Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis (264 visite)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2011 Sep; 12(9): 6312-6319.
Tipo di articolo: Journal Article,
Impact factor: 2.598, Impact factor a 5 anni: 2.617
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-80053206933&partnerID=40&md5=9ec9c40b3434ed0ebff0bd50fadccefe
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,
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
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.
Tipo di articolo: Journal Article,
Impact factor: 2.598, Impact factor a 5 anni: 2.617
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-80053206933&partnerID=40&md5=9ec9c40b3434ed0ebff0bd50fadccefe
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,
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
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
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.
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De Simone G, Supuran CT
* (In)organic anions as carbonic anhydrase inhibitors (246 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2012 Jun; 111: 117-129.
Impact Factor: 3.197
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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 (367 visite)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2012 Apr 13; 420(3): 542-546.
Impact Factor: 2.406
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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 (232 visite)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
Impact Factor: 2.464
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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 (204 visite)
J Struct Biol (ISSN: 1047-8477), 2012 Feb; 177(2): 506-512.
Impact Factor: 3.361
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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 (194 visite)
Biomacromolecules (ISSN: 1525-7797), 2011 Jun; 12(6): 2311-2318.
Impact Factor: 5.479
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Casciaro S, Conversano F, Ragusa A, Malvindi MA, Franchini R, Greco A, Pellegrino T, Gigli G
* Optimal enhancement configuration of silica nanoparticles for ultrasound imaging and automatic detection at conventional diagnostic frequencies (254 visite)
Invest Radiol (ISSN: 0020-9996, 1536-0210, 1536-0210electronic), 2010 Nov; 45(11): 715-724.
Impact Factor: 4.67
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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 (200 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2010 Jun 15; 20(12): 3601-3605.
Impact Factor: 2.661
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De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (245 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
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Guler OO, De Simone G, Supuran CT
* Drug design studies of the novel antitumor targets carbonic anhydrase IX and XII (317 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2010; 17(15): 1516-1526.
Impact Factor: 4.63
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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 (272 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
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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 (205 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2009 Dec; 77(4): 1004-1008.
Impact Factor: 3.085
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Accardo A, Tesauro D, Morisco A, Mangiapia G, Vaccaro M, Gianolio E, Heenan RK, Paduano L, Morelli G
* Micelles obtained by aggregation of gemini surfactants containing the CCK8 peptide and a gadolinium complex (304 visite)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257linking), 2009 May; 14(4): 587-599.
Impact Factor: 3.415
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Grasso G, Rizzarelli E, Spoto G
* The proteolytic activity of insulin-degrading enzyme: a mass spectrometry study (280 visite)
J Mass Spectrom (ISSN: 1096-9888, 1076-5174), 2009 May; 44(5): 735-741.
Impact Factor: 3.411
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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 (233 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 122-130.
Impact Factor: 1.807
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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 (238 visite)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 73-138.
Impact Factor: 1.156
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Merlino A, Sica F, Mazzarella L, Zagari A, Vergara A
* Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10) (288 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2008 Sep; 137(1): 24-27.
Impact Factor: 2.362
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Accardo A, Tesauro D, Del Pozzo L, Mangiapia G, Paduano L, Morelli G
* Micelles by self-assembling peptide-conjugate amphiphile: Synthesis and structural characterization (281 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008 Sep; 14(8): 903-910.
Impact Factor: 1.654
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Calabrese V, Mancuso C, Calvani M, Rizzarelli E, Butterfield DA, Stella AM
* Nitric oxide in the central nervous system: neuroprotection versus neurotoxicity (342 visite)
Nature Reviews Neuroscience (ISSN: 1471-0048), 2007 Oct; 8(10): 766-775.
Impact Factor: 24.52
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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 (221 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Sep 1; 17(15): 4201-4207.
Impact Factor: 2.604
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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 (259 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Impact Factor: 2.604
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Cucinotta V, Giuffrida A, Grasso G, Maccarrone G, Messina M, Vecchio G
* High selectivity in new chiral separations of dansyl amino acids by cyclodextrin derivatives in electrokinetic chromatography (187 visite)
J Chromatogr A (ISSN: 0021-9673), 2007; 1155(2): 172-179.
Impact Factor: 3.641
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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 (191 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 (212 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Jan 15; 16(2): 437-442.
Impact Factor: 2.538
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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 (171 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005; 118(2-3): 102-112.
Impact Factor: 1.925
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Monfrecola G, Procaccini EM, D'Onofrio D, Roberti G, Liuzzi R, Staibano S, Manco A, De Rosa G, Santoianni P
* Hyperpigmentation induced by topical 5-aminolaevulinic acid plus visible light (224 visite)
J Photochem Photobiol B (ISSN: 1011-1344, 1011-1344print, 1011-1344linking), 2002 Nov; 68(2-3): 147-155.
Impact Factor: 1.573
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 (379 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 (270 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
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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 (264 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
50 Records (49 escludendo Abstract e Conferenze).
Impact factor totale: 189.634 (185.446 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 203.27 (196.107 escludendo Abstract e Conferenze).
Impact factor totale: 189.634 (185.446 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 203.27 (196.107 escludendo Abstract e Conferenze).
Esporta in BibTeX Esporta in EndNote
Ultima modifica di Marco Comerci in data Sunday 12 July 2020, 13:14:58
264 visite. Ultima visita in data Thursday 23 July 2020, 21:03:27
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