking NF-κB binding sites (435 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print, 0014-2956linking), 2001 Dec; 268(23): 6066-6075.
Impact Factor: 2.849
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Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S
* Fusion in Coq (481 views)
Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596.
Impact Factor: 0.415
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Saviano M, Romanelli A, Bucci E, Pedone C, Mischiati C, Bianchi N, Feriotto G, Borgatti M, Gambari R
Computational procedures to explain the different biological activity of DNA/DNA, DNA/PNA and PNA/PNA hybrid molecules mimicking NF-κB binding sites (494 views)
J Biomol Struct Dyn (ISSN: 0739-1102, 1538-0254electronic, 0739-1102linking), 2000 Dec; 18(3): 353-362.
Impact Factor: 1.826
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Fogliano V, Ritieni A, Monti SM, Gallo M, Della Medaglia D, Ambrosino ML, Sacchi R
Antioxidant activity of virgin olive oil phenolic compounds in a micellar system (301 views)
Journal Of The Science Of Food And Agriculture (ISSN: 0022-5142), 1999 Oct; 79(13): 1803-1808.
Impact Factor: 1.097
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* Selective inhibition of acylpeptide hydrolase in SAOS-2 osteosarcoma cells: is this enzyme a viable anticancer target? (21 views)
Mol Biol Rep (ISSN: 0301-4851linking), 2021 Feb; 48(2): 1505-1519.
Impact Factor: 2.316
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Santoro AM, D'Urso A, Cunsolo A, Milardi D, Purrello R, Sbardella D, Tundo GR, Coletta M, Diana D, Fattorusso R, Persico M, Fattorusso C
* Closing or opening proteasome doors by porphyrins (12 views)
Smart Elab, 2021; N/D: N/D-N/D.
Impact Factor: 0
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Santoro AM, D’urso A, Cunsolo A, Milardi D, Purrello R, Sbardella D, Tundo GR, Diana D, Fattorusso R, Di Dato A, Paladino A, Persico M, Coletta M, Fattorusso C
Cooperative binding of the cationic porphyrin tris-t4 enhances catalytic activity of 20s proteasome unveiling a complex distribution of functional states (21 views)
International Journal Of Molecular Sciences, 2020; N/D: N/D-N/D.
Impact Factor: 0
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Sbardella D, Tundo GR, Coletta A, Marcoux J, Koufogeorgou EI, Ciaccio C, Santoro AM, Milardi D, Grasso G, Cozza P, Bousquet-dubouch MP, Marini S, Coletta M
* The insulin-degrading enzyme is an allosteric modulator of the 20S proteasome and a potential competitor of the 19S (278 views) (PDF 110 views)
Cell Mol Life Sci (ISSN: 1420-9071electronic, 1420-682xlinking), 2018 Sep; 75(18): 3441-3456.
Impact Factor: 7.047
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Dato AD, Cunsolo A, Persico M, Santoro AM, D'Urso A, Milardi D, Purrello R, Stefanelli M, Paolesse R, Tundo GR, Sbardella D, Fattorusso C, Coletta M
* Electrostatic Map Of Proteasome alpha-Rings Encodes The Design of Allosteric Porphyrin-Based Inhibitors Able To Affect 20S Conformation By Cooperative Binding (361 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2017 Dec 6; 7(1): 17098-17098.
Impact Factor: 4.122
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Oliveri V, Lanza V, Milardi D, Viale M, Maric I, Sgarlata C, Vecchio G
* Amino- and chloro-8-hydroxyquinolines and their copper complexes as proteasome inhibitors and antiproliferative agents (478 views)
Metallomics (ISSN: 1756-5901, 1756-591x), 2017 Oct 18; 9(10): 1439-1446.
Impact Factor: 4.069
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Tomasello MF, Nardon C, Lanza V, Di Natale G, Pettenuzzo N, Salmaso S, Milardi D, Caliceti P, Pappalardo G, Fregona D
* New comprehensive studies of a gold(III) Dithiocarbamate complex with proven anticancer properties: Aqueous dissolution with cyclodextrins, pharmacokinetics and upstream inhibition of the ubiquitin-proteasome pathway (618 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2017 Jun 19; 138: 115-127.
Impact Factor: 4.816
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Tundo GR, Sbardella D, Ciaccio C, Grasso G, Gioia M, Coletta A, Polticelli F, Di Pierro D, Milardi D, Van Endert P, Marini S, Coletta M
* Multiple functions of insulin-degrading enzyme: a metabolic crosslight? (312 views)
Crit Rev Biochem Mol (ISSN: 1040-9238), 2017 Jun; N/D: 1-29.
Impact Factor: 5.279
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Palmieri G, Cocca E, Gogliettino M, Valentino R, Ruvo M, Cristofano G, Angiolillo A, Balestrieri M, Rossi M, Di Costanzo A
* Low Erythrocyte Levels of Proteasome and Acyl-Peptide Hydrolase (APEH) Activities in Alzheimer's Disease: A Sign of Defective Proteostasis? (350 views)
J Alzheimers Dis (ISSN: 1387-2877, 1387-2877linking), 2017; 60(3): 1097-1106.
Impact Factor: 3.476
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Palumbo R, Gogliettino M, Cocca E, Iannitti R, Sandomenico A, Ruvo M, Balestrieri M, Rossi M, Palmieri G
* APEH Inhibition Affects Osteosarcoma Cell Viability via Downregulation of the Proteasome (341 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2016 Sep 23; 17(10): N/D-N/D.
Impact Factor: 3.226
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Santoro AM, Monaco I, Attanasio F, Lanza V, Pappalardo G, Tomasello MF, Cunsolo A, Rizzarelli E, De Luigi A, Salmona M, Milardi D
* Copper(II) ions affect the gating dynamics of the 20S proteasome: a molecular and in cell study (358 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2016 Sep 16; 6: 33444-33444.
Impact Factor: 4.259
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Santoro AM, Cunsolo A, D'Urso A, Sbardella D, Tundo GR, Ciaccio C, Coletta M, Diana D, Fattorusso R, Persico M, Di Dato A, Fattorusso C, Milardi D, Purrello R
* Cationic porphyrins are tunable gatekeepers of the 20S proteasome (679 views) (PDF 233 views)
Chem Sci (ISSN: 2041-6520, 2041-6520linking, 2041-6520print), 2016; 7(2): 1286-1297.
Impact Factor: 8.668
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Tornatore L, Sandomenico A, Raimondo D, Low C, Rocci A, Tralau-Stewart C, Capece D, D'Andrea D, Bua M, Boyle E, van Duin M, Zoppoli P, Jaxa-Chamiec A, Thotakura AK, Dyson J, Walker BA, Leonardi A, Chambery A, Driessen C, Sonneveld P, Morgan G, Palumbo A, Tramontano A, Rahemtulla A, Ruvo M, Franzoso G
* Cancer-selective targeting of the NF-kappaB survival pathway with GADD45beta/MKK7 inhibitors (624 views)
Cancer Cell (ISSN: 1535-6108), 2014 Oct 13; 26(4): 495-508.
Impact Factor: 23.523
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Calce E, Mignogna E, Bugatti V, Galdiero M, Vittoria V, De Luca S
* Pectin functionalized with natural fatty acids as antimicrobial agent (391 views)
Int J Biol Macromol (ISSN: 0141-8130, 0141-8130linking, 1879-0003electronic), 2014 Jul; 68: 28-32.
Impact Factor: 2.858
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Ciccarelli M, Rusciano MR, Sorriento D, Basilicata MF, Santulli G, Campiglia P, Bertamino A, De Luca N, Trimarco B, Iaccarino G, Illario M
* CaMKII protects MKP-1 from proteasome degradation in endothelial cells (259 views)
Cell Signal (ISSN: 0898-6568), 2014; 26(10): 2167-2174.
Impact Factor: 4.315
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Bergamo P, Cocca E, Palumbo R, Gogliettino M, Rossi M, Palmieri G
* RedOx status, proteasome and APEH: Insights into anticancer mechanisms of t10, c12-conjugated linoleic acid isomer on A375 melanoma cells (742 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2013 Nov 19; 8(11): N/D-N/D.
Impact Factor: 3.534
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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 (428 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013; 587(21): 3487-3494.
Impact Factor: 3.341
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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 (676 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 843-854.
Impact Factor: 2.326
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Santoro AM, Lo Giudice MC, D'Urso A, Lauceri R, Purrello R, Milardi D
* Cationic porphyrins are reversible proteasome inhibitors (447 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2012 Jun 27; 134(25): 10451-10457.
Impact Factor: 10.677
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Calabrese V, Cornelius C, Dinkova-Kostova AT, Iavicoli I, Di Paola R, Koverech A, Cuzzocrea S, Rizzarelli E, Calabrese EJ
* Cellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity (4574 views)
Bba-Gen Subjects (ISSN: 0006-3002, 0925-4439, 1570-9639), 2012 May; 1822(5): 753-783.
Impact Factor: 3.733
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Sandomenico A, Russo A, Palmieri G, Bergamo P, Gogliettino M, Falcigno L, Ruvo M
* Small peptide inhibitors of acetyl-peptide hydrolase having an uncommon mechanism of inhibition and a stable bent conformation (521 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2012 Mar 8; 55(5): 2102-2111.
Impact Factor: 5.614
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Vitiello M, Galdiero M, Finamore E, Galdiero S, Galdiero M
* NF-κB as a potential therapeutic target in microbial diseases (487 views)
Mol Biosyst (ISSN: 1742-206x), 2012; 8(4): 1108-1120.
Impact Factor: 3.35
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Cantisani M, Vitiello M, Falanga A, Finamore E, Galdiero M, Galdiero S
* Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity (528 views)
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2012; 7: 2361-2371.
Impact Factor: 3.463
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Arena G, Fattorusso R, Grasso G, Grasso GI, Isernia C, Malgieri G, Milardi D, Rizzarelli E
* Zinc(II) complexes of ubiquitin: speciation, affinity and binding features (595 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Oct 4; 17(41): 11596-11603.
Impact Factor: 5.925
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Calabrese V, Cornelius C, Cuzzocrea S, Iavicoli I, Rizzarelli E, Calabrese EJ
* Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity (900 views)
Molecular Aspects Of Medicine (ISSN: 1872-9452, 0098-2997), 2011 Sep; 32(4-6): 279-304.
Impact Factor: 9.97
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Palmieri D, Valentino T, D'Angelo D, De Martino I, Postiglione I, Pacelli R, Croce CM, Fedele M, Fusco A
* HMGA proteins promote ATM expression and enhance cancer cell resistance to genotoxic agents (919 views)
Oncogene (ISSN: 0950-9232, 1476-5594), 2011 Jul 7; 30(27): 3024-3035.
Impact Factor: 6.373
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Janda E, Palmieri C, Pisano A, Pontoriero M, Iaccino E, Falcone C, Fiume G, Gaspari M, Nevolo M, Di Salle E, Rossi A, De Laurentiis A, Greco A, Di Napoli D, Verheij E, Britti D, Lavecchia L, Quinto I, Scala G
* Btk regulation in human and mouse B cells via protein kinase C phosphorylation of IBtkγ (452 views)
Blood (ISSN: 0006-4971, 0006-6497, 0390-6078), 2011 Jun 16; 117(24): 6520-6531.
Impact Factor: 9.898
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Monfregola L, Bugatti V, Amodeo P, De Luca S, Vittoria V
* Physical and Water Sorption Properties of Chemically Modified Pectin with an Environmentally Friendly Process (286 views)
Biomacromolecules (ISSN: 1525-7797), 2011 Jun; 12(6): 2311-2318.
Impact Factor: 5.479
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Ciccarelli M, Sorriento D, Cipolletta E, Santulli G, Fusco A, Zhou R-H, Eckhart AD, Peppel K, Koch WJ, Trimarco B, Iaccarino G
* Impaired neoangiogenesis in β2-adrenoceptor gene-deficient mice: Restoration by intravascular human β2-adrenoceptor gene transfer and role of NFkB and CREB transcription factors (370 views)
Br J Pharmacol British Journal Of Pharmacology (ISSN: 0007-1188), 2011; 162(3): 712-721.
Impact Factor: 4.409
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Romano S, D'Angelillo A, Pacelli R, Staibano S, De Luna E, Bisogni R, Eskelinen EL, Mascolo M, Calì G, Arra C, Romano M
* Role of FK506-binding protein 51 in the control of apoptosis of irradiated melanoma cells (470 views)
Cell Death Differ (ISSN: 1350-9047, 1476-5403electronic, 1350-9047linking), 2010 Jan; 17(1): 145-157.
Impact Factor: 9.05
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Sorriento D, Santulli G, Fusco A, Anastasio A, Trimarco B, Iaccarino G
* Intracardiac injection of AdGRK5-NT reduces left ventricular hypertrophy by inhibiting NF-κB-Dependent hypertrophic gene expression (502 views)
Hypertensionhypertension (ISSN: 0194-911x), 2010; 56(4): 696-704.
Impact Factor: 6.908
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Sorriento D, Iaccarino G, Trimarco B
The role of the transcription factor nuclear factor kappa B in the regulation of cardiac hypertrophy (455 views)
High Blood Press Cardiovasc Prev High Blood Pressure And Cardiovascular Prevention (ISSN: 1120-9879), 2010; 17(4): 209-217.
Impact Factor: 0
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Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S
* Viral fusion peptides induce several signal transduction pathway activations that are essential for interleukin-10 and beta-interferon production (478 views)
Intervirology (ISSN: 1423-0100, 0300-5526), 2010; 53(6): 381-389.
Impact Factor: 1.756
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Arnesano F, Scintilla S, Calò V, Bonfrate E, Ingrosso C, Losacco M, Pellegrino T, Rizzarelli E, Natile G
* Copper-triggered aggregation of ubiquitin (534 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 16; 4(9): e7052-e7052.
Impact Factor: 4.351
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Marasco D, Stilo R, Sandomenico A, Monti SM, Tizzano B, De Capua A, Varricchio E, Liguoro D, Zotti T, Formisano S, Ruvo M, Vito P
* Generation And Functional Characterization Of A Bcl10-Inhibitory Peptide That Represses Nf-Kappa B Activation (602 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2009 Sep 15; 422(3): 553-561.
Impact Factor: 5.155
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Sandomenico A, Monti SM, Sabatella M, De Capua A, Tornatore L, Doti N, Viparelli F, Dathan NA, Pedone C, Ruvo M, Marasco D
* Protein-protein interactions: a simple strategy to identify binding sites and peptide antagonists (607 views)
Chem Biol Drug Des (ISSN: 1747-0285, 1747-0277), 2009 May; 73(5): 483-493.
Impact Factor: 2.473
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Sorriento D, Campanile A, Santulli G, Leggiero E, Pastore L, Trimarco B, Iaccarino G
* A new synthetic protein, TAT-RH, inhibits tumor growth through the regulation of NFκB activity (359 views)
Mol Cancermolecular Cancer (ISSN: 1476-4598), 2009; 8: N/D-N/D.
Impact Factor: 4.16
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Chiechio S, Zammataro M, Morales ME, Busceti CL, Drago F, Th Gereau RW, Copani A, Nicoletti F
* Epigenetic modulation of mGlu2 receptors by histone deacetylase inhibitors in the treatment of inflammatory pain (587 views)
Mol Pharmacol (ISSN: 0026-895x), 2009; 75(5): 1014-1020.
Impact Factor: 4.531
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Calabrese V, Cornelius C, Mancuso C, Pennisi G, Calafato S, Bellia F, Bates TE, Giuffrida Stella AM, Schapira T, Dinkova Kostova AT, Rizzarelli E
* Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity (1402 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2008 Dec; 33(12): 2444-2471.
Impact Factor: 2.26
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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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Sciacca MFM, Milardi D, Pappalardo M, La Rosa C, Grasso DM
* Role of electrostatics in the thermal stability of ubiquitin: A combined DSC and MM study (248 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006 Nov; 86(2): 311-314.
Impact Factor: 1.438
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Borgatti M, Finotti A, Romanelli A, Saviano M, Bianchi N, Lampronti I, Lambertini E, Penolazzi L, Nastruzzi C, Mischiati C, Piva R, Pedone C, Gambari R
* Peptide nucleic acids (PNA)-DNA chimeras targeting transcription factors as a tool to modify gene expression (509 views)
Curr Drug Targets (ISSN: 1389-4501), 2004 Nov; 5(8): 735-744.
Impact Factor: 4.104
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Mischiati C, Sereni A, Finotti A, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Pedone C, Borgatti M, Gambari R
* Complexation to cationic microspheres of double-stranded peptide nucleic acid-DNA chimeras exhibiting decoy activity (378 views)
Journal Of Biomedical Science (ISSN: 1021-7770), 2004 Sep; 11(5): 697-704.
Impact Factor: 1.567
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Penolazzi L, Borgatti M, Lambertini E, Mischiati C, Finotti A, Romanelli A, Saviano M, Pedone C, Piva R, Gambari R
* Peptide nucleic acid-DNA decoy chimeras targeting NF-kappa B transcription factors: Induction of apoptosis in human primary osteoclasts (312 views)
International Journal Of Molecular Medicine (ISSN: 1107-3756), 2004 Sep; 14(2): 145-152.
Impact Factor: 3.19
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Galdiero M, Vitiello M, Galdiero S
* Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (549 views)
Fems Microbiology Letters (ISSN: 0378-1097), 2003 Sep 12; 226(1): 57-64.
Impact Factor: 1.932
View Export to BibTeX Export to EndNote
Borgatti M, Romanelli A, Saviano M, Pedone C, Lampronti I, Breda L, Nastruzzi C, Bianchi N, Mischiati C, Gambari R
* Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum (430 views)
Oncology Research (ISSN: 0965-0407), 2003; 13(5): 279-287.
Impact Factor: 1.794
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Borgatti M, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Mischiati C, Pedone C, Gambari R
* Cationic Liposomes As Delivery Systems For Double-Stranded Pna-Dna Chimeras Exhibiting Decoy Activity Against Nf-Kappab Transcription Factors (431 views)
Biochem Pharmacol Biochemical Pharmacology (ISSN: 1873-2968, 0006-2952), 2002 Sep 15; 64(4): 609-616.
Impact Factor: 3.542
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Romanelli A, Pedone C, Saviano M, Bianchi N, Borgatti M, Mischiati C, Gambari R
* Molecular interactions between nuclear factor κB (NF-κB) transcription factors and a PNA-DNA chimera mimicking NF-κB binding sites (435 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print, 0014-2956linking), 2001 Dec; 268(23): 6066-6075.
Impact Factor: 2.849
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Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S
* Fusion in Coq (481 views)
Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596.
Impact Factor: 0.415
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Saviano M, Romanelli A, Bucci E, Pedone C, Mischiati C, Bianchi N, Feriotto G, Borgatti M, Gambari R
Computational procedures to explain the different biological activity of DNA/DNA, DNA/PNA and PNA/PNA hybrid molecules mimicking NF-κB binding sites (494 views)
J Biomol Struct Dyn (ISSN: 0739-1102, 1538-0254electronic, 0739-1102linking), 2000 Dec; 18(3): 353-362.
Impact Factor: 1.826
View Export to BibTeX Export to EndNote
Fogliano V, Ritieni A, Monti SM, Gallo M, Della Medaglia D, Ambrosino ML, Sacchi R
Antioxidant activity of virgin olive oil phenolic compounds in a micellar system (301 views)
Journal Of The Science Of Food And Agriculture (ISSN: 0022-5142), 1999 Oct; 79(13): 1803-1808.
Impact Factor: 1.097
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51 Records (49 excluding Abstracts).
Total impact factor: 229.844 (221.959 excluding Abstracts).
Total 5 year impact factor: 241.016 (232.618 excluding Abstracts).
Total impact factor: 229.844 (221.959 excluding Abstracts).
Total 5 year impact factor: 241.016 (232.618 excluding Abstracts).
508 views. Last view on Monday 05 June 2023, 3:05:58
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