Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis (341 views visite)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2011 Sep; 12(9): 6312-6319.
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Paper type Tipo di articolo: Journal Article,
Impact factor: 2.598, 5-year impact factor Impact factor a 5 anni: 2.617
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-80053206933&partnerID=40&md5=9ec9c40b3434ed0ebff0bd50fadccefe
Keywords Parole chiave: Crystal Quality, Glutathione Synthetase, Psychrophile, Without-Oil Microbatch, X-Ray Crystallography, Glutathione Synthase, Article, Concentration (parameters), Controlled Study, Crystal Structure, Enzyme Purification, Escherichia Coli, Evaporation, Process Optimization, Protein Expression, Pseudoalteromonas, Pseudoalteromonas Haloplanktis, Psychrophilic Bacterium, Quality Control, Structure Analysis, Validation Process, X Ray Diffraction,
Affiliations Affiliazioni:
*** IBB - CNR ***
Dipartimento di Chimica Paolo Corradini, Università di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cinthia, Naples I-80126, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, Naples I-80134, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II, Via Pansini 5, Naples I-80131, Italy
Dipartimento di Studi delle Istituzioni e dei Sistemi Territoriali, Università di Napoli Parthenope, Via Medina 40, Naples I-80133, Italy
References Riferimenti:
Dalle-Donne, I., Rossi, R., Giustarini, D., Colombo, R., Milzani, A., S-glutathionylation in protein redox regulation (2007) Free Radic. Biol. Med, 43, pp. 883-89
Circu, M.L., Aw, T.Y., Glutathione and apoptosis (2008) Free Radic. Res, 42, pp. 689-706
Pallardo, F.V., Markovic, J., Garcia, J.L., Vina, J., Role of nuclear glutathione as a key regulator of cell proliferation (2009) Mol. Asp. Med, 30, pp. 77-85
Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., Katsube, Y., Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution (1993) J. Mol. Biol, 229, pp. 1083-1100
Mooz, E.D., Meister, A., Tripeptide (glutathione) synthetase: Purification, properties and mechanism of action (1967) Biochemistry, 6, pp. 1722-1734
Gali, R.R., Board, P.G., Sequencing and expression of a cDNA for human glutathione synthetase (1995) Biochem. J, 310, pp. 353-358
Ota, T., Suzuki, Y., Nishikawa, T., Otsuki, T., Sugiyama, T., Irie, R., Wakamatsu, A., Nagai, K., Complete sequencing and characterization of 21,243 full-length human cDNAs (2004) Nat. Genet, 36, pp. 40-45
Huang, C.S., He, W., Meister, A., Anderson, M.E., Amino acid sequence of rat kidney glutathione synthetase (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 1232-1236
Gushima, H., Yasuda, S., Soeda, E., Yokota, M., Kimura, A., Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II (1984) Nucleic Acids Res, 12, pp. 9299-9307
Polekhina, G., Board, P.G., Gali, R.R., Rossjohn, J., Parker, M.W., Molecular basis of glutathione synthetase deficiency and a rare gene permutation event (1999) EMBO J, 18, pp. 3204-3213
Castellano, I., di Maro, A., Ruocco, M.R., Chambery, A., Parente, A., di Martino, M.T., Parlato, G., de Vendittis, E., Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: Biochemical characterization and identification of a highly reactive cysteine residue (2006) Biochimie, 88, pp. 1377-1389
Castellano, I., Ruocco, M.R., Cecere, F., di Maro, A., Chambery, A., Michniewicz, A., Parlato, G., de Vendittis, E., Glutathionylation of the iron superoxide dismutase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis. Biochim. Biophys (2008) Acta Protein Proteonomics, 1784, pp. 816-826
Merlino, A., Russo Krauss, I., Castellano, I., de Vendittis, E., Rossi, B., Conte, M., Vergara, A., Sica, F., Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis (2010) J. Struct. Biol, 172, pp. 343-352
Matsuda, K., Mizuguchi, K., Nishioka, T., Kato, H., Go, N., Oda, J., Crystal structure of glutathione synthetase at optimal pH: Domain architecture and structural similarity with other proteins (1996) Protein Eng, 9, pp. 1083-1092
Hara, T., Kato, H., Katsube, Y., Oda, J.A., pseudo-Michaelis quaternary complex in the reverse reaction of a ligase: Structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 Å resolution (1996) Biochemistry, 35, pp. 11967-11974
Chayen, N.E., Shaw Stewart, P.D., Maeder, D.L., Blow, D.M., An automated system for micro-batch protein crystallization and screening (1990) J. Appl. Cryst, 23, pp. 297-302
Chayen, N.E., Recent advances in methodology for the crystallization of biological macromolecules (1999) J. Cryst. Growth, 199, pp. 649-655
Martins, P.M., Pessoa, J., Sarkany, Z., Rocha, F., Damas, A.M., Rationalizing protein crystallization Screenings through water equilibration theory and protein solubility data (2008) Cryst. Growth Des, 8, pp. 4233-4243
Rayment, I., Small-scale batch crystallization of proteins revisited: An underutilized way to grow large protein crystals (2002) Structure, 10, pp. 147-151
Matthews, B.W., Solvent content of protein crystals (1968) J. Mol. Biol, 33, pp. 491-497
Medigue, C., Krin, E., Pascal, G., Barbe, V., Bernsel, A., Bertin, P.N., Cheung, F., Duilio, A., Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125 (2005) Genome Res, 15, pp. 1325-1335
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Evans, P., Scaling and assessment of data quality (2006) Acta Cryst. D, 62, pp. 72-82
Weiss, M.S., Global indicators of X-ray data quality (2001) J. Appl. Crystallogr, 34, pp. 130-135
Storoni, L.C., McCoy, A.J., Read, R.J., Likelihood-enhanced fast rotation functions (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 432-438
Circu, M. L., Aw, T. Y., Glutathione and apoptosis (2008) Free Radic. Res, 42, pp. 689-706
Pallardo, F. V., Markovic, J., Garcia, J. L., Vina, J., Role of nuclear glutathione as a key regulator of cell proliferation (2009) Mol. Asp. Med, 30, pp. 77-85
Mooz, E. D., Meister, A., Tripeptide (glutathione) synthetase: Purification, properties and mechanism of action (1967) Biochemistry, 6, pp. 1722-1734
Gali, R. R., Board, P. G., Sequencing and expression of a cDNA for human glutathione synthetase (1995) Biochem. J, 310, pp. 353-358
Huang, C. S., He, W., Meister, A., Anderson, M. E., Amino acid sequence of rat kidney glutathione synthetase (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 1232-1236
Chayen, N. E., Shaw Stewart, P. D., Maeder, D. L., Blow, D. M., An automated system for micro-batch protein crystallization and screening (1990) J. Appl. Cryst, 23, pp. 297-302
Chayen, N. E., Recent advances in methodology for the crystallization of biological macromolecules (1999) J. Cryst. Growth, 199, pp. 649-655
Martins, P. M., Pessoa, J., Sarkany, Z., Rocha, F., Damas, A. M., Rationalizing protein crystallization Screenings through water equilibration theory and protein solubility data (2008) Cryst. Growth Des, 8, pp. 4233-4243
Matthews, B. W., Solvent content of protein crystals (1968) J. Mol. Biol, 33, pp. 491-497
Weiss, M. S., Global indicators of X-ray data quality (2001) J. Appl. Crystallogr, 34, pp. 130-135
Storoni, L. C., McCoy, A. J., Read, R. J., Likelihood-enhanced fast rotation functions (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 432-438
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2011 Sep; 12(9): 6312-6319.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.598, 5-year impact factor Impact factor a 5 anni: 2.617
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-80053206933&partnerID=40&md5=9ec9c40b3434ed0ebff0bd50fadccefe
Keywords Parole chiave: Crystal Quality, Glutathione Synthetase, Psychrophile, Without-Oil Microbatch, X-Ray Crystallography, Glutathione Synthase, Article, Concentration (parameters), Controlled Study, Crystal Structure, Enzyme Purification, Escherichia Coli, Evaporation, Process Optimization, Protein Expression, Pseudoalteromonas, Pseudoalteromonas Haloplanktis, Psychrophilic Bacterium, Quality Control, Structure Analysis, Validation Process, X Ray Diffraction,
Affiliations Affiliazioni:
*** IBB - CNR ***
Dipartimento di Chimica Paolo Corradini, Università di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cinthia, Naples I-80126, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, Naples I-80134, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II, Via Pansini 5, Naples I-80131, Italy
Dipartimento di Studi delle Istituzioni e dei Sistemi Territoriali, Università di Napoli Parthenope, Via Medina 40, Naples I-80133, Italy
References Riferimenti:
Dalle-Donne, I., Rossi, R., Giustarini, D., Colombo, R., Milzani, A., S-glutathionylation in protein redox regulation (2007) Free Radic. Biol. Med, 43, pp. 883-89
Circu, M.L., Aw, T.Y., Glutathione and apoptosis (2008) Free Radic. Res, 42, pp. 689-706
Pallardo, F.V., Markovic, J., Garcia, J.L., Vina, J., Role of nuclear glutathione as a key regulator of cell proliferation (2009) Mol. Asp. Med, 30, pp. 77-85
Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., Katsube, Y., Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution (1993) J. Mol. Biol, 229, pp. 1083-1100
Mooz, E.D., Meister, A., Tripeptide (glutathione) synthetase: Purification, properties and mechanism of action (1967) Biochemistry, 6, pp. 1722-1734
Gali, R.R., Board, P.G., Sequencing and expression of a cDNA for human glutathione synthetase (1995) Biochem. J, 310, pp. 353-358
Ota, T., Suzuki, Y., Nishikawa, T., Otsuki, T., Sugiyama, T., Irie, R., Wakamatsu, A., Nagai, K., Complete sequencing and characterization of 21,243 full-length human cDNAs (2004) Nat. Genet, 36, pp. 40-45
Huang, C.S., He, W., Meister, A., Anderson, M.E., Amino acid sequence of rat kidney glutathione synthetase (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 1232-1236
Gushima, H., Yasuda, S., Soeda, E., Yokota, M., Kimura, A., Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II (1984) Nucleic Acids Res, 12, pp. 9299-9307
Polekhina, G., Board, P.G., Gali, R.R., Rossjohn, J., Parker, M.W., Molecular basis of glutathione synthetase deficiency and a rare gene permutation event (1999) EMBO J, 18, pp. 3204-3213
Castellano, I., di Maro, A., Ruocco, M.R., Chambery, A., Parente, A., di Martino, M.T., Parlato, G., de Vendittis, E., Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: Biochemical characterization and identification of a highly reactive cysteine residue (2006) Biochimie, 88, pp. 1377-1389
Castellano, I., Ruocco, M.R., Cecere, F., di Maro, A., Chambery, A., Michniewicz, A., Parlato, G., de Vendittis, E., Glutathionylation of the iron superoxide dismutase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis. Biochim. Biophys (2008) Acta Protein Proteonomics, 1784, pp. 816-826
Merlino, A., Russo Krauss, I., Castellano, I., de Vendittis, E., Rossi, B., Conte, M., Vergara, A., Sica, F., Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis (2010) J. Struct. Biol, 172, pp. 343-352
Matsuda, K., Mizuguchi, K., Nishioka, T., Kato, H., Go, N., Oda, J., Crystal structure of glutathione synthetase at optimal pH: Domain architecture and structural similarity with other proteins (1996) Protein Eng, 9, pp. 1083-1092
Hara, T., Kato, H., Katsube, Y., Oda, J.A., pseudo-Michaelis quaternary complex in the reverse reaction of a ligase: Structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 Å resolution (1996) Biochemistry, 35, pp. 11967-11974
Chayen, N.E., Shaw Stewart, P.D., Maeder, D.L., Blow, D.M., An automated system for micro-batch protein crystallization and screening (1990) J. Appl. Cryst, 23, pp. 297-302
Chayen, N.E., Recent advances in methodology for the crystallization of biological macromolecules (1999) J. Cryst. Growth, 199, pp. 649-655
Martins, P.M., Pessoa, J., Sarkany, Z., Rocha, F., Damas, A.M., Rationalizing protein crystallization Screenings through water equilibration theory and protein solubility data (2008) Cryst. Growth Des, 8, pp. 4233-4243
Rayment, I., Small-scale batch crystallization of proteins revisited: An underutilized way to grow large protein crystals (2002) Structure, 10, pp. 147-151
Matthews, B.W., Solvent content of protein crystals (1968) J. Mol. Biol, 33, pp. 491-497
Medigue, C., Krin, E., Pascal, G., Barbe, V., Bernsel, A., Bertin, P.N., Cheung, F., Duilio, A., Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125 (2005) Genome Res, 15, pp. 1325-1335
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Evans, P., Scaling and assessment of data quality (2006) Acta Cryst. D, 62, pp. 72-82
Weiss, M.S., Global indicators of X-ray data quality (2001) J. Appl. Crystallogr, 34, pp. 130-135
Storoni, L.C., McCoy, A.J., Read, R.J., Likelihood-enhanced fast rotation functions (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 432-438
Circu, M. L., Aw, T. Y., Glutathione and apoptosis (2008) Free Radic. Res, 42, pp. 689-706
Pallardo, F. V., Markovic, J., Garcia, J. L., Vina, J., Role of nuclear glutathione as a key regulator of cell proliferation (2009) Mol. Asp. Med, 30, pp. 77-85
Mooz, E. D., Meister, A., Tripeptide (glutathione) synthetase: Purification, properties and mechanism of action (1967) Biochemistry, 6, pp. 1722-1734
Gali, R. R., Board, P. G., Sequencing and expression of a cDNA for human glutathione synthetase (1995) Biochem. J, 310, pp. 353-358
Huang, C. S., He, W., Meister, A., Anderson, M. E., Amino acid sequence of rat kidney glutathione synthetase (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 1232-1236
Chayen, N. E., Shaw Stewart, P. D., Maeder, D. L., Blow, D. M., An automated system for micro-batch protein crystallization and screening (1990) J. Appl. Cryst, 23, pp. 297-302
Chayen, N. E., Recent advances in methodology for the crystallization of biological macromolecules (1999) J. Cryst. Growth, 199, pp. 649-655
Martins, P. M., Pessoa, J., Sarkany, Z., Rocha, F., Damas, A. M., Rationalizing protein crystallization Screenings through water equilibration theory and protein solubility data (2008) Cryst. Growth Des, 8, pp. 4233-4243
Matthews, B. W., Solvent content of protein crystals (1968) J. Mol. Biol, 33, pp. 491-497
Weiss, M. S., Global indicators of X-ray data quality (2001) J. Appl. Crystallogr, 34, pp. 130-135
Storoni, L. C., McCoy, A. J., Read, R. J., Likelihood-enhanced fast rotation functions (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 432-438
Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis
Glutathione synthetases catalyze the ATP-dependent synthesis of glutathione from L-gamma-glutamyl-L-cysteine and glycine. Although these enzymes have been sequenced and characterized from a variety of biological sources, their exact catalytic mechanism is not fully understood and nothing is known about their adaptation at extremophilic environments. Glutathione synthetase from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhGshB) has been expressed, purified and successfully crystallized. An overall improvement of the crystal quality has been obtained by adapting the crystal growth conditions found with vapor diffusion experiments to the without-oil microbatch method. The best crystals of PhGshB diffract to 2.34 angstrom resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 83.28 angstrom, b = 119.88 angstrom, c = 159.82 angstrom. Refinement of the model, obtained using phases derived from the structure of the same enzyme from Escherichia coli by molecular replacement, is in progress. The structural determination will provide the first structural characterization of a psychrophilic glutathione synthetase reported to date.
Glutathione synthetases catalyze the ATP-dependent synthesis of glutathione from L-gamma-glutamyl-L-cysteine and glycine. Although these enzymes have been sequenced and characterized from a variety of biological sources, their exact catalytic mechanism is not fully understood and nothing is known about their adaptation at extremophilic environments. Glutathione synthetase from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhGshB) has been expressed, purified and successfully crystallized. An overall improvement of the crystal quality has been obtained by adapting the crystal growth conditions found with vapor diffusion experiments to the without-oil microbatch method. The best crystals of PhGshB diffract to 2.34 angstrom resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 83.28 angstrom, b = 119.88 angstrom, c = 159.82 angstrom. Refinement of the model, obtained using phases derived from the structure of the same enzyme from Escherichia coli by molecular replacement, is in progress. The structural determination will provide the first structural characterization of a psychrophilic glutathione synthetase reported to date.
Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis
| ▼ Galectins: Structure, function and therapeutic potential inhibitors Galectine: struttura, funzione e potenziali inibitori terapeutici |
Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis
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Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (362 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
Dettagli Esporta in BibTeX Esporta in EndNote
Guler OO, De Simone G, Supuran CT
* Drug design studies of the novel antitumor targets carbonic anhydrase IX and XII (457 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2010; 17(15): 1516-1526.
Impact Factor: 4.63
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Vitagliano L, Howes BD, Verde C, Di Prisco G, Smulevich G, Sica F, Vergara A
* Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins (368 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (283 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2009 Dec; 77(4): 1004-1008.
Impact Factor: 3.085
Dettagli Esporta in BibTeX Esporta in EndNote
Wekselman I, Davidovich C, Agmon I, Zimmerman E, Rozenberg H, Bashan A, Berisio R, Yonath A
* Ribosome's mode of function: Myths, facts and recent results (365 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 122-130.
Impact Factor: 1.807
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, Di Fiore A, D'Ambrosio K, Supuran CT, De Simone G
* X-Ray Crystallography of Carbonic Anhydrase Inhibitors and Its Importance in Drug Design (321 visite)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 73-138.
Impact Factor: 1.156
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Sica F, Mazzarella L, Zagari A, Vergara A
* Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10) (364 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2008 Sep; 137(1): 24-27.
Impact Factor: 2.362
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, De Simone G, Monti SM, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1, 3-disulfonamides-Solution and crystallographic studies (307 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Sep 1; 17(15): 4201-4207.
Impact Factor: 2.604
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Scozzafava A, Winum JY, Montero JL, Pedone C, Supuran CT, De Simone G
* Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties (392 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Impact Factor: 2.604
Dettagli Esporta in BibTeX Esporta in EndNote
Menchise V, De Simone G, Di Fiore A, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1, 3, 4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)1, 3, 4-thiadiazole-2-sulfon amide to human isoform II (285 visite)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Dec 15; 16(24): 6204-6208.
Impact Factor: 2.538
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Pedone C, D'Ambrosio K, Scozzafava A, De Simone G, Supuran CT
* Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib (297 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Jan 15; 16(2): 437-442.
Impact Factor: 2.538
Dettagli Esporta in BibTeX Esporta in EndNote
Vergara A, Lorber B, Sauter C, Giege R, Zagari A
* Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology (299 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005; 118(2-3): 102-112.
Impact Factor: 1.925
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction (481 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58(10II): 1695-1699.
Impact Factor: 1.76
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (390 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Sorrentino G, Carotenuto L, Piccolo C, Mazzarella L, Zagari A
Effects of microgravity on the crystal quality of a collagen-like polypeptide (356 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2000 Jan; 56(1): 55-61.
Impact Factor: 3.067
Dettagli Esporta in BibTeX Esporta in EndNote
34 Records (34 escludendo Abstract e Conferenze).
Impact factor totale: 108.924 (108.924 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 111.977 (111.977 escludendo Abstract e Conferenze).
Vai a fine pagina Versione per copia e incolla facile Esporta tutto in BibTeX Esporta tutto in EndNote
Mancuso F, Di Fiore A, De Luca L, Angeli A, De Simone G, Supuran CT, Gitto R
* Design, synthesis and biochemical evaluation of novel carbonic anhydrase inhibitors triggered by structural knowledge on hCA VII (2 visite)
Bioorg Med Chem (ISSN: 0968-0896linking), 2021 Aug 15; 44: 116279-116279.
Impact Factor: 3.641
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Wilson D, Deacon AM, Duncton MAJ, Pellicena P, Georgiadis MM, Yeh AP, Arvai AS, Moiani D, Tainer JA, Das D
* Fragment- and structure-based drug discovery for developing therapeutic agents targeting the DNA Damage Response (2 visite)
Prog Biophys Mol Biol (ISSN: 0079-6107linking), 2021 Aug; 163: 130-142.
Impact Factor: 3.667
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Langella E, Alterio V, D'Ambrosio K, Cadoni R, Winum JY, Supuran CT, Monti SM, De Simone G, Di Fiore A
* Exploring benzoxaborole derivatives as carbonic anhydrase inhibitors: a structural and computational analysis reveals their conformational variability as a tool to increase enzyme selectivity (211 visite)
J Enzym Inhib Med Ch (ISSN: 1475-6366linking, 1475-6374electronic), 2019 Dec; 34(1): 1498-1505.
Impact Factor: 4.027
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Esposito L, Donnarumma F, Ruggiero A, Leone S, Vitagliano L, Picone D
* Structure, stability and aggregation propensity of a Ribonuclease A-Onconase chimera (263 visite)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Jul 15; 133: 1125-1133.
Impact Factor: 4.784
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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 (276 visite)
Eur J Med Chem (ISSN: 1768-3254electronic, 0223-5234linking), 2019 Feb 1; 163: 443-452.
Impact Factor: 4.833
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, Esposito D, Monti SM, Supuran CT, De Simone G
* Crystal structure of the human carbonic anhydrase II adduct with 1-(4-sulfamoylphenyl-ethyl)-2, 4, 6-triphenylpyridinium perchlorate, a membrane-impermeant, isoform selective inhibitor (507 visite)
J Enzym Inhib Med Ch (ISSN: 1475-6374electronic, 1475-6366linking), 2018 Dec; 33(1): 151-157.
Impact Factor: 4.293
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Merlino A, Marzo T, Messori L
* Protein Metalation by Anticancer Metallodrugs: A Joint ESI MS and XRD Investigative Strategy (221 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2017 May 23; 23(29): 6942-6947.
Impact Factor: 5.16
Dettagli Esporta in BibTeX Esporta in EndNote
Vullo D, Supuran CT, Scozzafava A, De Simone G, Monti SM, Alterio V, Carta F
* Kinetic and X-ray crystallographic investigations of substituted 2-thio-6-oxo-1, 6-dihydropyrimidine-benzenesulfonamides acting as carbonic anhydrase inhibitors (231 visite)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391), 2016 Aug 15; 24(16): 3643-3648.
Impact Factor: 2.93
Dettagli Esporta in BibTeX Esporta in EndNote
Pica A, Chi M-C, Chen Y-Y, D'Ischia M, Lin L-L, Merlino A
* The maturation mechanism of γ-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies (297 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1864(2): 195-203.
Impact Factor: 5.476
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Messori L, Marzo T, Merlino A
* Interactions of carboplatin and oxaliplatin with proteins: Insights from X-ray structures and mass spectrometry studies of their ribonuclease A adducts (290 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2015; N/D: N/D-N/D.
Impact Factor: 3.205
Dettagli Esporta in BibTeX Esporta in EndNote
D'Ambrosio K, Lopez M, Dathan NA, Ouahrani-bettache S, Köhler S, Ascione G, Monti SM, Winum JY, De Simone G
* Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis (416 visite)
Biochimie (ISSN: 0300-9084, 1638-6183, 0300-9084linking), 2014 Feb; 97(1): 114-120.
Impact Factor: 2.963
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, Pan P, Parkkila S, Buonanno M, Supuran CT, Monti SM, De Simone G
* The Structural Comparison Between Membrane-Associated Human Carbonic Anhydrases Provides Insights Into Drug Design Of Selective Inhibitors (377 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2014; 101(7): 769-778.
Impact Factor: 2.385
Dettagli Esporta in BibTeX Esporta in EndNote
Ronda L, Merlino A, Bettati S, Verde C, Balsamo A, Mazzarella L, Mozzarelli A, Vergara A
* Role of tertiary structures on the Root effect in fish hemoglobins (380 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Sep; 1834(9): 1885-1893.
Impact Factor: 3.191
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Alterio V, Supuran CT
* Exploiting the hydrophobic and hydrophilic binding sites for designing carbonic anhydrase inhibitors (392 visite)
Expert Opin Drug Discov (ISSN: 1746-0441), 2013 Jul; 8(7): 793-810.
Impact Factor: 3.467
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Supuran CT
* (In)organic anions as carbonic anhydrase inhibitors (351 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2012 Jun; 111: 117-129.
Impact Factor: 3.197
Dettagli Esporta in BibTeX Esporta in EndNote
Ascione G, de Pascale D, De Santi C, Pedone C, Dathan NA, Monti SM
* Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity (472 visite)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2012 Apr 13; 420(3): 542-546.
Impact Factor: 2.406
Dettagli Esporta in BibTeX Esporta in EndNote
Russo Krauss I, Sica F, Mattia CA, Merlino A
* Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data (394 visite)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
Impact Factor: 2.464
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Ruggiero A, Masullo M, Ruocco MR, Lamberti A, Arcari P, Zagari A, Vitagliano L
* Crystallographic and spectroscopic characterizations of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability (283 visite)
J Struct Biol (ISSN: 1047-8477), 2012 Feb; 177(2): 506-512.
Impact Factor: 3.361
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Monti SM, Innocenti A, Winum J-Y, De Simone G, Supuran CT
* Carbonic anhydrase inhibitors: Crystallographic and solution binding studies for the interaction of a boron-containing aromatic sulfamide with mammalian isoforms I-XV (320 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2010 Jun 15; 20(12): 3601-3605.
Impact Factor: 2.661
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (362 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
Dettagli Esporta in BibTeX Esporta in EndNote
Guler OO, De Simone G, Supuran CT
* Drug design studies of the novel antitumor targets carbonic anhydrase IX and XII (457 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2010; 17(15): 1516-1526.
Impact Factor: 4.63
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Vitagliano L, Howes BD, Verde C, Di Prisco G, Smulevich G, Sica F, Vergara A
* Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins (368 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (283 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2009 Dec; 77(4): 1004-1008.
Impact Factor: 3.085
Dettagli Esporta in BibTeX Esporta in EndNote
Wekselman I, Davidovich C, Agmon I, Zimmerman E, Rozenberg H, Bashan A, Berisio R, Yonath A
* Ribosome's mode of function: Myths, facts and recent results (365 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 122-130.
Impact Factor: 1.807
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, Di Fiore A, D'Ambrosio K, Supuran CT, De Simone G
* X-Ray Crystallography of Carbonic Anhydrase Inhibitors and Its Importance in Drug Design (321 visite)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 73-138.
Impact Factor: 1.156
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Sica F, Mazzarella L, Zagari A, Vergara A
* Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10) (364 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2008 Sep; 137(1): 24-27.
Impact Factor: 2.362
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, De Simone G, Monti SM, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1, 3-disulfonamides-Solution and crystallographic studies (307 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Sep 1; 17(15): 4201-4207.
Impact Factor: 2.604
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Scozzafava A, Winum JY, Montero JL, Pedone C, Supuran CT, De Simone G
* Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties (392 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Impact Factor: 2.604
Dettagli Esporta in BibTeX Esporta in EndNote
Menchise V, De Simone G, Di Fiore A, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1, 3, 4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)1, 3, 4-thiadiazole-2-sulfon amide to human isoform II (285 visite)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Dec 15; 16(24): 6204-6208.
Impact Factor: 2.538
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Pedone C, D'Ambrosio K, Scozzafava A, De Simone G, Supuran CT
* Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib (297 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Jan 15; 16(2): 437-442.
Impact Factor: 2.538
Dettagli Esporta in BibTeX Esporta in EndNote
Vergara A, Lorber B, Sauter C, Giege R, Zagari A
* Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology (299 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005; 118(2-3): 102-112.
Impact Factor: 1.925
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction (481 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58(10II): 1695-1699.
Impact Factor: 1.76
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (390 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Sorrentino G, Carotenuto L, Piccolo C, Mazzarella L, Zagari A
Effects of microgravity on the crystal quality of a collagen-like polypeptide (356 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2000 Jan; 56(1): 55-61.
Impact Factor: 3.067
Dettagli Esporta in BibTeX Esporta in EndNote
34 Records (34 escludendo Abstract e Conferenze).
Impact factor totale: 108.924 (108.924 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 111.977 (111.977 escludendo Abstract e Conferenze).
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