Minimal structural requirements for root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi (506 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 1; 62(2): 316-321.
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Paper type: Journal Article,
Impact factor: 3.73, 5-year impact factor: 2.964
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-30144436769&partnerID=40&md5=07f824d57b5d3d0c008ec831a970b026
Keywords: Antarctic Fish Hemoglobin, Cooperativity, Root Effect, Aspartic Acid, Bohr Effect Protein, Histidine, Isoleucine, Oxygen, Root Effect Protein, Serine, Unclassified Drug, Amino Acid Sequence, Binding Affinity, Crystal Structure, Hydrogen Bond, Molecular Interaction, Nonhuman, Priority Journal, Protein Function, Protein Isolation, Protein Stability, Protein Structure, Trematomus Newnesi, Animals, Antarctic Regions, Carboxyhemoglobin, Crystallization, Crystallography, X-Ray, Electrons, Macromolecular Substances, Models, Protein Conformation, Secondary,
Affiliations:
*** IBB - CNR ***
Dipartimento di Chimica, Universitá degli Studi di Napoli Federico II, Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Naples, Italy
Centro Regionale di Competenza Bioteknet, Complesso Ristrutturato S. Andrea delle Dame, Naples, Italy
Istituto di Biochimica delle Proteine, CNR, Naples, Italy
References:
Perutz, M.F., Wilkinson, A.J., Paoli, M., Dodson, G.G., The stereochemical mechanism of the cooperative effects in hemoglobin revisited (1998) Ann Rev Biophys Biomol Struct, 27, pp. 1-3
Perutz, M., Stereochemistry of cooperative effects in hemoglobin. Bohr effect and combination with organic phosphates (1970) Nature (London), 228, pp. 734-739
Weber, R.E., Fago, A., Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins (2004) Respir Physiol Neurobiol, 144, pp. 141-159
Bonaventura, C., Crumbliss, A.L., Weber, R.E., New insights into the proton-dependent oxygen affinity of Root effect haemoglobins (2004) Acta Physiol Scand, 182, pp. 245-258
Brittain, T., The Root effect in hemoglobins (2005) J Inorg Biochem, 99, pp. 120-129
Berenbrink, M., Koldkiaer, P., Kepp, O., Cossins, A.R., Evolution of oxygen secretion in fishes and the emergence of a complex physiological system (2005) Science, 307, pp. 1752-1757
Pelster, B., Decker, H., The Root effect - A physiological perspective (2004) Micron, 35, pp. 73-74
Perutz, M.F., Brunori, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature (London), 299, pp. 421-426
Ito, N., Komiyama, N.H., Fermi, G., Structure of deoxyhemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the root effect by comparison of the liganded and unliganded hemoglobin structures (1995) J Mol Biol, 250, pp. 648-658
Mazzarella, L., D'Avino, R., Di Prisco, G., Savino, C., Vitagliano, L., Pce, M., Zagari, A., Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question (1999) J Mol Biol, 287, pp. 897-906
Mylvaganam, S.E., Bonaventura, C., Bonaventura, J., Getzoff, E.D., Structural basis for the Root effect in hemoglobin (1996) Nat Struct Biol, 3, pp. 275-283
Perutz, M.F., Cause of the Root effect in fish hemoglobins (1996) Nat Struct Biol, 3, pp. 211-212
Yokoyama, T., Chong, K.T., Miyazaki, G., Morimoto, H., Shih, D.T.B., Unzai, S., Tame, J.R.H., Park, S.-Y., Novel mechanisms of pH sensitivity in tuna hemoglobin: A structural explanation of the root effect (2004) J Biol Chem, 279, pp. 28632-28640
D'Avino, R., Caruso, C., Tamburrini, M., Romano, M., Rutigliano, B., Polverino De Laureto, P., Camardella, L., Di Prisco, G., Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi (1994) J Biol Chem, 269, pp. 9675-9681
Perutz, M.F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R.C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Acc Chem Res, 9, pp. 309-321
D'Avino, R., De Luca, R., Molecular modeling of Trematomus newnesi Hb 1: Insights for a lowered oxygen affinity and lack of root effect (2000) Proteins, 39, pp. 155-165
Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G., Perutz, M.F., Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative (1992) J Mol Biol, 224, pp. 449-460
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Navaza, J., AMoRe an automated package for molecular replacement (1994) Acta Cryst A, 50, pp. 157-163
Brunger, A.T., (1996) X-PLOR Version 8.5, , Yale University Press. New Haven, CT
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjedgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Cryst D, 56, pp. 714-721
Hooft, R.W., Vriend, G., Sander, C., Abola, E.E., Errors in protein structures (1996) Nature (London), 381, p. 272
Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The Protein Data Bank (2000) Nucleic Acids Res, 28, pp. 235-242
Tame, J.R.H., Wilson, J.C., Weber, R.E., The crystal structure of Trout Hb I in the deoxy and carbomonoxy forms (1996) J Mol Biol, 259, pp. 249-760
Nagai, K., Perutz, M.F., Poyart, C., Studies of hemoglobin functions by site-directed mutagenesis (1986) Phil Trans Royal Soc London A, 317, pp. 443-447
Nagai, K., Luisi, B., Shih, D., Miyazaki, G., Imai, K., Poyart, C., De Young, A., Yu, N.-T., Distal residues in the oxygen binding site of haemoglobin studied by protein engineering (1987) Nature (London), 329, pp. 858-860
Vitagliano, L., Bonomi, G., Riccio, A., Di Prisco, G., Smulevich, G., Mazzarella, L., The oxidation process of Antarctic fish hemoglobins (2004) Eur J Biochem, 271, pp. 1651-1659
Binotti, I., Giovenco, S., Giardina, B., Antonini, E., Brunori, M., Wyman, J., Functional properties of fish hemoglobins. II. Oxygen equilibrium of the isolated hemoglobin components from trout blood (1971) Arch Biochem Biophys, 142, pp. 274-280
Shih Daniel, T.B., Jones, R.T., Imai, K., Tyima, I., Involvement of Glu G3(101)b in the function of hemoglobin. Comparative oxygen equilibrium studies of human mutant hemoglobins (1985) J Biol Chem, 260, pp. 5919-5924
Riccio, A., Vitagliano, L., Di Prisco, G., Zagari, A., Mazzarella, L., Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: Crystallization of an R-state haemichrome intermediate (2001) Acta Cryst D, 57, pp. 1144-1146
Perutz, M. F., Wilkinson, A. J., Paoli, M., Dodson, G. G., The stereochemical mechanism of the cooperative effects in hemoglobin revisited (1998) Ann Rev Biophys Biomol Struct, 27, pp. 1-3
Weber, R. E., Fago, A., Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins (2004) Respir Physiol Neurobiol, 144, pp. 141-159
Perutz, M. F., Brunori, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature (London), 299, pp. 421-426
Mylvaganam, S. E., Bonaventura, C., Bonaventura, J., Getzoff, E. D., Structural basis for the Root effect in hemoglobin (1996) Nat Struct Biol, 3, pp. 275-283
Perutz, M. F., Cause of the Root effect in fish hemoglobins (1996) Nat Struct Biol, 3, pp. 211-212
Perutz, M. F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R. C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Acc Chem Res, 9, pp. 309-321
Brunger, A. T., (1996) X-PLOR Version 8. 5, , Yale University Press. New Haven, CT
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjedgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Cryst D, 56, pp. 714-721
Hooft, R. W., Vriend, G., Sander, C., Abola, E. E., Errors in protein structures (1996) Nature (London), 381, p. 272
Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., Bourne, P. E., The Protein Data Bank (2000) Nucleic Acids Res, 28, pp. 235-242
Tame, J. R. H., Wilson, J. C., Weber, R. E., The crystal structure of Trout Hb I in the deoxy and carbomonoxy forms (1996) J Mol Biol, 259, pp. 249-760
Shih Daniel, T. B., Jones, R. T., Imai, K., Tyima, I., Involvement of Glu G3 (101) b in the function of hemoglobin. Comparative oxygen equilibrium studies of human mutant hemoglobins (1985) J Biol Chem, 260, pp. 5919-5924
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 1; 62(2): 316-321.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.73, 5-year impact factor: 2.964
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-30144436769&partnerID=40&md5=07f824d57b5d3d0c008ec831a970b026
Keywords: Antarctic Fish Hemoglobin, Cooperativity, Root Effect, Aspartic Acid, Bohr Effect Protein, Histidine, Isoleucine, Oxygen, Root Effect Protein, Serine, Unclassified Drug, Amino Acid Sequence, Binding Affinity, Crystal Structure, Hydrogen Bond, Molecular Interaction, Nonhuman, Priority Journal, Protein Function, Protein Isolation, Protein Stability, Protein Structure, Trematomus Newnesi, Animals, Antarctic Regions, Carboxyhemoglobin, Crystallization, Crystallography, X-Ray, Electrons, Macromolecular Substances, Models, Protein Conformation, Secondary,
Affiliations:
*** IBB - CNR ***
Dipartimento di Chimica, Universitá degli Studi di Napoli Federico II, Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Naples, Italy
Centro Regionale di Competenza Bioteknet, Complesso Ristrutturato S. Andrea delle Dame, Naples, Italy
Istituto di Biochimica delle Proteine, CNR, Naples, Italy
References:
Perutz, M.F., Wilkinson, A.J., Paoli, M., Dodson, G.G., The stereochemical mechanism of the cooperative effects in hemoglobin revisited (1998) Ann Rev Biophys Biomol Struct, 27, pp. 1-3
Perutz, M., Stereochemistry of cooperative effects in hemoglobin. Bohr effect and combination with organic phosphates (1970) Nature (London), 228, pp. 734-739
Weber, R.E., Fago, A., Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins (2004) Respir Physiol Neurobiol, 144, pp. 141-159
Bonaventura, C., Crumbliss, A.L., Weber, R.E., New insights into the proton-dependent oxygen affinity of Root effect haemoglobins (2004) Acta Physiol Scand, 182, pp. 245-258
Brittain, T., The Root effect in hemoglobins (2005) J Inorg Biochem, 99, pp. 120-129
Berenbrink, M., Koldkiaer, P., Kepp, O., Cossins, A.R., Evolution of oxygen secretion in fishes and the emergence of a complex physiological system (2005) Science, 307, pp. 1752-1757
Pelster, B., Decker, H., The Root effect - A physiological perspective (2004) Micron, 35, pp. 73-74
Perutz, M.F., Brunori, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature (London), 299, pp. 421-426
Ito, N., Komiyama, N.H., Fermi, G., Structure of deoxyhemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the root effect by comparison of the liganded and unliganded hemoglobin structures (1995) J Mol Biol, 250, pp. 648-658
Mazzarella, L., D'Avino, R., Di Prisco, G., Savino, C., Vitagliano, L., Pce, M., Zagari, A., Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question (1999) J Mol Biol, 287, pp. 897-906
Mylvaganam, S.E., Bonaventura, C., Bonaventura, J., Getzoff, E.D., Structural basis for the Root effect in hemoglobin (1996) Nat Struct Biol, 3, pp. 275-283
Perutz, M.F., Cause of the Root effect in fish hemoglobins (1996) Nat Struct Biol, 3, pp. 211-212
Yokoyama, T., Chong, K.T., Miyazaki, G., Morimoto, H., Shih, D.T.B., Unzai, S., Tame, J.R.H., Park, S.-Y., Novel mechanisms of pH sensitivity in tuna hemoglobin: A structural explanation of the root effect (2004) J Biol Chem, 279, pp. 28632-28640
D'Avino, R., Caruso, C., Tamburrini, M., Romano, M., Rutigliano, B., Polverino De Laureto, P., Camardella, L., Di Prisco, G., Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi (1994) J Biol Chem, 269, pp. 9675-9681
Perutz, M.F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R.C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Acc Chem Res, 9, pp. 309-321
D'Avino, R., De Luca, R., Molecular modeling of Trematomus newnesi Hb 1: Insights for a lowered oxygen affinity and lack of root effect (2000) Proteins, 39, pp. 155-165
Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G., Perutz, M.F., Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative (1992) J Mol Biol, 224, pp. 449-460
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Navaza, J., AMoRe an automated package for molecular replacement (1994) Acta Cryst A, 50, pp. 157-163
Brunger, A.T., (1996) X-PLOR Version 8.5, , Yale University Press. New Haven, CT
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjedgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Cryst D, 56, pp. 714-721
Hooft, R.W., Vriend, G., Sander, C., Abola, E.E., Errors in protein structures (1996) Nature (London), 381, p. 272
Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The Protein Data Bank (2000) Nucleic Acids Res, 28, pp. 235-242
Tame, J.R.H., Wilson, J.C., Weber, R.E., The crystal structure of Trout Hb I in the deoxy and carbomonoxy forms (1996) J Mol Biol, 259, pp. 249-760
Nagai, K., Perutz, M.F., Poyart, C., Studies of hemoglobin functions by site-directed mutagenesis (1986) Phil Trans Royal Soc London A, 317, pp. 443-447
Nagai, K., Luisi, B., Shih, D., Miyazaki, G., Imai, K., Poyart, C., De Young, A., Yu, N.-T., Distal residues in the oxygen binding site of haemoglobin studied by protein engineering (1987) Nature (London), 329, pp. 858-860
Vitagliano, L., Bonomi, G., Riccio, A., Di Prisco, G., Smulevich, G., Mazzarella, L., The oxidation process of Antarctic fish hemoglobins (2004) Eur J Biochem, 271, pp. 1651-1659
Binotti, I., Giovenco, S., Giardina, B., Antonini, E., Brunori, M., Wyman, J., Functional properties of fish hemoglobins. II. Oxygen equilibrium of the isolated hemoglobin components from trout blood (1971) Arch Biochem Biophys, 142, pp. 274-280
Shih Daniel, T.B., Jones, R.T., Imai, K., Tyima, I., Involvement of Glu G3(101)b in the function of hemoglobin. Comparative oxygen equilibrium studies of human mutant hemoglobins (1985) J Biol Chem, 260, pp. 5919-5924
Riccio, A., Vitagliano, L., Di Prisco, G., Zagari, A., Mazzarella, L., Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: Crystallization of an R-state haemichrome intermediate (2001) Acta Cryst D, 57, pp. 1144-1146
Perutz, M. F., Wilkinson, A. J., Paoli, M., Dodson, G. G., The stereochemical mechanism of the cooperative effects in hemoglobin revisited (1998) Ann Rev Biophys Biomol Struct, 27, pp. 1-3
Weber, R. E., Fago, A., Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins (2004) Respir Physiol Neurobiol, 144, pp. 141-159
Perutz, M. F., Brunori, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature (London), 299, pp. 421-426
Mylvaganam, S. E., Bonaventura, C., Bonaventura, J., Getzoff, E. D., Structural basis for the Root effect in hemoglobin (1996) Nat Struct Biol, 3, pp. 275-283
Perutz, M. F., Cause of the Root effect in fish hemoglobins (1996) Nat Struct Biol, 3, pp. 211-212
Perutz, M. F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R. C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Acc Chem Res, 9, pp. 309-321
Brunger, A. T., (1996) X-PLOR Version 8. 5, , Yale University Press. New Haven, CT
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjedgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Cryst D, 56, pp. 714-721
Hooft, R. W., Vriend, G., Sander, C., Abola, E. E., Errors in protein structures (1996) Nature (London), 381, p. 272
Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., Bourne, P. E., The Protein Data Bank (2000) Nucleic Acids Res, 28, pp. 235-242
Tame, J. R. H., Wilson, J. C., Weber, R. E., The crystal structure of Trout Hb I in the deoxy and carbomonoxy forms (1996) J Mol Biol, 259, pp. 249-760
Shih Daniel, T. B., Jones, R. T., Imai, K., Tyima, I., Involvement of Glu G3 (101) b in the function of hemoglobin. Comparative oxygen equilibrium studies of human mutant hemoglobins (1985) J Biol Chem, 260, pp. 5919-5924
Minimal structural requirements for root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi
The cathodic hemoglobin component of the Antarctic fish Trematomus newnesi (HbCTn) is a Root-effect protein. The interpretation of its functional properties in relation to its sequence is puzzling. Indeed, HbCTn sequence is characterized by an extremely low histidyl content, and in particular by the lack of His146 beta and His69 beta, which are believed to be important in Bohr and Root effects, respectively. Furthermore, previous analyses suggested that the local environment of Asp95 alpha, Asp99 beta, and Asp101 beta should not be appropriate for the formation of Asp-Asp interactions, which are important for the Root effect. Here, we report the high-resolution crystal structure of the deoxy form of HbCTn. Our data provide a structural interpretation for the very low oxygen affinity of the protein and insights into the structural determinants of the Root effect protein. The structure demonstrates that the presence of Ile41 alpha and Ser97 alpha at the alpha(1)beta(2) interface does not prevent the formation of the inter-Asp interactions in HbCTn, as previous studies had suggested. The present data indicate that the hydrogen bond formed between Asp95a and Asp101 beta, which is stabilized by Asp99 beta, is per se sufficient to generate the Root effect, and it is the minimal structural requirement needed for the design of Root-effect Hbs.
The cathodic hemoglobin component of the Antarctic fish Trematomus newnesi (HbCTn) is a Root-effect protein. The interpretation of its functional properties in relation to its sequence is puzzling. Indeed, HbCTn sequence is characterized by an extremely low histidyl content, and in particular by the lack of His146 beta and His69 beta, which are believed to be important in Bohr and Root effects, respectively. Furthermore, previous analyses suggested that the local environment of Asp95 alpha, Asp99 beta, and Asp101 beta should not be appropriate for the formation of Asp-Asp interactions, which are important for the Root effect. Here, we report the high-resolution crystal structure of the deoxy form of HbCTn. Our data provide a structural interpretation for the very low oxygen affinity of the protein and insights into the structural determinants of the Root effect protein. The structure demonstrates that the presence of Ile41 alpha and Ser97 alpha at the alpha(1)beta(2) interface does not prevent the formation of the inter-Asp interactions in HbCTn, as previous studies had suggested. The present data indicate that the hydrogen bond formed between Asp95a and Asp101 beta, which is stabilized by Asp99 beta, is per se sufficient to generate the Root effect, and it is the minimal structural requirement needed for the design of Root-effect Hbs.
Minimal structural requirements for root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi
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Minimal structural requirements for root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi
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Merlino A, Vitagliano L, Howes BD, Verde C, Di Prisco G, Smulevich G, Sica F, Vergara A
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Zannetti A, Del Vecchio S, Iommelli F, Del Gatto A, De Luca S, Zaccaro L, Papaccioli A, Sommella J, Panico M, Speranza A, Grieco P, Novellino E, Saviano M, Pedone C, Salvatore M
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Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, Di Prisco G, Lee HC, Peisach J, Mazzarella L
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La Mendola D, Magrì A, Hansson O, Bonomo RP, Rizzarelli E
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Zaccaro L, Del Gatto A, Pedone C, Saviano M
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Verde C, Vergara A, Mazzarella L, Di Prisco G
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Pastore C, Franzese M, Sica F, Temussi P, Pastore A
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Verde C, Vergara A, Giordano D, Mazzarella L, Di Prisco G
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Vitagliano L, Bonomi G, Franzese M, Merlino A, Vergara A, Verde C, Di Prisco G, Mazzarella L
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Esposito L, Vitagliano L, Sica F, Sorrentino G, Zagari A, Mazzarella L
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Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
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Capasso S, Di Donato A, Esposito L, Sica F, Sorrentino G, Vitagliano L, Zagari A, Mazzarella L
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Sijens PE, Knopp MV, Brunetti A, Wicklow K, Alfano B, Bachert P, Sanders JA, Stillman AE, Kett H, Sauter R
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Cervo A, Cocozza S, Saccà F, Giorgio SM, Morra VB, Tedeschi E, Marsili A, Vacca G, Palma V, Brunetti A, Quarantelli M
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Lin L-L, Chen Y-Y, Chi M-C, Merlino A
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Ronda L, Merlino A, Bettati S, Verde C, Balsamo A, Mazzarella L, Mozzarelli A, Vergara A
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Dolga AM, Netter MF, Perocchi F, Doti N, Meissner L, Tobaben S, Grohm J, Zischka H, Plesnila N, Decher N, Culmsee C
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Impact Factor: 3.514
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Vergara A, Vitagliano L, Merlino A, Sica F, Marino K, Verde C, di Prisco G, Mazzarella L
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Impact Factor: 5.328
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Coppola D, Giordano D, Vergara A, Mazzarella L, Di Prisco G, Verde C, Russo R
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Guarnieri D, De Capua A, Ventre M, Borzacchiello A, Pedone C, Marasco D, Ruvo M, Netti PA
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Impact Factor: 4.824
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Monfregola L, Saviano M, De Luca S
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Impact Factor: 1.034
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Satriano C, Messina GM, Marino C, Aiello I, Conte E, La Mendola D, Distefano DA, D'Alessandro F, Pappalardo G, Impellizzeri G
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Impact Factor: 3.068
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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 (413 views)
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Impact Factor: 2.605
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Zannetti A, Del Vecchio S, Iommelli F, Del Gatto A, De Luca S, Zaccaro L, Papaccioli A, Sommella J, Panico M, Speranza A, Grieco P, Novellino E, Saviano M, Pedone C, Salvatore M
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Impact Factor: 6.747
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Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, Di Prisco G, Lee HC, Peisach J, Mazzarella L
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Impact Factor: 4.39
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D'Ambrosio K, Limauro D, Pedone E, Galdi I, Pedone C, Bartolucci S, De Simone G
* Insights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricus (469 views)
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Impact Factor: 3.085
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Ruggiero I, Cantiello P, Lamberti A, Sorrentino A, Martucci NM, Ruggiero A, Arcone R, Vitagliano L, Arcari P, Masullo M
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Impact Factor: 3.897
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La Mendola D, Magrì A, Hansson O, Bonomo RP, Rizzarelli E
* Copper(II) complexes with peptide fragments encompassing the sequence 122-130 of human doppel protein (361 views)
Journal Of Inorganic Biochemistry, 2009 May; 103(5): 758-765.
Impact Factor: 3.444
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Bonomo RP, Di Natale G, Rizzarelli E, Tabbì G, Vagliasindi LI
* Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies (411 views)
Dalton T (ISSN: 1477-9226, 1477-7922, 1477-9234), 2009 Apr 14; (14): 2637-2646.
Impact Factor: 2.908
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Zaccaro L, Del Gatto A, Pedone C, Saviano M
* Peptides for tumour therapy and diagnosis: current status and future directions (1011 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2009 Mar; 16(7): 780-795.
Impact Factor: 4.708
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Merlino A, Vergara A, Sica F, Mazzarella L
* The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins (331 views)
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 51-56.
Impact Factor: 1.2
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Verde C, Vergara A, Mazzarella L, Di Prisco G
* The Hemoglobins of Fishes Living at Polar Latitudes - Current Knowledge on Structural Adaptations in a Changing Environment (389 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Dec; 9(6): 578-590.
Impact Factor: 3.011
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Caraci F, Busceti C, Biagioni F, Aronica E, Mastroiacovo F, Cappuccio I, Battaglia G, Bruno V, Caricasole A, Copani A, Nicoletti
* The Wnt antagonist, Dickkopf-1, as a target for the treatment of neurodegenerative disorders (388 views)
Neurochemical Research (ISSN: 0364-3190, 1573-6903), 2008 Dec; 33(12): 2401-2406.
Impact Factor: 2.26
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Pastore C, Franzese M, Sica F, Temussi P, Pastore A
* Understanding the binding properties of an unusual metal-binding protein - a study of bacterial frataxin (409 views)
Febs Journal (ISSN: 1742-464x), 2007 Sep; 274(16): 4199-4210.
Impact Factor: 3.396
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Verde C, Vergara A, Giordano D, Mazzarella L, Di Prisco G
* The Root effect - a structural and evolutionary perspective (250 views)
Antarctic Science (ISSN: 0954-1020), 2007 Jun; 19(2): 271-278.
Impact Factor: 1.265
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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 (290 views)
J Chromatogr A (ISSN: 0021-9673, 0021-9673linking), 2007; 1155(2): 172-179.
Impact Factor: 3.641
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Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, Di Prisco G
* High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the root effect (389 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Nov 1; 65(2): 490-498.
Impact Factor: 3.73
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D'Andrea LD, Del Gatto A, Pedone C, Benedetti E
* Peptide-based molecules in angiogenesis (828 views)
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285, 1747-0277linking), 2006 Feb; 67(2): 115-126.
Impact Factor: 2.507
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Herga S, Brutus A, Vitale RM, Miche H, Perrier J, Puigserver A, Scaloni A, Giardina T
* Site-directed mutagenesis and molecular modelling studies show the role of Asp82 and cysteines in rat acylase 1, a member of the M20 family (338 views)
Biochem Biophys Res Commun (ISSN: 0006-291xprint, 0006-291xlinking), 2005 May 6; 330(2): 540-546.
Impact Factor: 3
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Vitagliano L, Bonomi G, Franzese M, Merlino A, Vergara A, Verde C, Di Prisco G, Mazzarella L
* Structural Characterization Of The Oxidation Pathway Of Antarctic Fish Hemoglobins (313 views)
Acta Crystallogr D Biol Crystallogr, 2005; N/D: N/D-N/D.
Impact Factor: 2.069
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Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L
* The oxidation process of Antarctic fish hemoglobins (451 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 May; 271(9): 1651-1659.
Impact Factor: 3.26
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Merlino A, Vitagliano L, Ceruso M, Di Nola A, Mazzarella L
* Global and local motions in ribonuclease A: A molecular dynamics study (411 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2002 Nov 15; 65(4): 274-283.
Impact Factor: 2.372
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Dathan N, Zaccaro L, Esposito S, Isernia C, Omichinski JG, Riccio A, Pedone C, Di Blasio B, Fattorusso R, Pedone PV
* The Arabidopsis SUPERMAN protein is able to specifically bind DNA through its single Cys(2)-His(2) zinc finger motif (635 views)
Nucleic Acids Res (ISSN: 0305-1048, 1362-4962, 1362-4962electronic), 2002 Nov 15; 30(22): 4945-4951.
Impact Factor: 7.051
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De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (425 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
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Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (424 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
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Garzillo AM, Colao MC, Buonocore V, Oliva R, Falcigno L, Saviano M, Santoro AM, Zappala R, Bonomo RP, Bianco C, Giardina P, Palmieri G, Sannia G
* Structural and kinetic characterization of native laccases from Pleurotas ostreatus, Rigidoporus lignosus, and Trametes trogii (456 views)
Journal Of Protein Chemistry (ISSN: 0277-8033), 2001 Apr; 20(3): 191-201.
Impact Factor: 1.021
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Esposito L, Vitagliano L, Sica F, Sorrentino G, Zagari A, Mazzarella L
The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis (679 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Mar 31; 297(3): 713-732.
Impact Factor: 5.388
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Mazzarella L, D'Avino R, Di Prisco G, Savino C, Vitagliano L, Moody P, Zagari A
Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question (388 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Apr 16; 287(5): 897-906.
Impact Factor: 5.501
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Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins (378 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 1999 Jan 12; 38(2): 549-559.
Impact Factor: 4.493
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Capasso S, Di Donato A, Esposito L, Sica F, Sorrentino G, Vitagliano L, Zagari A, Mazzarella L
Deamidation in proteins: The crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67 (481 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1996; 257(3): 492-496.
Impact Factor: 5.673
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Sijens PE, Knopp MV, Brunetti A, Wicklow K, Alfano B, Bachert P, Sanders JA, Stillman AE, Kett H, Sauter R
1H MR spectroscopy in patients with metastatic brain tumors: A multicenter study (350 views)
Magn Reson Med (ISSN: 0740-3194, 1522-2594electronic, 0740-3194linking), 1995 Jun; 33(6): 818-826.
Impact Factor: 3.012
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51 Records (50 excluding Abstracts).
Total impact factor: 216.457 (214.388 excluding Abstracts).
Total 5 year impact factor: 235.234 (217.997 excluding Abstracts).
Total impact factor: 216.457 (214.388 excluding Abstracts).
Total 5 year impact factor: 235.234 (217.997 excluding Abstracts).
506 views. Last view on Saturday 14 January 2023, 19:39:25
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