Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (386 views)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2012 Feb 15; 22(4): 1560-1564.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.338, 5-year impact factor: 2.427
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84856650479&partnerID=40&md5=c2a1c1a6110bc59c42b21b52d5f6f2a5
Keywords: Ca Inhibitors, Carbonic Anhydrase Vii, Catalytic Activity, Cysteine Reactivity, Glutathionylation, Acetazolamide, Carbon Dioxide, Carbonate Dehydratase, Carbonate Dehydratase Ii, Esterase, Glutathione Transferase, Oxygen, Phosphatase, Scavenger, Sulfonamide, Unclassified Drug, Animal Cell, Article, Catalysis, Cell Protection, Controlled Study, Enzyme Activity, Enzyme Inhibition, Enzyme Mechanism, Enzyme Modification, Human, Human Cell, Hydration, Hydrolysis, In Vitro Study, In Vivo Study, Nonhuman, Oxidation, Oxidative Stress, Protein Analysis, Protein Expression, Protein Function, Protein Localization, Amino Acid Sequence, Carbonic Anhydrase Inhibitors, Cytosol, Enzyme Activation, Inhibitory Concentration 50, Molecular Sequence Data, Protein Isoforms, S-Nitrosoglutathione, Sequence Alignment, Spectrometry, Electrospray Ionization,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 0134 Napoli, Italy
Università Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
Universit Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
References:
Supuran, C.T., (2008) Nat. Rev. Drug Disc., 7, p. 16
Alterio, V., Di Fiore, A., D'ambrosio, K., Supuran, C.T., De Simone, G., X-ray crystallography of carbonic anhydrase inhibitors and its importance in drug design Drug Design of Zinc-Enzyme Inhibitors: Functional, Structural, and Disease Applications
Supuran, C.T., Winum, J.-Y., (2009) Wiley: Hoboken, New Jersey, pp. 73-138
Supuran, C.T., (2011) Future Med. Chem., 3, p. 1165
Supuran, C.T., Conroy, C.W., Maren, T.H., (1997) Proteins, 27, p. 272
Briganti, F., Mangani, S., Scozzafava, A., Vernaglione, G., Supuran, C.T., (1999) J. Biol. Inorg. Chem., 4, p. 528
Guerri, A., Briganti, F., Scozzafava, A., Supuran, C.T., Mangani, S., (2000) Biochemistry, 39, p. 12391
Pocker, Y., Dickerson, D.G., (1968) Biochemistry, 7, p. 1995
Pocker, Y., Meany, J.E., (1967) Biochemistry, 6, p. 239
Pocker, Y., Stone, J.T., (1967) Biochemistry, 6, p. 668
Verpoorte, J.A., Mehta, S., Edsall, J.T., (1967) J. Biol. Chem., 242, p. 4221
Kaiser, E.T., Lo, K.W., (1969) J. Am. Chem. Soc., 91, p. 4912
Höst, G., Martensson, L.G., Jonsson, B.H., (2006) Biochim. Biophys. Acta, 1764, p. 1601
Innocenti, A., Scozzafava, A., Parkkila, S., Puccetti, L., De Simone, G., Supuran, C.T., (2008) Bioorg. Med. Chem. Lett., 18, p. 2267
Hilvo, M., Innocenti, A., Monti, S.M., De Simone, G., Supuran, C.T., Parkkila, S., (2008) Curr. Pharm. Des., 14, p. 672
Guzel, O., Innocenti, A., Scozzafava, A., Salman, A., Supuran, C.T., (2009) Bioorg. Med. Chem. Lett., 19, p. 3170
Nishimori, I., Minakuchi, T., Onishi, S., Vullo, D., Cecchi, A., Scozzafava, A., Supuran, C.T., (2009) J. Enzyme Inhib. Med. Chem., 24, p. 70
Ruusuvuori, E., Li, H., Huttu, K., Palva, J.M., Smirnov, S., Rivera, C., Kaila, K., Voipio, J., (2004) J. Neurosci., 24, p. 2699
Bootorabi, F., Jänis, J., Smith, E., Waheed, A., Kukkurainen, S., Hytönen, V., Valjakka, J., Parkkila, S., (2010) Biochimie, 92, p. 1072
Di Fiore, A., Truppo, E., Supuran, C.T., Alterio, V., Dathan, N., Bootorabi, F., Parkkila, S., De Simone, G., (2010) Bioorg. Med. Chem. Lett., 20, p. 5023
Thiry, A., Dogné, J.M., Supuran, C.T., Masereel, B., (2007) Curr. Top. Med. Chem., 7, p. 855
Asiedu, M., Ossipov, M.H., Kaila, K., Price, T.J., (2010) Pain, 148, p. 302
Di Fiore, A., Monti, S.M., Hilvo, M., Parkkila, S., Romano, V., Scaloni, A., Pedone, C., De Simone, G., (2008) Proteins, 74, p. 164
Papa, S., Monti, S.M., Vitale, R.M., Bubici, C., Jayawardena, S., Alvarez, K., De Smaele, E., Franzoso, G., (2007) J. Biol. Chem., 282, p. 19029
Tornatore, L., Marasco, D., Dathan, N., Vitale, R.M., Benedetti, E., Papa, S., Franzoso, G., Monti, S.M., (2008) J. Mol. Biol., 378, p. 97
Kadokura, H., Katzen, F., Beckwith, J., (2003) Annu. Rev. Biochem., 72, p. 111
Filomeni, G., Rotilio, G., Ciriolo, M.R., (2005) Cell Death Differ., 12, p. 1555
Chai, Y.C., Jung, C.H., Lii, C.K., Ashraf, S.S., Hendrich, S., Wolf, B., Sies, H., Thomas, J.A., (1991) Arch. Biochem. Biophys., 284, p. 270
Lii, C.K., Wang, S.T., Chen, H.W., (1996) Toxicol. Lett., 84, p. 97
Rokutan, K., Thomas, J.A., Sies, H., (1989) Eur. J. Biochem., 179, p. 233
Mallis, R.J., Poland, B.W., Chatterjee, T.K., Fisher, R.A., Darmawan, S., Honzatko, R.B., Thomas, J.A., (2000) FEBS Lett., 482, p. 237
Zimmerman, U.J., Wang, P., Zhang, X., Bogdanovich, S., Forster, R., (2004) IUBMB Life, 56, p. 343
Räisänen, S.R., Lehenkari, P., Tasanen, M., Rahkila, P., Härkönen, P.L., Väänänen, H.K., (1999) FASEB J., 13, p. 513
Roy, P., Reavey, E., Rayne, M., Roy, S., Abed El Baky, M., Ishii, Y., Bartholomew, C., (2010) FEBS J., 277, p. 441
Khalifah, R.G., (1971) J. Biol. Chem., 246, p. 2561
Pullan, L.M., Noltmann, E., (1985) A. Biochemistry, 24, p. 635
Vullo, D., Voipio, J., Innocenti, A., Rivera, C., Ranki, H., Scozzafava, A., Kaila, K., Supuran, C.T., (2005) Bioorg. Med. Chem. Lett., 15, p. 971
Marí, M., Morales, A., Colell, A., García-Ruiz, C., Fernández-Checa, J.C., (2009) Antioxid. Redox Signal., 11, p. 2685
Marí, M., Colell, A., Morales, A., Von Montfort, C., Garcia-Ruiz, C., Fernández-Checa, J.C., (2010) Antioxid. Redox Signal., 12, p. 1295
Supuran, C. T., (2008) Nat. Rev. Drug Disc., 7, p. 16
Supuran, C. T., Winum, J. -Y., (2009) Wiley: Hoboken, New Jersey, pp. 73-138
Supuran, C. T., Conroy, C. W., Maren, T. H., (1997) Proteins, 27, p. 272
Verpoorte, J. A., Mehta, S., Edsall, J. T., (1967) J. Biol. Chem., 242, p. 4221
Kaiser, E. T., Lo, K. W., (1969) J. Am. Chem. Soc., 91, p. 4912
H st, G., Martensson, L. G., Jonsson, B. H., (2006) Biochim. Biophys. Acta, 1764, p. 1601
Bootorabi, F., J nis, J., Smith, E., Waheed, A., Kukkurainen, S., Hyt nen, V., Valjakka, J., Parkkila, S., (2010) Biochimie, 92, p. 1072
Thiry, A., Dogn, J. M., Supuran, C. T., Masereel, B., (2007) Curr. Top. Med. Chem., 7, p. 855
Chai, Y. C., Jung, C. H., Lii, C. K., Ashraf, S. S., Hendrich, S., Wolf, B., Sies, H., Thomas, J. A., (1991) Arch. Biochem. Biophys., 284, p. 270
Lii, C. K., Wang, S. T., Chen, H. W., (1996) Toxicol. Lett., 84, p. 97
Mallis, R. J., Poland, B. W., Chatterjee, T. K., Fisher, R. A., Darmawan, S., Honzatko, R. B., Thomas, J. A., (2000) FEBS Lett., 482, p. 237
Zimmerman, U. J., Wang, P., Zhang, X., Bogdanovich, S., Forster, R., (2004) IUBMB Life, 56, p. 343
R is nen, S. R., Lehenkari, P., Tasanen, M., Rahkila, P., H rk nen, P. L., V n nen, H. K., (1999) FASEB J., 13, p. 513
Khalifah, R. G., (1971) J. Biol. Chem., 246, p. 2561
Pullan, L. M., Noltmann, E., (1985) A. Biochemistry, 24, p. 635
Mar, M., Morales, A., Colell, A., Garc a-Ruiz, C., Fern ndez-Checa, J. C., (2009) Antioxid. Redox Signal., 11, p. 2685
Mar, M., Colell, A., Morales, A., Von Montfort, C., Garcia-Ruiz, C., Fern ndez-Checa, J. C., (2010) Antioxid. Redox Signal., 12, p. 1295
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2012 Feb 15; 22(4): 1560-1564.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.338, 5-year impact factor: 2.427
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84856650479&partnerID=40&md5=c2a1c1a6110bc59c42b21b52d5f6f2a5
Keywords: Ca Inhibitors, Carbonic Anhydrase Vii, Catalytic Activity, Cysteine Reactivity, Glutathionylation, Acetazolamide, Carbon Dioxide, Carbonate Dehydratase, Carbonate Dehydratase Ii, Esterase, Glutathione Transferase, Oxygen, Phosphatase, Scavenger, Sulfonamide, Unclassified Drug, Animal Cell, Article, Catalysis, Cell Protection, Controlled Study, Enzyme Activity, Enzyme Inhibition, Enzyme Mechanism, Enzyme Modification, Human, Human Cell, Hydration, Hydrolysis, In Vitro Study, In Vivo Study, Nonhuman, Oxidation, Oxidative Stress, Protein Analysis, Protein Expression, Protein Function, Protein Localization, Amino Acid Sequence, Carbonic Anhydrase Inhibitors, Cytosol, Enzyme Activation, Inhibitory Concentration 50, Molecular Sequence Data, Protein Isoforms, S-Nitrosoglutathione, Sequence Alignment, Spectrometry, Electrospray Ionization,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 0134 Napoli, Italy
Università Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
Universit Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
References:
Supuran, C.T., (2008) Nat. Rev. Drug Disc., 7, p. 16
Alterio, V., Di Fiore, A., D'ambrosio, K., Supuran, C.T., De Simone, G., X-ray crystallography of carbonic anhydrase inhibitors and its importance in drug design Drug Design of Zinc-Enzyme Inhibitors: Functional, Structural, and Disease Applications
Supuran, C.T., Winum, J.-Y., (2009) Wiley: Hoboken, New Jersey, pp. 73-138
Supuran, C.T., (2011) Future Med. Chem., 3, p. 1165
Supuran, C.T., Conroy, C.W., Maren, T.H., (1997) Proteins, 27, p. 272
Briganti, F., Mangani, S., Scozzafava, A., Vernaglione, G., Supuran, C.T., (1999) J. Biol. Inorg. Chem., 4, p. 528
Guerri, A., Briganti, F., Scozzafava, A., Supuran, C.T., Mangani, S., (2000) Biochemistry, 39, p. 12391
Pocker, Y., Dickerson, D.G., (1968) Biochemistry, 7, p. 1995
Pocker, Y., Meany, J.E., (1967) Biochemistry, 6, p. 239
Pocker, Y., Stone, J.T., (1967) Biochemistry, 6, p. 668
Verpoorte, J.A., Mehta, S., Edsall, J.T., (1967) J. Biol. Chem., 242, p. 4221
Kaiser, E.T., Lo, K.W., (1969) J. Am. Chem. Soc., 91, p. 4912
Höst, G., Martensson, L.G., Jonsson, B.H., (2006) Biochim. Biophys. Acta, 1764, p. 1601
Innocenti, A., Scozzafava, A., Parkkila, S., Puccetti, L., De Simone, G., Supuran, C.T., (2008) Bioorg. Med. Chem. Lett., 18, p. 2267
Hilvo, M., Innocenti, A., Monti, S.M., De Simone, G., Supuran, C.T., Parkkila, S., (2008) Curr. Pharm. Des., 14, p. 672
Guzel, O., Innocenti, A., Scozzafava, A., Salman, A., Supuran, C.T., (2009) Bioorg. Med. Chem. Lett., 19, p. 3170
Nishimori, I., Minakuchi, T., Onishi, S., Vullo, D., Cecchi, A., Scozzafava, A., Supuran, C.T., (2009) J. Enzyme Inhib. Med. Chem., 24, p. 70
Ruusuvuori, E., Li, H., Huttu, K., Palva, J.M., Smirnov, S., Rivera, C., Kaila, K., Voipio, J., (2004) J. Neurosci., 24, p. 2699
Bootorabi, F., Jänis, J., Smith, E., Waheed, A., Kukkurainen, S., Hytönen, V., Valjakka, J., Parkkila, S., (2010) Biochimie, 92, p. 1072
Di Fiore, A., Truppo, E., Supuran, C.T., Alterio, V., Dathan, N., Bootorabi, F., Parkkila, S., De Simone, G., (2010) Bioorg. Med. Chem. Lett., 20, p. 5023
Thiry, A., Dogné, J.M., Supuran, C.T., Masereel, B., (2007) Curr. Top. Med. Chem., 7, p. 855
Asiedu, M., Ossipov, M.H., Kaila, K., Price, T.J., (2010) Pain, 148, p. 302
Di Fiore, A., Monti, S.M., Hilvo, M., Parkkila, S., Romano, V., Scaloni, A., Pedone, C., De Simone, G., (2008) Proteins, 74, p. 164
Papa, S., Monti, S.M., Vitale, R.M., Bubici, C., Jayawardena, S., Alvarez, K., De Smaele, E., Franzoso, G., (2007) J. Biol. Chem., 282, p. 19029
Tornatore, L., Marasco, D., Dathan, N., Vitale, R.M., Benedetti, E., Papa, S., Franzoso, G., Monti, S.M., (2008) J. Mol. Biol., 378, p. 97
Kadokura, H., Katzen, F., Beckwith, J., (2003) Annu. Rev. Biochem., 72, p. 111
Filomeni, G., Rotilio, G., Ciriolo, M.R., (2005) Cell Death Differ., 12, p. 1555
Chai, Y.C., Jung, C.H., Lii, C.K., Ashraf, S.S., Hendrich, S., Wolf, B., Sies, H., Thomas, J.A., (1991) Arch. Biochem. Biophys., 284, p. 270
Lii, C.K., Wang, S.T., Chen, H.W., (1996) Toxicol. Lett., 84, p. 97
Rokutan, K., Thomas, J.A., Sies, H., (1989) Eur. J. Biochem., 179, p. 233
Mallis, R.J., Poland, B.W., Chatterjee, T.K., Fisher, R.A., Darmawan, S., Honzatko, R.B., Thomas, J.A., (2000) FEBS Lett., 482, p. 237
Zimmerman, U.J., Wang, P., Zhang, X., Bogdanovich, S., Forster, R., (2004) IUBMB Life, 56, p. 343
Räisänen, S.R., Lehenkari, P., Tasanen, M., Rahkila, P., Härkönen, P.L., Väänänen, H.K., (1999) FASEB J., 13, p. 513
Roy, P., Reavey, E., Rayne, M., Roy, S., Abed El Baky, M., Ishii, Y., Bartholomew, C., (2010) FEBS J., 277, p. 441
Khalifah, R.G., (1971) J. Biol. Chem., 246, p. 2561
Pullan, L.M., Noltmann, E., (1985) A. Biochemistry, 24, p. 635
Vullo, D., Voipio, J., Innocenti, A., Rivera, C., Ranki, H., Scozzafava, A., Kaila, K., Supuran, C.T., (2005) Bioorg. Med. Chem. Lett., 15, p. 971
Marí, M., Morales, A., Colell, A., García-Ruiz, C., Fernández-Checa, J.C., (2009) Antioxid. Redox Signal., 11, p. 2685
Marí, M., Colell, A., Morales, A., Von Montfort, C., Garcia-Ruiz, C., Fernández-Checa, J.C., (2010) Antioxid. Redox Signal., 12, p. 1295
Supuran, C. T., (2008) Nat. Rev. Drug Disc., 7, p. 16
Supuran, C. T., Winum, J. -Y., (2009) Wiley: Hoboken, New Jersey, pp. 73-138
Supuran, C. T., Conroy, C. W., Maren, T. H., (1997) Proteins, 27, p. 272
Verpoorte, J. A., Mehta, S., Edsall, J. T., (1967) J. Biol. Chem., 242, p. 4221
Kaiser, E. T., Lo, K. W., (1969) J. Am. Chem. Soc., 91, p. 4912
H st, G., Martensson, L. G., Jonsson, B. H., (2006) Biochim. Biophys. Acta, 1764, p. 1601
Bootorabi, F., J nis, J., Smith, E., Waheed, A., Kukkurainen, S., Hyt nen, V., Valjakka, J., Parkkila, S., (2010) Biochimie, 92, p. 1072
Thiry, A., Dogn, J. M., Supuran, C. T., Masereel, B., (2007) Curr. Top. Med. Chem., 7, p. 855
Chai, Y. C., Jung, C. H., Lii, C. K., Ashraf, S. S., Hendrich, S., Wolf, B., Sies, H., Thomas, J. A., (1991) Arch. Biochem. Biophys., 284, p. 270
Lii, C. K., Wang, S. T., Chen, H. W., (1996) Toxicol. Lett., 84, p. 97
Mallis, R. J., Poland, B. W., Chatterjee, T. K., Fisher, R. A., Darmawan, S., Honzatko, R. B., Thomas, J. A., (2000) FEBS Lett., 482, p. 237
Zimmerman, U. J., Wang, P., Zhang, X., Bogdanovich, S., Forster, R., (2004) IUBMB Life, 56, p. 343
R is nen, S. R., Lehenkari, P., Tasanen, M., Rahkila, P., H rk nen, P. L., V n nen, H. K., (1999) FASEB J., 13, p. 513
Khalifah, R. G., (1971) J. Biol. Chem., 246, p. 2561
Pullan, L. M., Noltmann, E., (1985) A. Biochemistry, 24, p. 635
Mar, M., Morales, A., Colell, A., Garc a-Ruiz, C., Fern ndez-Checa, J. C., (2009) Antioxid. Redox Signal., 11, p. 2685
Mar, M., Colell, A., Morales, A., Von Montfort, C., Garcia-Ruiz, C., Fern ndez-Checa, J. C., (2010) Antioxid. Redox Signal., 12, p. 1295
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic isoform. Cys183 and Cys217 were found to be the residues involved in reaction with glutathione for hCA VII. The two reactive cysteines were then mutated and the corresponding variant (C183S/C217S) expressed. The native enzyme, the variant and the S-glutathionylated adduct (sgCA VII) as well as hCA III were fully characterized for their CO 2 hydration, esterase/ phosphatase activities, and inhibition with sulfonamides. Our findings suggest that hCA VII could use the in vivo S-glutathionylation to function as an oxygen radical scavenger for protecting cells from oxidative damage, as the activity and affinity for inhibitors of the modified enzyme are similar to those of the wild type. © 2012 Elsevier Ltd. All rights reserved.
Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic isoform. Cys183 and Cys217 were found to be the residues involved in reaction with glutathione for hCA VII. The two reactive cysteines were then mutated and the corresponding variant (C183S/C217S) expressed. The native enzyme, the variant and the S-glutathionylated adduct (sgCA VII) as well as hCA III were fully characterized for their CO 2 hydration, esterase/ phosphatase activities, and inhibition with sulfonamides. Our findings suggest that hCA VII could use the in vivo S-glutathionylation to function as an oxygen radical scavenger for protecting cells from oxidative damage, as the activity and affinity for inhibitors of the modified enzyme are similar to those of the wild type. © 2012 Elsevier Ltd. All rights reserved.
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
Other filter: ([btitle,keywords] "Ca Inhibitors" OR [b ...
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* An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (447 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
Impact Factor: 3.559
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Monti SM, Supuran CT, De Simone G, Di Fiore A
* Carbonic Anhydrase VII (215 views)
Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 151-168.
Impact Factor: 0
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Del Giudice R, Monti DM, Truppo E, Arciello A, Supuran CT, De Simone G, Monti SM
* Human Carbonic Anhydrase Vii Protects Cells From Oxidative Damage (367 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1431-1673, 1437-4315), 2013; 394(10): 1343-1348.
Impact Factor: 2.689
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Di Fiore A, Truppo E, Supuran CT, Alterio V, Dathan N, Bootorabi F, Parkkila S, Monti SM, De Simone G
* Crystal structure of the C183S/C217S mutant of human CA VII in complex with acetazolamide (460 views)
Bioorg Med Chem Lett (ISSN: 0960-894x), 2010 Sep 1; 20(17): 5023-5026.
Impact Factor: 2.661
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Hilvo M, De Simone G, Supuran CT, Parkkila S
* Advances in the Inhibitory and Structural Investigations on Carbonic Anhydrase Isozymes XIII and XV (290 views)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 273-283.
Impact Factor: 1.156
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Hilvo M, Innocenti A, Monti SM, De Simone G, Supuran CT, Parkkila S
* Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV (497 views)
Curr Pharm Des Current Pharmaceutical Design (ISSN: 1381-6128, 1873-4286), 2008; 14(7): 672-678.
Impact Factor: 4.399
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Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (442 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
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Bonomo RP, Cennamo G, Purrello R, Santoro AM, Zappala R
* Comparison Of Three Fungal Laccases From Rigidoporus Lignosus And Pleurotus Ostreatus: Correlation Between Conformation Changes And Catalytic Activity (321 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2001 Jan 1; 83(1): 67-75.
Impact Factor: 1.729
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* Synthesis, Characterization, and Study of Catalytic Activity of Chiral Cu(II) and Ni(II) Salen Complexes in the α-Amino Acid C-α Alkylation Reaction (7 views)
Molecules, 2023 Jan 25; 28: 1180-1196.
Impact Factor: 4.927
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Akgül Ö, Lucarini E, Mannelli LDC, Ghelardini C, D'Xambrosio K, Buonanno M, Monti SM, De Simone G, Angeli A, Supuran CT, Carta F
* Sultam based Carbonic Anhydrase VII inhibitors for the management of neuropathic pain (17 views)
Eur J Med Chem (ISSN: 0223-5234linking), 2022 Jan 5; 227: 113956-113956.
Impact Factor: 7.088
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Bocedi A, Gambardella G, Cattani G, Bartolucci S, Limauro D, Pedone E, Iavarone F, Castagnola M, Ricci G
* Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins (62 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2020 Jun 2; 10(1): 8943-8943.
Impact Factor: 3.998
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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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De Simone G, Di Fiore A, Truppo E, Langella E, Vullo D, Supuran CT, Monti SM
* Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach (223 views)
J Enzym Inhib Med Ch (ISSN: 1475-6366linking, 1475-6374electronic), 2019 Dec; 34(1): 1506-1510.
Impact Factor: 4.027
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Caporale A, Monti A, Selis F, Sandomenico A, Tonon G, Ruvo M, Doti N
* A comparative analysis of catalytic activity and stability of microbial transglutaminase in controlled denaturing conditions (164 views)
J Biotechnol (ISSN: 0168-1656linking), 2019 Aug 20; 302: 48-57.
Impact Factor: 3.163
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Buemi MR, Di Fiore A, De Luca L, Angeli A, Mancuso F, Ferro S, Monti SM, Buonanno M, Russo E, De Sarro G, De Simone G, Supuran CT, Gitto R
* Exploring structural properties of potent human carbonic anhydrase inhibitors bearing a 4-(cycloalkylamino-1-carbonyl)benzenesulfonamide moiety (327 views)
Eur J Med Chem (ISSN: 1768-3254electronic, 0223-5234linking), 2019 Feb 1; 163: 443-452.
Impact Factor: 4.833
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Zambrano G, Ruggiero E, Malafronte A, Chino M, Maglio O, Pavone V, Nastri F, Lombardi A
* Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials (264 views)
Int J Mol Sc (ISSN: 1422-0067electronic, 1422-0067linking, 1661-6596), 2018 Sep 24; 19(10): N/D-N/D.
Impact Factor: 3.687
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Buonanno M, Di Fiore A, Langella E, D’ambrosio K, Supuran CT, Monti SM, De Simone G
* The Crystal Structure of a hCA VII Variant Provides Insights into the Molecular Determinants Responsible for Its Catalytic Behavior (304 views)
Int J Mol Sc (ISSN: 1661-6596, 1422-0067, 1422-0067electronic), 2018 May; 19(6): 19-24.
Impact Factor: 3.687
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Monti DM, De Simone G, Langella E, Supuran CT, Di Fiore A, Monti SM
* Insights into the role of reactive sulfhydryl groups of Carbonic Anhydrase III and VII during oxidative damage (364 views)
J Enzym Inhib Med Ch (ISSN: 1475-6366, 1475-6374electronic, 1475-6366linking), 2017 Dec; 32(1): 5-12.
Impact Factor: 3.638
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Vitale R, Lista L, Cerrone C, Caserta G, Chino M, Maglio O, Nastri F, Pavone V, Lombardi A
* An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (447 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
Impact Factor: 3.559
View Export to BibTeX Export to EndNote
Monti SM, Supuran CT, De Simone G, Di Fiore A
* Carbonic Anhydrase VII (215 views)
Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 151-168.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Del Giudice R, Monti DM, Truppo E, Arciello A, Supuran CT, De Simone G, Monti SM
* Human Carbonic Anhydrase Vii Protects Cells From Oxidative Damage (367 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1431-1673, 1437-4315), 2013; 394(10): 1343-1348.
Impact Factor: 2.689
View Export to BibTeX Export to EndNote
Di Fiore A, Truppo E, Supuran CT, Alterio V, Dathan N, Bootorabi F, Parkkila S, Monti SM, De Simone G
* Crystal structure of the C183S/C217S mutant of human CA VII in complex with acetazolamide (460 views)
Bioorg Med Chem Lett (ISSN: 0960-894x), 2010 Sep 1; 20(17): 5023-5026.
Impact Factor: 2.661
View Export to BibTeX Export to EndNote
Hilvo M, De Simone G, Supuran CT, Parkkila S
* Advances in the Inhibitory and Structural Investigations on Carbonic Anhydrase Isozymes XIII and XV (290 views)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 273-283.
Impact Factor: 1.156
View Export to BibTeX Export to EndNote
Hilvo M, Innocenti A, Monti SM, De Simone G, Supuran CT, Parkkila S
* Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV (497 views)
Curr Pharm Des Current Pharmaceutical Design (ISSN: 1381-6128, 1873-4286), 2008; 14(7): 672-678.
Impact Factor: 4.399
View Export to BibTeX Export to EndNote
Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (442 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Bonomo RP, Cennamo G, Purrello R, Santoro AM, Zappala R
* Comparison Of Three Fungal Laccases From Rigidoporus Lignosus And Pleurotus Ostreatus: Correlation Between Conformation Changes And Catalytic Activity (321 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2001 Jan 1; 83(1): 67-75.
Impact Factor: 1.729
View Export to BibTeX Export to EndNote
18 Records (18 excluding Abstracts).
Total impact factor: 61.095 (61.095 excluding Abstracts).
Total 5 year impact factor: 50.409 (50.409 excluding Abstracts).
Total impact factor: 61.095 (61.095 excluding Abstracts).
Total 5 year impact factor: 50.409 (50.409 excluding Abstracts).
386 views. Last view on Tuesday 04 April 2023, 13:44:10
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