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.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 10.677, 5-year impact factor: 10.237
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84863490720&partnerID=40&md5=504f1817a8bdc96bcee859fd239e8b72
Keywords: Anticancer Properties, Axial Coordination, Cationic Porphyrin, Central Metals, Inhibition Activity, Inhibition Assays, Inhibitory Effect, Macrocycles, Metalloporphyrins, Micromolar Range, Molecular Levels, Peptidase Activity, Protease Activities, Proteasome Inhibitors, Spectroscopic Characterization, Uv-Vis Spectra, Water-Soluble Porphyrin, Dyes, Metal Ions, Scaffolds, Anion, Antineoplastic Agent, Cationic Porphyrin Derivative, Macrocyclic Compound, Proteinase, Unclassified Drug, Amino Terminal Sequence, Article, Canonical Analysis, Cell Assay, Controlled Study, Drug Activity, Drug Effect, Drug Efficacy, Drug Protein Binding, Drug Structure, Drug Targeting, Enzyme Activity, Human, Human Cell, Molecular Docking, Protein Structure, Protein Subunit, Static Electricity, Ultraviolet Radiation, Enzyme Activation, Enzyme Inhibitors, Hela Cells, Models, Proteasome Endopeptidase Complex, Cations Pharmacology, Enzyme Activation Drug Effects, Enzyme Inhibitors Pharmacology, Porphyrins Pharmacology,
Affiliations:
*** IBB - CNR ***
IBB-CNR, Istituto di Biostrutture e Bioimmagini, UOS di Catania C/o Dipartimento di Scienze Chimiche, Viale A. Doria 6, 95125 Catania, Italy
ISE-CNR, Istituto per Lo Studio Degli Ecosistemi, Largo Tonolli, 50, 28922 Verbania Pallanza (VB), Italy
Department of Periodontology and Biomaterials, Radboud University Nijmegen Medical Center, Philips van Leydenlaan 25, 6525 EX Nijmegen, Netherlands
References:
Maiti, N.C., Mazumdar, S., Periasamy, N., (1998) J. Phys. Chem. B, 102, pp. 1528-153
Lauceri, R., Raudino, A., Monsù Scolaro, L., Micali, N., Purrello, R., (2002) J. Am. Chem. Soc., 124, pp. 894-895
Segawa, H., Takehara, C., Honda, K., Shimidzu, T., Asahi, T., Mataga, N., (1992) J. Phys. Chem., 2, pp. 503-506
Pasternack, R.F., Francesconi, L., Raff, D., Spiro, E., (1973) Inorg. Chem., 11, pp. 2606-2611
Pasternack, R.F., Gibbs, E.J., Villafranca, J.J., (1983) Biochemistry, 22, pp. 2406-2414
D'Urso, A., Holmes, A.E., Berova, N., Balaz, M., Purrello, R., (2011) Chem. Asian J., 6, pp. 3104-3109
Shohei, S., Atsuhiro, O., (2011) Angew Chem. Int., 50, pp. 4342-4373
Dougherty, T.J., Gomer, C.J., Henderson, B.W., Jori, G., (1998) J. Natl. Cancer. Inst., 90, pp. 889-905
Pandey, R.K., Zheng, G., (2000) The Porphyrin Handbook, 6, pp. 157-230. , In
Kadish, K. M. Smith, K. M. Guilard, R. Academic Press, Boston
Celli, J.P., Spring, B.Q., Rizvi, I., Evans, C.L., Samkoe, K.S., Verma, S., Pogue, B.W., Hasan, T., (2010) Chem. Rev., 110, pp. 2795-2838
Barth, R.F., Coderre, J.A., Vicente, M.G., Blue, T.E., (2005) Clin. Cancer Res., 11, pp. 3987-4002
Soloway, A.H., Tjarks, W., Barnum, B.A., Rong, F.G., Barth, R.F., Codogni, I.M., Wilson, J.G., (1998) Chem. Rev., 98, pp. 1515-1562
Dixon, I.M., Lopez, F., Estève, J.P., Tejera, A.M., Blasco, M.A., Pratviel, G., Meunier, B., (2005) Chembiochem., 6, pp. 123-132
Harley, C.B., Futcher, A.B., Greider, C.W., (1990) Nature, 345, pp. 458-460
Mergny, J.L., Riou, J.F., Mailliet, P., (2002) Nucleic Acids Res., 30, pp. 839-865
Szokalska, A., Makowski, M., Nowis, D., Wilczynski, G.M., Kujawa, M., Wójcik, C., Młynarczuk-Biały, I., Golab, J., (2009) Cancer Res., 69, pp. 4235-4243
Gallastegui, N., Groll, M., (2010) Trends Biochem. Sci., 35, pp. 634-642
Hershko, A., Ciechanover, A., (1998) Annu. Rev. Biochem., 67, pp. 425-479
Pickart, C.M., Cohen, R.E., (2004) Nat. Rev. Mol. Cell Biol., 5, pp. 177-187
Coux, O., Tanaka, K., Goldberg, A.L., (1996) Annu. Rev. Biochem., 65, pp. 810-847
Kisselev, A.F., Callard, A., Goldberg, A.L., (2006) J. Biol. Chem., 281, pp. 8582-8590
Matsuo, Y., Sawai, H., Ochi, N., Yasuda, A., Sakamoto, M., Takahashi, H., Funahashi, H., Guha, S., (2010) Dig. Dis. Sci., 55, pp. 1167-1176
Adams, J., (2004) Cancer Cell., 5, pp. 417-421
Crawford, L.J., Walker, B., Ovaa, H., Chauhan, D., Anderson, K.C., Morris, T.C., Irvine, A.E., (2006) Cancer Res., 66, pp. 6379-6386
Milardi, D., Arnesano, F., Grasso, G., Magrì, A., Tabbì, G., Scintilla, S., Natile, G., Rizzarelli, E., (2007) Angew. Chem Int. Ed., 46, pp. 7993-7995
Arena, G., Fattorusso, R., Grasso, G., Grasso, G.I., Isernia, C., Malgieri, G., Milardi, D., Rizzarelli, E., (2011) Chem.-Eur. J., 17, pp. 11596-11603
Demo, S.D., Kirk, C.J., Aujay, M.A., Buchholz, T.J., Dajee, M., Ho, M.N., Jiang, J., Bennett, M.K., (2007) Cancer Res., 67, pp. 6383-6391
Herrmansn, O., Ehdi, H.U., Orsin, A., (1978) Can. J. Chem., 56, pp. 1084-1087
Rodgers, K.J., Dean, R.T., (2003) Int. J. Biochem. Cell. Biol., 35, pp. 716-727
Copeland, R.A., (2005) Evaluation of Enzyme Inhibitors in Drug Discovery
Methods of Biochemical Analysis, p. 46. , In
Wiley Press: Hoboken, NJ
Trott, O., Olson, A.J., (2010) J. Comput. Chem., 31, pp. 455-461
Huey, R., Morris, G.M., Olson, A.J., Goodsell, D.S., (2007) J. Comput. Chem., 28, pp. 1145-1152
Dewar, M.J.S., Zoebisch, E.G., Healy, E.F., Stewart, J.J.P., (1985) J. Am. Chem. Soc., 107, pp. 3902-3909
De Bettignies, G., Coux, O., (2010) Biochimie, 92, pp. 1530-1545
Portero-Otín, M., Pamplona, R., Ruiz, M.C., Cabiscol, E., Prat, J., Bellmunt, M., (1999) J. Diabetes, 48, pp. 2215-2220
McNaught, K.S., Olanow, C.W., Halliwell, B., Isacson, O., Jenner, P., (2001) Nat. Rev. Neur., 2, pp. 589-594
Gaczynska, M., Rock, K.L., Spies, T., Goldberg, A.L., (1994) Proc. Natl. Acad. Sci. U.S.A., 91, pp. 9213-9217
Kisselev, A.F., Garcia-Calvo, M., Overkleeft, H.S., Peterson, E., Pennington, M.W., Ploegh, H.L., Thornberry, N.A., Goldberg, A.L., (2003) J. Biol. Chem., 278, pp. 35869-35877
Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., Schreiber, S.L., (1995) Science, 268, pp. 726-731
Stauch, B., Simon, B., Basile, T., Schneider, G., Malek, N.P., Kalesse, M., Carlomagno, T., (2010) Angew. Chem., 122, pp. 4026-4030
Parkinson, G.N., Ghosh, R., Neidle, S., (2007) Biochemistry, 46, pp. 2390-2397
Giordano, S., Petrelli, A., (2008) Curr. Med. Chem., 15, pp. 422-432
McMillin, D.R., Shelton, A.H., Bejune, S.A., Fanwick, P.E., Wall, R.K., (2005) Coord. Chem. Rev., 249, pp. 1451-1459
Mita, H., Ohyama, T., Tanaka, Y., Yamamoto, Y., (2006) Biochemistry, 45, pp. 6765-6772
Wang, K., Zhang, Z., Wu, L., Li, Z.-Y., (2007) Chem. Biodiv, pp. 514-522
Jia, G., Feng, Z., Wei, C., Zhou, J., Wang, X., Li, C., (2009) J. Phys. Chem.B, 113, pp. 16237-16245
Kornguth, S.E., Kalinke, T., Robins, H.I., Cohen, J.D., Turski, P., (1989) Cancer Res., 49, pp. 6390-6395
Dick, L.R., Fleming, P.E., (2010) Drug Discov. Today, 15, pp. 243-249
Blackburn, C., Gigstad, K.M., Hales, P., Garcia, K., Jones, M., Bruzzese, F.J., Barrett, C., Blank, J.L., (2010) Biochem. J., 430, pp. 461-476
Maiti, N. C., Mazumdar, S., Periasamy, N., (1998) J. Phys. Chem. B, 102, pp. 1528-153
Pasternack, R. F., Francesconi, L., Raff, D., Spiro, E., (1973) Inorg. Chem., 11, pp. 2606-2611
Dougherty, T. J., Gomer, C. J., Henderson, B. W., Jori, G., (1998) J. Natl. Cancer. Inst., 90, pp. 889-905
Pandey, R. K., Zheng, G., (2000) The Porphyrin Handbook, 6, pp. 157-230. , In
Celli, J. P., Spring, B. Q., Rizvi, I., Evans, C. L., Samkoe, K. S., Verma, S., Pogue, B. W., Hasan, T., (2010) Chem. Rev., 110, pp. 2795-2838
Barth, R. F., Coderre, J. A., Vicente, M. G., Blue, T. E., (2005) Clin. Cancer Res., 11, pp. 3987-4002
Soloway, A. H., Tjarks, W., Barnum, B. A., Rong, F. G., Barth, R. F., Codogni, I. M., Wilson, J. G., (1998) Chem. Rev., 98, pp. 1515-1562
Dixon, I. M., Lopez, F., Est ve, J. P., Tejera, A. M., Blasco, M. A., Pratviel, G., Meunier, B., (2005) Chembiochem., 6, pp. 123-132
Harley, C. B., Futcher, A. B., Greider, C. W., (1990) Nature, 345, pp. 458-460
Mergny, J. L., Riou, J. F., Mailliet, P., (2002) Nucleic Acids Res., 30, pp. 839-865
Pickart, C. M., Cohen, R. E., (2004) Nat. Rev. Mol. Cell Biol., 5, pp. 177-187
Kisselev, A. F., Callard, A., Goldberg, A. L., (2006) J. Biol. Chem., 281, pp. 8582-8590
Crawford, L. J., Walker, B., Ovaa, H., Chauhan, D., Anderson, K. C., Morris, T. C., Irvine, A. E., (2006) Cancer Res., 66, pp. 6379-6386
Demo, S. D., Kirk, C. J., Aujay, M. A., Buchholz, T. J., Dajee, M., Ho, M. N., Jiang, J., Bennett, M. K., (2007) Cancer Res., 67, pp. 6383-6391
Rodgers, K. J., Dean, R. T., (2003) Int. J. Biochem. Cell. Biol., 35, pp. 716-727
Copeland, R. A., (2005) Evaluation of Enzyme Inhibitors in Drug Discovery
Dewar, M. J. S., Zoebisch, E. G., Healy, E. F., Stewart, J. J. P., (1985) J. Am. Chem. Soc., 107, pp. 3902-3909
Portero-Ot n, M., Pamplona, R., Ruiz, M. C., Cabiscol, E., Prat, J., Bellmunt, M., (1999) J. Diabetes, 48, pp. 2215-2220
McNaught, K. S., Olanow, C. W., Halliwell, B., Isacson, O., Jenner, P., (2001) Nat. Rev. Neur., 2, pp. 589-594
Kisselev, A. F., Garcia-Calvo, M., Overkleeft, H. S., Peterson, E., Pennington, M. W., Ploegh, H. L., Thornberry, N. A., Goldberg, A. L., (2003) J. Biol. Chem., 278, pp. 35869-35877
Parkinson, G. N., Ghosh, R., Neidle, S., (2007) Biochemistry, 46, pp. 2390-2397
McMillin, D. R., Shelton, A. H., Bejune, S. A., Fanwick, P. E., Wall, R. K., (2005) Coord. Chem. Rev., 249, pp. 1451-1459
Kornguth, S. E., Kalinke, T., Robins, H. I., Cohen, J. D., Turski, P., (1989) Cancer Res., 49, pp. 6390-6395
Dick, L. R., Fleming, P. E., (2010) Drug Discov. Today, 15, pp. 243-249
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2012 Jun 27; 134(25): 10451-10457.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 10.677, 5-year impact factor: 10.237
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84863490720&partnerID=40&md5=504f1817a8bdc96bcee859fd239e8b72
Keywords: Anticancer Properties, Axial Coordination, Cationic Porphyrin, Central Metals, Inhibition Activity, Inhibition Assays, Inhibitory Effect, Macrocycles, Metalloporphyrins, Micromolar Range, Molecular Levels, Peptidase Activity, Protease Activities, Proteasome Inhibitors, Spectroscopic Characterization, Uv-Vis Spectra, Water-Soluble Porphyrin, Dyes, Metal Ions, Scaffolds, Anion, Antineoplastic Agent, Cationic Porphyrin Derivative, Macrocyclic Compound, Proteinase, Unclassified Drug, Amino Terminal Sequence, Article, Canonical Analysis, Cell Assay, Controlled Study, Drug Activity, Drug Effect, Drug Efficacy, Drug Protein Binding, Drug Structure, Drug Targeting, Enzyme Activity, Human, Human Cell, Molecular Docking, Protein Structure, Protein Subunit, Static Electricity, Ultraviolet Radiation, Enzyme Activation, Enzyme Inhibitors, Hela Cells, Models, Proteasome Endopeptidase Complex, Cations Pharmacology, Enzyme Activation Drug Effects, Enzyme Inhibitors Pharmacology, Porphyrins Pharmacology,
Affiliations:
*** IBB - CNR ***
IBB-CNR, Istituto di Biostrutture e Bioimmagini, UOS di Catania C/o Dipartimento di Scienze Chimiche, Viale A. Doria 6, 95125 Catania, Italy
ISE-CNR, Istituto per Lo Studio Degli Ecosistemi, Largo Tonolli, 50, 28922 Verbania Pallanza (VB), Italy
Department of Periodontology and Biomaterials, Radboud University Nijmegen Medical Center, Philips van Leydenlaan 25, 6525 EX Nijmegen, Netherlands
References:
Maiti, N.C., Mazumdar, S., Periasamy, N., (1998) J. Phys. Chem. B, 102, pp. 1528-153
Lauceri, R., Raudino, A., Monsù Scolaro, L., Micali, N., Purrello, R., (2002) J. Am. Chem. Soc., 124, pp. 894-895
Segawa, H., Takehara, C., Honda, K., Shimidzu, T., Asahi, T., Mataga, N., (1992) J. Phys. Chem., 2, pp. 503-506
Pasternack, R.F., Francesconi, L., Raff, D., Spiro, E., (1973) Inorg. Chem., 11, pp. 2606-2611
Pasternack, R.F., Gibbs, E.J., Villafranca, J.J., (1983) Biochemistry, 22, pp. 2406-2414
D'Urso, A., Holmes, A.E., Berova, N., Balaz, M., Purrello, R., (2011) Chem. Asian J., 6, pp. 3104-3109
Shohei, S., Atsuhiro, O., (2011) Angew Chem. Int., 50, pp. 4342-4373
Dougherty, T.J., Gomer, C.J., Henderson, B.W., Jori, G., (1998) J. Natl. Cancer. Inst., 90, pp. 889-905
Pandey, R.K., Zheng, G., (2000) The Porphyrin Handbook, 6, pp. 157-230. , In
Kadish, K. M. Smith, K. M. Guilard, R. Academic Press, Boston
Celli, J.P., Spring, B.Q., Rizvi, I., Evans, C.L., Samkoe, K.S., Verma, S., Pogue, B.W., Hasan, T., (2010) Chem. Rev., 110, pp. 2795-2838
Barth, R.F., Coderre, J.A., Vicente, M.G., Blue, T.E., (2005) Clin. Cancer Res., 11, pp. 3987-4002
Soloway, A.H., Tjarks, W., Barnum, B.A., Rong, F.G., Barth, R.F., Codogni, I.M., Wilson, J.G., (1998) Chem. Rev., 98, pp. 1515-1562
Dixon, I.M., Lopez, F., Estève, J.P., Tejera, A.M., Blasco, M.A., Pratviel, G., Meunier, B., (2005) Chembiochem., 6, pp. 123-132
Harley, C.B., Futcher, A.B., Greider, C.W., (1990) Nature, 345, pp. 458-460
Mergny, J.L., Riou, J.F., Mailliet, P., (2002) Nucleic Acids Res., 30, pp. 839-865
Szokalska, A., Makowski, M., Nowis, D., Wilczynski, G.M., Kujawa, M., Wójcik, C., Młynarczuk-Biały, I., Golab, J., (2009) Cancer Res., 69, pp. 4235-4243
Gallastegui, N., Groll, M., (2010) Trends Biochem. Sci., 35, pp. 634-642
Hershko, A., Ciechanover, A., (1998) Annu. Rev. Biochem., 67, pp. 425-479
Pickart, C.M., Cohen, R.E., (2004) Nat. Rev. Mol. Cell Biol., 5, pp. 177-187
Coux, O., Tanaka, K., Goldberg, A.L., (1996) Annu. Rev. Biochem., 65, pp. 810-847
Kisselev, A.F., Callard, A., Goldberg, A.L., (2006) J. Biol. Chem., 281, pp. 8582-8590
Matsuo, Y., Sawai, H., Ochi, N., Yasuda, A., Sakamoto, M., Takahashi, H., Funahashi, H., Guha, S., (2010) Dig. Dis. Sci., 55, pp. 1167-1176
Adams, J., (2004) Cancer Cell., 5, pp. 417-421
Crawford, L.J., Walker, B., Ovaa, H., Chauhan, D., Anderson, K.C., Morris, T.C., Irvine, A.E., (2006) Cancer Res., 66, pp. 6379-6386
Milardi, D., Arnesano, F., Grasso, G., Magrì, A., Tabbì, G., Scintilla, S., Natile, G., Rizzarelli, E., (2007) Angew. Chem Int. Ed., 46, pp. 7993-7995
Arena, G., Fattorusso, R., Grasso, G., Grasso, G.I., Isernia, C., Malgieri, G., Milardi, D., Rizzarelli, E., (2011) Chem.-Eur. J., 17, pp. 11596-11603
Demo, S.D., Kirk, C.J., Aujay, M.A., Buchholz, T.J., Dajee, M., Ho, M.N., Jiang, J., Bennett, M.K., (2007) Cancer Res., 67, pp. 6383-6391
Herrmansn, O., Ehdi, H.U., Orsin, A., (1978) Can. J. Chem., 56, pp. 1084-1087
Rodgers, K.J., Dean, R.T., (2003) Int. J. Biochem. Cell. Biol., 35, pp. 716-727
Copeland, R.A., (2005) Evaluation of Enzyme Inhibitors in Drug Discovery
Methods of Biochemical Analysis, p. 46. , In
Wiley Press: Hoboken, NJ
Trott, O., Olson, A.J., (2010) J. Comput. Chem., 31, pp. 455-461
Huey, R., Morris, G.M., Olson, A.J., Goodsell, D.S., (2007) J. Comput. Chem., 28, pp. 1145-1152
Dewar, M.J.S., Zoebisch, E.G., Healy, E.F., Stewart, J.J.P., (1985) J. Am. Chem. Soc., 107, pp. 3902-3909
De Bettignies, G., Coux, O., (2010) Biochimie, 92, pp. 1530-1545
Portero-Otín, M., Pamplona, R., Ruiz, M.C., Cabiscol, E., Prat, J., Bellmunt, M., (1999) J. Diabetes, 48, pp. 2215-2220
McNaught, K.S., Olanow, C.W., Halliwell, B., Isacson, O., Jenner, P., (2001) Nat. Rev. Neur., 2, pp. 589-594
Gaczynska, M., Rock, K.L., Spies, T., Goldberg, A.L., (1994) Proc. Natl. Acad. Sci. U.S.A., 91, pp. 9213-9217
Kisselev, A.F., Garcia-Calvo, M., Overkleeft, H.S., Peterson, E., Pennington, M.W., Ploegh, H.L., Thornberry, N.A., Goldberg, A.L., (2003) J. Biol. Chem., 278, pp. 35869-35877
Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., Schreiber, S.L., (1995) Science, 268, pp. 726-731
Stauch, B., Simon, B., Basile, T., Schneider, G., Malek, N.P., Kalesse, M., Carlomagno, T., (2010) Angew. Chem., 122, pp. 4026-4030
Parkinson, G.N., Ghosh, R., Neidle, S., (2007) Biochemistry, 46, pp. 2390-2397
Giordano, S., Petrelli, A., (2008) Curr. Med. Chem., 15, pp. 422-432
McMillin, D.R., Shelton, A.H., Bejune, S.A., Fanwick, P.E., Wall, R.K., (2005) Coord. Chem. Rev., 249, pp. 1451-1459
Mita, H., Ohyama, T., Tanaka, Y., Yamamoto, Y., (2006) Biochemistry, 45, pp. 6765-6772
Wang, K., Zhang, Z., Wu, L., Li, Z.-Y., (2007) Chem. Biodiv, pp. 514-522
Jia, G., Feng, Z., Wei, C., Zhou, J., Wang, X., Li, C., (2009) J. Phys. Chem.B, 113, pp. 16237-16245
Kornguth, S.E., Kalinke, T., Robins, H.I., Cohen, J.D., Turski, P., (1989) Cancer Res., 49, pp. 6390-6395
Dick, L.R., Fleming, P.E., (2010) Drug Discov. Today, 15, pp. 243-249
Blackburn, C., Gigstad, K.M., Hales, P., Garcia, K., Jones, M., Bruzzese, F.J., Barrett, C., Blank, J.L., (2010) Biochem. J., 430, pp. 461-476
Maiti, N. C., Mazumdar, S., Periasamy, N., (1998) J. Phys. Chem. B, 102, pp. 1528-153
Pasternack, R. F., Francesconi, L., Raff, D., Spiro, E., (1973) Inorg. Chem., 11, pp. 2606-2611
Dougherty, T. J., Gomer, C. J., Henderson, B. W., Jori, G., (1998) J. Natl. Cancer. Inst., 90, pp. 889-905
Pandey, R. K., Zheng, G., (2000) The Porphyrin Handbook, 6, pp. 157-230. , In
Celli, J. P., Spring, B. Q., Rizvi, I., Evans, C. L., Samkoe, K. S., Verma, S., Pogue, B. W., Hasan, T., (2010) Chem. Rev., 110, pp. 2795-2838
Barth, R. F., Coderre, J. A., Vicente, M. G., Blue, T. E., (2005) Clin. Cancer Res., 11, pp. 3987-4002
Soloway, A. H., Tjarks, W., Barnum, B. A., Rong, F. G., Barth, R. F., Codogni, I. M., Wilson, J. G., (1998) Chem. Rev., 98, pp. 1515-1562
Dixon, I. M., Lopez, F., Est ve, J. P., Tejera, A. M., Blasco, M. A., Pratviel, G., Meunier, B., (2005) Chembiochem., 6, pp. 123-132
Harley, C. B., Futcher, A. B., Greider, C. W., (1990) Nature, 345, pp. 458-460
Mergny, J. L., Riou, J. F., Mailliet, P., (2002) Nucleic Acids Res., 30, pp. 839-865
Pickart, C. M., Cohen, R. E., (2004) Nat. Rev. Mol. Cell Biol., 5, pp. 177-187
Kisselev, A. F., Callard, A., Goldberg, A. L., (2006) J. Biol. Chem., 281, pp. 8582-8590
Crawford, L. J., Walker, B., Ovaa, H., Chauhan, D., Anderson, K. C., Morris, T. C., Irvine, A. E., (2006) Cancer Res., 66, pp. 6379-6386
Demo, S. D., Kirk, C. J., Aujay, M. A., Buchholz, T. J., Dajee, M., Ho, M. N., Jiang, J., Bennett, M. K., (2007) Cancer Res., 67, pp. 6383-6391
Rodgers, K. J., Dean, R. T., (2003) Int. J. Biochem. Cell. Biol., 35, pp. 716-727
Copeland, R. A., (2005) Evaluation of Enzyme Inhibitors in Drug Discovery
Dewar, M. J. S., Zoebisch, E. G., Healy, E. F., Stewart, J. J. P., (1985) J. Am. Chem. Soc., 107, pp. 3902-3909
Portero-Ot n, M., Pamplona, R., Ruiz, M. C., Cabiscol, E., Prat, J., Bellmunt, M., (1999) J. Diabetes, 48, pp. 2215-2220
McNaught, K. S., Olanow, C. W., Halliwell, B., Isacson, O., Jenner, P., (2001) Nat. Rev. Neur., 2, pp. 589-594
Kisselev, A. F., Garcia-Calvo, M., Overkleeft, H. S., Peterson, E., Pennington, M. W., Ploegh, H. L., Thornberry, N. A., Goldberg, A. L., (2003) J. Biol. Chem., 278, pp. 35869-35877
Parkinson, G. N., Ghosh, R., Neidle, S., (2007) Biochemistry, 46, pp. 2390-2397
McMillin, D. R., Shelton, A. H., Bejune, S. A., Fanwick, P. E., Wall, R. K., (2005) Coord. Chem. Rev., 249, pp. 1451-1459
Kornguth, S. E., Kalinke, T., Robins, H. I., Cohen, J. D., Turski, P., (1989) Cancer Res., 49, pp. 6390-6395
Dick, L. R., Fleming, P. E., (2010) Drug Discov. Today, 15, pp. 243-249
Cationic porphyrins are reversible proteasome inhibitors
The aim of this study is to verify if water-soluble porphyrins can be used as proteasome inhibitors. We have found that cationic porphyrins inhibit proteasome peptidase activities much more effectively than the corresponding anionic derivatives. The relevance of electrostatics in driving porphyin-proteasome interactions has been confirmed by the observation that the inhibitory efficiency of the cationic macrocycles decreases with the number of positive substituents. We have also investigated various metalloporphyrins, which differ due to the different propension of the central metal ion toward axial coordination. Our experimental results indicate that the naked cationic porphyrins are the most active in reversibly inhibiting the three main protease activities of the proteasome in the micromolar range. A spectroscopic characterization of porphyrin-proteasome interactions by UV-vis spectra parallels the results of inhibition assays: the higher the inhibitory effect the stronger the spectroscopic variations are. To interpret the action of porphyrins at a molecular level, we have performed calculations evidencing that cationic porphyrins may hinder the access to the canonical proteolytic site on the proteasome β5 subunit. In particular, an inspection of the top-scoring docking modes shows that the tetracationic porphyrin blocks the catalytic pocket, close to the N termini of the β5 proteasome subunit, more efficiently than its anionic counterpart. Proteasome inhibition activity of porphyrins unites their known anticancer properties making them suitable as a scaffold for the design of novel multitargeted molecules. © 2012 American Chemical Society.
The aim of this study is to verify if water-soluble porphyrins can be used as proteasome inhibitors. We have found that cationic porphyrins inhibit proteasome peptidase activities much more effectively than the corresponding anionic derivatives. The relevance of electrostatics in driving porphyin-proteasome interactions has been confirmed by the observation that the inhibitory efficiency of the cationic macrocycles decreases with the number of positive substituents. We have also investigated various metalloporphyrins, which differ due to the different propension of the central metal ion toward axial coordination. Our experimental results indicate that the naked cationic porphyrins are the most active in reversibly inhibiting the three main protease activities of the proteasome in the micromolar range. A spectroscopic characterization of porphyrin-proteasome interactions by UV-vis spectra parallels the results of inhibition assays: the higher the inhibitory effect the stronger the spectroscopic variations are. To interpret the action of porphyrins at a molecular level, we have performed calculations evidencing that cationic porphyrins may hinder the access to the canonical proteolytic site on the proteasome β5 subunit. In particular, an inspection of the top-scoring docking modes shows that the tetracationic porphyrin blocks the catalytic pocket, close to the N termini of the β5 proteasome subunit, more efficiently than its anionic counterpart. Proteasome inhibition activity of porphyrins unites their known anticancer properties making them suitable as a scaffold for the design of novel multitargeted molecules. © 2012 American Chemical Society.
Cationic porphyrins are reversible proteasome inhibitors
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Cationic porphyrins are reversible proteasome inhibitors
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D’errico S, Falanga AP, Capasso D, Di Gaetano S, Marzano M, Terracciano M, Roviello GN, Piccialli G, Oliviero G, Borbone N
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Pharmaceutics (ISSN: 1999-4923linking), 2020 Jul 4; 12(7): 627-627.
Impact Factor: 4.421
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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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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)
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Impact Factor: 4.816
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Gaglione R, Pirone L, Farina B, Fusco S, Smaldone G, Aulitto M, Dell'Olmo E, Roscetto E, Del Gatto A, Fattorusso R, Notomista E, Zaccaro L, Arciello A, Pedone E, Contursi P
* Insights into the anticancer properties of the first antimicrobial peptide from Archaea (409 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 0304-4165linking), 2017 Jun 15; 1861(9): 2155-2164.
Impact Factor: 4.28
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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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Sandomenico A, Celentano V, D'Andrea LD, Palmieri G, Ruvo M
* Screening of beta-hairpin peptide-engrafted 1, 2, 3-triazoles to identify APEH enzyme inhibitors (412 views)
Rsc Adv (ISSN: 2046-2069), 2015; 5(13): 9965-9972.
Impact Factor: 3.289
View Export to BibTeX Export to EndNote
* Probing the DNA Reactivity and the Anticancer Properties of a Novel Tubercidin-Pt(II) Complex (136 views)
Pharmaceutics (ISSN: 1999-4923linking), 2020 Jul 4; 12(7): 627-627.
Impact Factor: 4.421
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
Gaglione R, Pirone L, Farina B, Fusco S, Smaldone G, Aulitto M, Dell'Olmo E, Roscetto E, Del Gatto A, Fattorusso R, Notomista E, Zaccaro L, Arciello A, Pedone E, Contursi P
* Insights into the anticancer properties of the first antimicrobial peptide from Archaea (409 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 0304-4165linking), 2017 Jun 15; 1861(9): 2155-2164.
Impact Factor: 4.28
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
Sandomenico A, Celentano V, D'Andrea LD, Palmieri G, Ruvo M
* Screening of beta-hairpin peptide-engrafted 1, 2, 3-triazoles to identify APEH enzyme inhibitors (412 views)
Rsc Adv (ISSN: 2046-2069), 2015; 5(13): 9965-9972.
Impact Factor: 3.289
View Export to BibTeX Export to EndNote
6 Records (6 excluding Abstracts).
Total impact factor: 25.474 (25.474 excluding Abstracts).
Total 5 year impact factor: 21.53 (21.53 excluding Abstracts).
Total impact factor: 25.474 (25.474 excluding Abstracts).
Total 5 year impact factor: 21.53 (21.53 excluding Abstracts).
447 views. Last view on Monday 29 May 2023, 11:42:52
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