The oxidation process of Antarctic fish hemoglobins (451 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 May; 271(9): 1651-1659.
Export to BibTeX Export to EndNote
Paper type: Erratum, Journal Article,
Impact factor: 3.26, 5-year impact factor: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2342503233&partnerID=40&md5=1566add68c835ad2a9652f9dddb6c301
Keywords: Antarctic Fish, Hemichrome, Hemoglobin, Hexa-Coordination, Oxidation, Alpha (aquomet) Beta (bishistidylhemichrome), Ferricyanide, Hemoglobin Derivative, Reducing Agent, Unclassified Drug, Alpha Chain, Article, Beta Chain, Controlled Study, Nonhuman, Priority Journal, Protein Structure, Ultraviolet Spectroscopy, Vertebrate, X Ray Crystallography, Animals, Antarctic Regions, Crystallization, Oxidation-Reduction, Quaternary, Tertiary, Spectrum Analysis, Notothenioidei, Pisces, Trematomus, Trematomus Bernacchii, Trematomus Newnesi, Erratum, Fishes Blood, Hemoglobins Chemistry,
Affiliations:
*** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, CNR, Napoli, Italy
Dipartimento di Chimica, Univ. Studi di Napoli 'Federico II', Complesso Univ. di M.S. Angelo, Napoli, Italy
Ist. di Biochimica delle Proteine, CNR, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy.,
References:
Royer Jr., W.E., Knapp, J.E., Strand, K., Heaslet, H.A., Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms (2001) Trends Biochem. Sci., 26, pp. 297-30
Di Prisco, G., Molecular adaptations of Antarctic fish haemoglobins (1998) Fishes of Antarctica: Biological Overview, pp. 339-353. , di Prisco G., Pisano E. & Clark A., eds, Springer, Milan
Di Prisco, G., D'Avino, R., Caruso, C., Tamburrini, M., Camardella, L., Rutigliano, B., Carratore, V., Romano, M., The biochemistry of oxygen transport in red-blooded Antarctic fish (1991) Biology of Antarctic Fish, pp. 263-281. , di Prisco, G., Maresca, B. & Tota, B., eds, Springer-Verlag, Milan
Ruud, J.T., Vertebrates without erythrocytes and blood pigment (1954) Nature (London), 173, pp. 848-850
Di Prisco, G., Macdonald, J.A., Brunori, M., Antarctic fishes survive exposure to carbon monoxide (1992) Experientia, 48, pp. 473-475
Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G., Perutz, M.F., Haemoglobin 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
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 Crystallogr., D57, pp. 1144-1146
Baldwin, J., Chothia, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) J. Mol. Biol., 129, pp. 175-220
Perutz, M.F., Nature of haem-haem interaction (1972) Nature (London), 237, pp. 495-499
Tamburrini, M., Brancaccio, A., Ippoliti, R., Di Prisco, G., The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps (1992) Arch. Biochem. Biophys., 292, pp. 295-302
Perez, J.E., Maclean, N., Multiple globins and haemoglobins in four species of grey mullet (Mugilidae, Teleosta) (1976) Comp. Biochem. Physiol. B, 53, pp. 465-468
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Mazzarella, L., Di D'Avino, R., Di Prisco, G., Savino, C., Vitagliano, L., Moody, P.C.E., Zagari, A., Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question (1999) J. Mol. Biol., 287, pp. 897-906
Navaza, J., AMoRe an automated package for molecular replacement (1994) Acta Crystallogr., A50, pp. 157-163
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.-S., Warren, G.L., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr., D54, pp. 905-921
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr., A47, pp. 110-119
Ito, N., Komiyama, N.H., Fermi, G., Structure of deoxyhaemoglobin of the antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the root effect by comparison of the liganded and unliganded haemoglobin structures (1995) J. Mol. Biol., 250, pp. 648-658
Schneider, T.R., Objective comparison of protein structures: Error-scaled difference distance matrices (2000) Acta Crystallogr., D56, pp. 714-721
Antonini, E., Brunori, M., (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, , North-Holland Publishers Co, Amsterdam
Feis, A., Marzocchi, M.P., Paoli, M., Smulevich, G., Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures (1994) Biochemistry, 33, pp. 4577-4583
Jensen, F.B., Comparative analysis of autoxidation of haemoglobin (2001) J. Exp. Biol., 204, pp. 2029-2033
Wilson Jr., R.R., Knowles, F.C., Temperature adaptation of fish hemoglobins reflected in rates of autoxidation (1987) Arch. Biochem. Biophys., 255, pp. 210-213
Perutz, M.F., Heidner, E.J., Ladner, J.E., Beetlestone, J.G., Ho, C., Slade, E.F., Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction (1974) Biochemistry, 13, pp. 2187-2200
Stam, W.T., Beintema, J.J., D'Avino, R., Tamburrini, M., Di Prisco, G., Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei) (1997) J. Mol. Evol., 45, pp. 437-445
Rifkind, J.M., Abugo, O., Levy, A., Heim, J., Detection, formation, and relevance of hemichromes and hemochromes (1994) Methods Enzymol., 231, pp. 449-480
Rachmilewitz, E.A., Peisach, J., Blumberg, W.E., Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives (1971) J. Biol. Chem., 246, pp. 3356-3366
Hargrove, M.S., Brucker, E.A., Stec, B., Sarath, G., Arredondo-Peter, R., Klucas, R.V., Olson, J.S., Phillips Jr., G.N., Crystal structure of a nonsymbiotic plant hemoglobin (2000) Struct. Fold. Des., 8, pp. 1005-1014
Robinson, V.L., Smith, B.B., Arnone, A., A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin (2003) Biochemistry, 42, pp. 10113-10125
Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, M., Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity (2003) Structure, 11, pp. 1087-1095
Derewenda, Z., Dodson, G., Emsley, P., Harris, D., Nagai, K., Perutz, M., Renaud, J.P., Reynaud, J.P., Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins (1990) J. Mol. Biol., 211, pp. 515-519
Smalas, A.O., Leiros, H.K., Os, V., Willassen, N.P., Cold adapted enzymes (2000) Biotechnol. Annu. Rev., 6, pp. 1-57
Trent III, J.T., Watts, R.A., Hargrove, M.S., Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen (2001) J. Biol. Chem., 276, pp. 30106-30110
Hvitved, A.N., Trent III, J.T., Premer, S.A., Hargrove, M.S., Ligand binding and hexacoordination in synechocystis hemoglobin (2001) J. Biol. Chem., 276, pp. 34714-34721
Wittenberg, J.B., Bolognesi, M., Wittenberg, B.A., Guertin, M., Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants (2002) J. Biol. Chem., 277, pp. 871-874
Duff, S.M., Wittenberg, J.B., Hill, R.D., Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands (1997) J. Biol. Chem., 272, pp. 16746-16752
Svistunenko, D.A., Sharpe, M.A., Nicholls, P., Blenkinsop, C., Davies, N.A., Dunne, J., Wilson, M.T., Cooper, C.E., The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: An EPR study (2000) Biochem. J., 351, pp. 595-605
Graham, M.S., Fletcher, G.L., High concentrations of methemoglobin in five species of temperate marine teleosts (1986) J. Exp. Zool., 239, pp. 139-142
Royer Jr., W. E., Knapp, J. E., Strand, K., Heaslet, H. A., Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms (2001) Trends Biochem. Sci., 26, pp. 297-30
Ruud, J. T., Vertebrates without erythrocytes and blood pigment (1954) Nature (London), 173, pp. 848-850
Perutz, M. F., Nature of haem-haem interaction (1972) Nature (London), 237, pp. 495-499
Perez, J. E., Maclean, N., Multiple globins and haemoglobins in four species of grey mullet (Mugilidae, Teleosta) (1976) Comp. Biochem. Physiol. B, 53, pp. 465-468
Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. -S., Warren, G. L., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr., D54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr., A47, pp. 110-119
Schneider, T. R., Objective comparison of protein structures: Error-scaled difference distance matrices (2000) Acta Crystallogr., D56, pp. 714-721
Jensen, F. B., Comparative analysis of autoxidation of haemoglobin (2001) J. Exp. Biol., 204, pp. 2029-2033
Wilson Jr., R. R., Knowles, F. C., Temperature adaptation of fish hemoglobins reflected in rates of autoxidation (1987) Arch. Biochem. Biophys., 255, pp. 210-213
Perutz, M. F., Heidner, E. J., Ladner, J. E., Beetlestone, J. G., Ho, C., Slade, E. F., Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction (1974) Biochemistry, 13, pp. 2187-2200
Stam, W. T., Beintema, J. J., D'Avino, R., Tamburrini, M., Di Prisco, G., Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei) (1997) J. Mol. Evol., 45, pp. 437-445
Rifkind, J. M., Abugo, O., Levy, A., Heim, J., Detection, formation, and relevance of hemichromes and hemochromes (1994) Methods Enzymol., 231, pp. 449-480
Rachmilewitz, E. A., Peisach, J., Blumberg, W. E., Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives (1971) J. Biol. Chem., 246, pp. 3356-3366
Hargrove, M. S., Brucker, E. A., Stec, B., Sarath, G., Arredondo-Peter, R., Klucas, R. V., Olson, J. S., Phillips Jr., G. N., Crystal structure of a nonsymbiotic plant hemoglobin (2000) Struct. Fold. Des., 8, pp. 1005-1014
Robinson, V. L., Smith, B. B., Arnone, A., A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin (2003) Biochemistry, 42, pp. 10113-10125
Smalas, A. O., Leiros, H. K., Os, V., Willassen, N. P., Cold adapted enzymes (2000) Biotechnol. Annu. Rev., 6, pp. 1-57
Trent III, J. T., Watts, R. A., Hargrove, M. S., Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen (2001) J. Biol. Chem., 276, pp. 30106-30110
Hvitved, A. N., Trent III, J. T., Premer, S. A., Hargrove, M. S., Ligand binding and hexacoordination in synechocystis hemoglobin (2001) J. Biol. Chem., 276, pp. 34714-34721
Wittenberg, J. B., Bolognesi, M., Wittenberg, B. A., Guertin, M., Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants (2002) J. Biol. Chem., 277, pp. 871-874
Duff, S. M., Wittenberg, J. B., Hill, R. D., Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands (1997) J. Biol. Chem., 272, pp. 16746-16752
Svistunenko, D. A., Sharpe, M. A., Nicholls, P., Blenkinsop, C., Davies, N. A., Dunne, J., Wilson, M. T., Cooper, C. E., The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: An EPR study (2000) Biochem. J., 351, pp. 595-605
Graham, M. S., Fletcher, G. L., High concentrations of methemoglobin in five species of temperate marine teleosts (1986) J. Exp. Zool., 239, pp. 139-142
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 May; 271(9): 1651-1659.
Export to BibTeX Export to EndNote
Paper type: Erratum, Journal Article,
Impact factor: 3.26, 5-year impact factor: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2342503233&partnerID=40&md5=1566add68c835ad2a9652f9dddb6c301
Keywords: Antarctic Fish, Hemichrome, Hemoglobin, Hexa-Coordination, Oxidation, Alpha (aquomet) Beta (bishistidylhemichrome), Ferricyanide, Hemoglobin Derivative, Reducing Agent, Unclassified Drug, Alpha Chain, Article, Beta Chain, Controlled Study, Nonhuman, Priority Journal, Protein Structure, Ultraviolet Spectroscopy, Vertebrate, X Ray Crystallography, Animals, Antarctic Regions, Crystallization, Oxidation-Reduction, Quaternary, Tertiary, Spectrum Analysis, Notothenioidei, Pisces, Trematomus, Trematomus Bernacchii, Trematomus Newnesi, Erratum, Fishes Blood, Hemoglobins Chemistry,
Affiliations:
*** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, CNR, Napoli, Italy
Dipartimento di Chimica, Univ. Studi di Napoli 'Federico II', Complesso Univ. di M.S. Angelo, Napoli, Italy
Ist. di Biochimica delle Proteine, CNR, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy.,
References:
Royer Jr., W.E., Knapp, J.E., Strand, K., Heaslet, H.A., Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms (2001) Trends Biochem. Sci., 26, pp. 297-30
Di Prisco, G., Molecular adaptations of Antarctic fish haemoglobins (1998) Fishes of Antarctica: Biological Overview, pp. 339-353. , di Prisco G., Pisano E. & Clark A., eds, Springer, Milan
Di Prisco, G., D'Avino, R., Caruso, C., Tamburrini, M., Camardella, L., Rutigliano, B., Carratore, V., Romano, M., The biochemistry of oxygen transport in red-blooded Antarctic fish (1991) Biology of Antarctic Fish, pp. 263-281. , di Prisco, G., Maresca, B. & Tota, B., eds, Springer-Verlag, Milan
Ruud, J.T., Vertebrates without erythrocytes and blood pigment (1954) Nature (London), 173, pp. 848-850
Di Prisco, G., Macdonald, J.A., Brunori, M., Antarctic fishes survive exposure to carbon monoxide (1992) Experientia, 48, pp. 473-475
Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G., Perutz, M.F., Haemoglobin 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
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 Crystallogr., D57, pp. 1144-1146
Baldwin, J., Chothia, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) J. Mol. Biol., 129, pp. 175-220
Perutz, M.F., Nature of haem-haem interaction (1972) Nature (London), 237, pp. 495-499
Tamburrini, M., Brancaccio, A., Ippoliti, R., Di Prisco, G., The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps (1992) Arch. Biochem. Biophys., 292, pp. 295-302
Perez, J.E., Maclean, N., Multiple globins and haemoglobins in four species of grey mullet (Mugilidae, Teleosta) (1976) Comp. Biochem. Physiol. B, 53, pp. 465-468
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Mazzarella, L., Di D'Avino, R., Di Prisco, G., Savino, C., Vitagliano, L., Moody, P.C.E., Zagari, A., Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question (1999) J. Mol. Biol., 287, pp. 897-906
Navaza, J., AMoRe an automated package for molecular replacement (1994) Acta Crystallogr., A50, pp. 157-163
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.-S., Warren, G.L., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr., D54, pp. 905-921
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr., A47, pp. 110-119
Ito, N., Komiyama, N.H., Fermi, G., Structure of deoxyhaemoglobin of the antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the root effect by comparison of the liganded and unliganded haemoglobin structures (1995) J. Mol. Biol., 250, pp. 648-658
Schneider, T.R., Objective comparison of protein structures: Error-scaled difference distance matrices (2000) Acta Crystallogr., D56, pp. 714-721
Antonini, E., Brunori, M., (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, , North-Holland Publishers Co, Amsterdam
Feis, A., Marzocchi, M.P., Paoli, M., Smulevich, G., Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures (1994) Biochemistry, 33, pp. 4577-4583
Jensen, F.B., Comparative analysis of autoxidation of haemoglobin (2001) J. Exp. Biol., 204, pp. 2029-2033
Wilson Jr., R.R., Knowles, F.C., Temperature adaptation of fish hemoglobins reflected in rates of autoxidation (1987) Arch. Biochem. Biophys., 255, pp. 210-213
Perutz, M.F., Heidner, E.J., Ladner, J.E., Beetlestone, J.G., Ho, C., Slade, E.F., Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction (1974) Biochemistry, 13, pp. 2187-2200
Stam, W.T., Beintema, J.J., D'Avino, R., Tamburrini, M., Di Prisco, G., Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei) (1997) J. Mol. Evol., 45, pp. 437-445
Rifkind, J.M., Abugo, O., Levy, A., Heim, J., Detection, formation, and relevance of hemichromes and hemochromes (1994) Methods Enzymol., 231, pp. 449-480
Rachmilewitz, E.A., Peisach, J., Blumberg, W.E., Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives (1971) J. Biol. Chem., 246, pp. 3356-3366
Hargrove, M.S., Brucker, E.A., Stec, B., Sarath, G., Arredondo-Peter, R., Klucas, R.V., Olson, J.S., Phillips Jr., G.N., Crystal structure of a nonsymbiotic plant hemoglobin (2000) Struct. Fold. Des., 8, pp. 1005-1014
Robinson, V.L., Smith, B.B., Arnone, A., A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin (2003) Biochemistry, 42, pp. 10113-10125
Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, M., Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity (2003) Structure, 11, pp. 1087-1095
Derewenda, Z., Dodson, G., Emsley, P., Harris, D., Nagai, K., Perutz, M., Renaud, J.P., Reynaud, J.P., Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins (1990) J. Mol. Biol., 211, pp. 515-519
Smalas, A.O., Leiros, H.K., Os, V., Willassen, N.P., Cold adapted enzymes (2000) Biotechnol. Annu. Rev., 6, pp. 1-57
Trent III, J.T., Watts, R.A., Hargrove, M.S., Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen (2001) J. Biol. Chem., 276, pp. 30106-30110
Hvitved, A.N., Trent III, J.T., Premer, S.A., Hargrove, M.S., Ligand binding and hexacoordination in synechocystis hemoglobin (2001) J. Biol. Chem., 276, pp. 34714-34721
Wittenberg, J.B., Bolognesi, M., Wittenberg, B.A., Guertin, M., Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants (2002) J. Biol. Chem., 277, pp. 871-874
Duff, S.M., Wittenberg, J.B., Hill, R.D., Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands (1997) J. Biol. Chem., 272, pp. 16746-16752
Svistunenko, D.A., Sharpe, M.A., Nicholls, P., Blenkinsop, C., Davies, N.A., Dunne, J., Wilson, M.T., Cooper, C.E., The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: An EPR study (2000) Biochem. J., 351, pp. 595-605
Graham, M.S., Fletcher, G.L., High concentrations of methemoglobin in five species of temperate marine teleosts (1986) J. Exp. Zool., 239, pp. 139-142
Royer Jr., W. E., Knapp, J. E., Strand, K., Heaslet, H. A., Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms (2001) Trends Biochem. Sci., 26, pp. 297-30
Ruud, J. T., Vertebrates without erythrocytes and blood pigment (1954) Nature (London), 173, pp. 848-850
Perutz, M. F., Nature of haem-haem interaction (1972) Nature (London), 237, pp. 495-499
Perez, J. E., Maclean, N., Multiple globins and haemoglobins in four species of grey mullet (Mugilidae, Teleosta) (1976) Comp. Biochem. Physiol. B, 53, pp. 465-468
Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. -S., Warren, G. L., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr., D54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr., A47, pp. 110-119
Schneider, T. R., Objective comparison of protein structures: Error-scaled difference distance matrices (2000) Acta Crystallogr., D56, pp. 714-721
Jensen, F. B., Comparative analysis of autoxidation of haemoglobin (2001) J. Exp. Biol., 204, pp. 2029-2033
Wilson Jr., R. R., Knowles, F. C., Temperature adaptation of fish hemoglobins reflected in rates of autoxidation (1987) Arch. Biochem. Biophys., 255, pp. 210-213
Perutz, M. F., Heidner, E. J., Ladner, J. E., Beetlestone, J. G., Ho, C., Slade, E. F., Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction (1974) Biochemistry, 13, pp. 2187-2200
Stam, W. T., Beintema, J. J., D'Avino, R., Tamburrini, M., Di Prisco, G., Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei) (1997) J. Mol. Evol., 45, pp. 437-445
Rifkind, J. M., Abugo, O., Levy, A., Heim, J., Detection, formation, and relevance of hemichromes and hemochromes (1994) Methods Enzymol., 231, pp. 449-480
Rachmilewitz, E. A., Peisach, J., Blumberg, W. E., Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives (1971) J. Biol. Chem., 246, pp. 3356-3366
Hargrove, M. S., Brucker, E. A., Stec, B., Sarath, G., Arredondo-Peter, R., Klucas, R. V., Olson, J. S., Phillips Jr., G. N., Crystal structure of a nonsymbiotic plant hemoglobin (2000) Struct. Fold. Des., 8, pp. 1005-1014
Robinson, V. L., Smith, B. B., Arnone, A., A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin (2003) Biochemistry, 42, pp. 10113-10125
Smalas, A. O., Leiros, H. K., Os, V., Willassen, N. P., Cold adapted enzymes (2000) Biotechnol. Annu. Rev., 6, pp. 1-57
Trent III, J. T., Watts, R. A., Hargrove, M. S., Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen (2001) J. Biol. Chem., 276, pp. 30106-30110
Hvitved, A. N., Trent III, J. T., Premer, S. A., Hargrove, M. S., Ligand binding and hexacoordination in synechocystis hemoglobin (2001) J. Biol. Chem., 276, pp. 34714-34721
Wittenberg, J. B., Bolognesi, M., Wittenberg, B. A., Guertin, M., Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants (2002) J. Biol. Chem., 277, pp. 871-874
Duff, S. M., Wittenberg, J. B., Hill, R. D., Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands (1997) J. Biol. Chem., 272, pp. 16746-16752
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The oxidation process of Antarctic fish hemoglobins
Analysis of the molecular properties of proteins extracted from organisms living under extreme conditions often highlights peculiar features. We investigated by UV-visible spectroscopy and X-ray crystallography the oxidation process, promoted by air or ferricyanide, of five hemoglobins extracted from Antarctic fishes (Notothenioidei). Spectroscopic analysis revealed that these hemoglobins share a common oxidation pathway, which shows striking differences from the oxidation processes of hemoglobins from other vertebrates. Indeed, simple exposure of these hemoglobins to air leads to the formation of a significant amount of the low-spin hexacoordinated form, denoted hemichrome. This hemichrome form, which is detected under a variety of experimental conditions, can be reversibly transformed to either carbomonoxy or deoxygenated forms with reducing agents. Interestingly, the spectra of the fully oxidized species, obtained by treating the protein with ferricyanide, show the simultaneous presence of peaks corresponding to different hexacoordinated states, the aquomet and the hemichrome. In order to assign the heme region state of the alpha and beta chains, the air-oxidized and ferricyanide-oxidized forms of Trematomus bernacchii hemoglobin were crystallized. Crystallographic analysis revealed that these forms correspond to an alpha(aquomet)-beta(bishistidyl-hemichrome) state. This demonstrates that the alpha and beta chains of Antarctic fish hemoglobins follow very different oxidation pathways. As found for Trematomus newnesi hemoglobin in a partial hemichrome state [Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A. & Mazzarella, L. (2002) Proc. Natl Acad. Sci. USA99, 9801-9806], the quaternary structures of these alpha(aquomet)-beta(bishistidyl-hemichrome) forms are intermediate between the physiological R and T hemoglobin states. Together, these structures provide information on the general features of this intermediate state.
Analysis of the molecular properties of proteins extracted from organisms living under extreme conditions often highlights peculiar features. We investigated by UV-visible spectroscopy and X-ray crystallography the oxidation process, promoted by air or ferricyanide, of five hemoglobins extracted from Antarctic fishes (Notothenioidei). Spectroscopic analysis revealed that these hemoglobins share a common oxidation pathway, which shows striking differences from the oxidation processes of hemoglobins from other vertebrates. Indeed, simple exposure of these hemoglobins to air leads to the formation of a significant amount of the low-spin hexacoordinated form, denoted hemichrome. This hemichrome form, which is detected under a variety of experimental conditions, can be reversibly transformed to either carbomonoxy or deoxygenated forms with reducing agents. Interestingly, the spectra of the fully oxidized species, obtained by treating the protein with ferricyanide, show the simultaneous presence of peaks corresponding to different hexacoordinated states, the aquomet and the hemichrome. In order to assign the heme region state of the alpha and beta chains, the air-oxidized and ferricyanide-oxidized forms of Trematomus bernacchii hemoglobin were crystallized. Crystallographic analysis revealed that these forms correspond to an alpha(aquomet)-beta(bishistidyl-hemichrome) state. This demonstrates that the alpha and beta chains of Antarctic fish hemoglobins follow very different oxidation pathways. As found for Trematomus newnesi hemoglobin in a partial hemichrome state [Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A. & Mazzarella, L. (2002) Proc. Natl Acad. Sci. USA99, 9801-9806], the quaternary structures of these alpha(aquomet)-beta(bishistidyl-hemichrome) forms are intermediate between the physiological R and T hemoglobin states. Together, these structures provide information on the general features of this intermediate state.
The oxidation process of Antarctic fish hemoglobins
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The oxidation process of Antarctic fish hemoglobins
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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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Pacelli R, Taira J, Cook JA, Wink DA, Krishna MC
Hydroxyurea reacts with heme proteins to generate nitric oxide [6] (334 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
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Bonomo RP, De Flora A, Rizzarelli E, Santoro AM, Tabbì G, Tonetti M
Copper(II) complexes encapsulated in human red blood cells (587 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Sep; 59(4): 773-784.
Impact Factor: 1.342
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Manna R, Salvatore M, Di Leo MA, Scuderi F, Greco AV, Ghirlanda G, Gambassi G
Relationship between urinary neopterin excretion and islet cell antibodies in type 1 (insulin-dependent) diabetes (432 views)
Diabetes Res (ISSN: 0265-5985), 1991 May; 17(1): 33-36.
Impact Factor: 0
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Salvati AM, d'Onofrio G, Berti P, Cappabianca MP, Marsili G, De Philippis C, Cossa L, Quarantelli M, Zini G, Mango G
An assessment of the operating characteristics of Coulter Counter model S-Plus STKR (585 views)
Haematologica (ISSN: 0390-6078, 0006-4971, 0006-6497), 1991 Mar; 76(2): 94-103.
Impact Factor: 2.56
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* The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus (176 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2019 Dec 12; 9(1): 18987-18987.
Impact Factor: 5.078
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Mazzarella L, Merlino A, Balasco N, Balsamo A, Vergara A
* Crystal structure of the ferric homotetrameric beta4 human hemoglobin (238 views)
Biophys Chem (ISSN: 0301-4622linking), 2018 Sep; 240: 9-14.
Impact Factor: 1.87
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Vitagliano L, Mazzarella L, Merlino A, Vergara A
* Fine Sampling of the R--> T Quaternary-Structure Transition of a Tetrameric Hemoglobin (332 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2017 Jan 12; 23(3): 605-613.
Impact Factor: 5.16
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Caviglia GP, Cabianca L, Fagoonee S, Gili FM
* Colorectal cancer detection in an asymptomatic population: Fecal immunochemical test for hemoglobin vs. Fecal M2-type pyruvate kinase (329 views)
Biochem Medica (ISSN: 1330-0962), 2016; 26(1): 114-120.
Impact Factor: 2.934
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Bisconte MG, Caldora M, Musollino G, Cardiero G, Flagiello A, La Porta G, Lagona L, Prezioso R, Qualtieri G, Gaudiano C, Medulla E, Merlino A, Pucci P, Lacerra G
* α-thalassemia associated with Hb instability: A tale of two features. The case of Hb Rogliano or α1 Cod 108(G15)Thr→Asn and Hb Policoro or α2 Cod 124(H7)Ser→Pro (420 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2015; 10(3): N/D-N/D.
Impact Factor: 3.057
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Mazzarella L, Merlino A, Vitagliano L, Verde C, Di Prisco G, Peisach J, Vergara A
* Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin (287 views)
Rsc Adv (ISSN: 2046-2069), 2014; 4(49): 25852-25856.
Impact Factor: 3.84
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Alcides Petruk A, Vergara A, Estrin D, Merlino A
* Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study (393 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013 Sep 2; 587(15): 2393-2398.
Impact Factor: 3.341
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Paolillo S, Rengo G, Pagano G, Pellegrino T, Savarese G, Femminella GD, Tuccillo M, Boemio A, Attena E, Formisano R, Petraglia L, Scopacasa F, Galasso G, Leosco D, Trimarco B, Cuocolo A, Perrone-Filardi P
* Impact of diabetes on cardiac sympathetic innervation in patients with heart failure: a 123I meta-iodobenzylguanidine (123I MIBG) scintigraphic study (313 views)
Diabetes Care (ISSN: 1935-5548, 0149-5992), 2013 Sep; 36(8): 2395-2401.
Impact Factor: 8.57
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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 (511 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Sep; 1834(9): 1885-1893.
Impact Factor: 3.191
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Merlino A, Fuchs MR, Pica A, Balsamo A, Dworkowski FSN, Pompidor G, Mazzarella L, Vergara A
* Selective X-ray-induced NO photodissociation in haemoglobin crystals: evidence from a Raman-assisted crystallographic study (339 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jan; 69: 137-140.
Impact Factor: 7.232
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Merlino A, Fuchs MR, Pica A, Balsamo A, Dworkowski FSN, Pompidor G, Mazzarella L, Vergara A
* Selective X-Ray Induced No-Photodissociation In Hemoglobin Crystals: Evidence From A Raman Assisted-Crystallographic Study (302 views)
Acta Cryst D 69, 2013; 1: 137-140.
Impact Factor: 0
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Fonti R, Larobina M, Del Vecchio S, Fabbricini R, Catalano L, Pane F, Salvatore M, Pace L
* Metabolic tumor volume assessed by 18F-FDG PET/CT for the prediction of outcome in patients with multiple myeloma (583 views)
J Nucl Med (ISSN: 1535-5667, 0161-5505, 1535-5667electronic), 2012 Dec; 53(12): 1829-1835.
Impact Factor: 5.774
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Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
* ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus (343 views)
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Impact Factor: 3.35
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Risitano AM, Imbriaco M, Marando L, Seneca E, Soscia E, Malcovati L, Iori AP, Pane F, Notaro R, Matarazzo M
* From perpetual haemosiderinuria to possible iron overload: iron redistribution in paroxysmal nocturnal haemoglobinuria patients on eculizumab by magnetic resonance imaging (359 views)
Br J Haematol (ISSN: 0007-1048, 0007-1048linking, 1365-2141electronic), 2012 Sep; 158(3): 415-418.
Impact Factor: 4.942
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De Rosa A, Rossi F, Lieto M, Bruno R, De Renzo A, Palma V, Quarantelli M, De Michele G
* Subacute combined degeneration of the spinal cord in a vegan (355 views)
Clin Neurol Neurosurg (ISSN: 0303-8467), 2012 Sep; 114(7): 1000-1002.
Impact Factor: 1.234
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Marciano C, Galderisi M, Gargiulo P, Acampa W, D'Amore C, Esposito R, Capasso E, Savarese G, Casaretti L, Lo Iudice F, Esposito G, Rengo G, Leosco D, Cuocolo A, Perrone-Filardi P
* Effects of type 2 diabetes mellitus on coronary microvascular function and myocardial perfusion in patients without obstructive coronary artery disease (738 views)
Eur J Nucl Med (ISSN: 1619-7070, 1619-7089, 0340-6997), 2012 Jul; 39(7): 1199-1206.
Impact Factor: 5.114
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Balsamo A, Sannino F, Merlino A, Parrilli E, Tutino ML, Mazzarella L, Vergara A
* Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins (407 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2012 Apr; 94(4): 953-960.
Impact Factor: 3.142
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Striano P, Caranci F, Pappata S, Zara F, Striano S
* Hemidystonia in uncontrolled type 2 diabetes mellitus (275 views)
Arch Neurol (ISSN: 1538-3687electronic, 0003-9942linking), 2011 May; 68(5): 674-675.
Impact Factor: 7.584
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Merlino A, Howes BD, Prisco G, Verde C, Smulevich G, Mazzarella L, Vergara A
* Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins (410 views)
Iubmb Life (ISSN: 1521-6543, 1521-6551), 2011 May; 63(5): 295-303.
Impact Factor: 3.514
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Riccio A, Mangiapia G, Giordano D, Flagiello A, Tedesco R, Bruno S, Vergara A, Mazzarella L, di Prisco G, Pucci P, Paduano L, Verde C
* Polymerization of Hemoglobins in Arctic Fish: Lycodes reticulatus and Gadus morhua (361 views)
Iubmb Life (ISSN: 1521-6543, 1521-6551), 2011 May; 63(5): 346-354.
Impact Factor: 3.514
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Boechi L, Marti MA, Vergara A, Sica F, Mazzarella L, Estrin DA, Merlino A
* Protonation of Histidine 55 Affects the Oxygen Access to Heme in the Alpha Chain of the Hemoglobin from the Antarctic Fish Trematomus bernacchii (370 views)
Iubmb Life (ISSN: 1521-6543, 1521-6551), 2011 Mar; 63(3): 175-182.
Impact Factor: 3.514
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Bozzetto L, Prinster A, Mancini M, Giacco R, De Natale C, Salvatore M, Riccardi G, Rivellese AA, Annuzzi G
* Liver fat in obesity: role of type 2 diabetes mellitus and adipose tissue distribution (418 views)
Eur J Clin Invest (ISSN: 0014-2972, 1365-2362, 0014-2972linking), 2011 Jan; 41(1): 39-44.
Impact Factor: 3.018
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Merlino A, Vitagliano L, Balsamo A, Nicoletti FP, Howes BD, Giordano D, Coppola D, Di Prisco G, Verde C, Smulevich G, Mazzarella L, Vergara A
* Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major haemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form (317 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2010 Nov; 66: 1536-1540.
Impact Factor: 0.563
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Vergara A, Vitagliano L, Merlino A, Sica F, Marino K, Verde C, di Prisco G, Mazzarella L
* An Order-Disorder Transition Plays a Role in Switching Off the Root Effect in Fish Hemoglobins (363 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2010 Oct 15; 285(42): 32568-32575.
Impact Factor: 5.328
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Coppola D, Giordano D, Vergara A, Mazzarella L, Di Prisco G, Verde C, Russo R
* The hemoglobins of sub-Antarctic fishes of the suborder Notothenioidei (404 views)
Polar Science (ISSN: 1873-9652), 2010 Sep; 4(2): 295-308.
Impact Factor: 31.477
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Mainenti PP, Segreto S, Mancini M, Rispo A, Cozzolino I, Masone S, Rinaldi CR, Nardone G, Salvatore M
* Intestinal amyloidosis: two cases with different patterns of clinical and imaging presentation (386 views)
World J Gastroentero (ISSN: 2219-2840, 1007-9327, 1007-9327linking), 2010 May 28; 16(20): 2566-2570.
Impact Factor: 2.24
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Merlino A, Vergara A, Sica F, Aschi M, Amadei A, Di Nola A, Mazzarella L
* Free-Energy Profile for CO Binding to Separated Chains of Human and Trematomus newnesi Hemoglobin: Insights from Molecular Dynamics Simulations and Perturbed Matrix Method (301 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 May 27; 114(20): 7002-7008.
Impact Factor: 3.603
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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)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
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Risitano AM, Seneca E, Marando L, Imbriaco M, Soscia E, Soscia F, Pizzuti LM, Malcovati L, Fenu S, Iori AP, Notaro R, Matarazzo M, Rotoli B
* From Renal Siderosis Due to Perpetual Hemosiderinuria to Possible Liver Overload Due to Extravascular Hemolysis: Changes in Iron Metabolism in Paroxysmal Nocturnal Hemoglobinuria (PNH) Patients On Eculizumab (353 views)
Haematologica (ISSN: 0006-4971, 0006-6497, 0390-6078), 2009 Nov 20; 114(22): N/D-N/D.
Impact Factor: 10.555
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Cigliano L, Pugliese CR, Spagnuolo MS, Palumbo R, Abrescia P
* Haptoglobin binds the antiatherogenic protein apolipoprotein e - Impairment of apolipoprotein e stimulation of both lecithin: Cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (396 views)
Febs J (ISSN: 1742-464x), 2009 Nov; 276(21): 6158-6171.
Impact Factor: 3.042
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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
* Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins (405 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2009 Sep 5; 97(3): 866-874.
Impact Factor: 4.39
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Giordano D, Boechi L, Vergara A, Marti MA, Samuni U, Dantsker D, Grassi L, Estrin DA, Friedman JM, Mazzarella L, Di Prisco G, Verde C
* The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - oxygen-binding equilibria, kinetics and molecular dynamics (708 views)
Febs Journal (ISSN: 1742-464x), 2009 Apr; 276(8): 2266-2277.
Impact Factor: 3.042
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Verde C, Giordano D, Russo R, Riccio A, Vergara A, Mazzarella L, Di Prisco G
* Hemoproteins in the cold (275 views)
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 67-73.
Impact Factor: 1.2
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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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Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (962 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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Vitagliano L, Vergara A, Bonomi G, Merlino A, Verde C, Di Prisco G, Howes BD, Smulevich G, Mazzarella L
* Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (400 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
Impact Factor: 8.091
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Cigliano L, Maresca B, Salvatore A, Nino M, Monfrecola G, Ayala F, Carlucci A, Pugliese RC, Pedone C, Abrescia P
* Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity (401 views)
Journal Of The European Academy Of Dermatology And Venereology (ISSN: 1468-3083, 0926-9959), 2008 Apr; 22(4): 417-425.
Impact Factor: 2.276
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Merlino A, Verde C, Di Prisco G, Mazzarella L, Vergara A
* Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (382 views)
Spectroscopy An International Journal (ISSN: 0712-4813), 2008; 22(2-3): 143-152.
Impact Factor: 0.82
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Vitagliano L, Vergara A, Bonomi G, Merlino A, Verde C, Di Prisco G, Howes BD, Smulevich G, Mazzarella L
* Spectroscopic And Crystallographic Characterization Of A Tetrameric Hemoglobin Oxidation Pathway Reveals Structural Features Of A Functional Intermediate R/T State (278 views)
Biophys J, 2008; 94: 4031-4040.
Impact Factor: 3.832
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Vergara A, Vitagliano L, Verde C, di Prisco G, Mazzarella L
* Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins (426 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic), 2008; 436: 425-444.
Impact Factor: 2.312
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Vergara A, Vitagliano L, Di Prisco G, Verde C, Mazzarella L
* Spectroscopic And Crystallographic Characterization Of Hemichromes In Tetrameric Hemoglobins (321 views)
Methods In Enzymology, 2008; 436: 421-440.
Impact Factor: 2.194
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Giordano D, Vergara A, Lee HC, Peisach J, Balestrieri M, Mazzarella L, Parisi E, Di Priseo G, Verde C
* Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus (389 views)
Gene (ISSN: 0378-1119), 2007 Dec 30; 406(1-2): 58-68.
Impact Factor: 2.871
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Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (407 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
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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 (753 views)
Nature Reviews Neuroscience (ISSN: 1471-0048), 2007 Oct; 8(10): 766-775.
Impact Factor: 24.52
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Vergara A, Franzese M, Merlino A, Vitagliano L, Verde C, Di Prisco G, Lee HC, Peisach J, Mazzarella L
* Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder notothenioidei (375 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2007 Oct; 93(8): 2822-2829.
Impact Factor: 4.627
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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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Mazzarella L, Bonomi G, Lubrano MC, Merlino A, Riccio A, Vergara A, Vitagliano L, Verde C, Di Prisco G
* 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.
Impact Factor: 3.73
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Spagnuolo MS, Cigliano L, D'Andrea LD, Pedone C, Abrescia P
* Assignment of the binding site for haptoglobin on apolipoprotein A-I (479 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Jan 14; 280(2): 1193-1198.
Impact Factor: 5.854
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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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Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (378 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
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Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (521 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2002 Jul 23; 99(15): 9801-9806.
Impact Factor: 10.7
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Tedesco I, Russo GL, Nazzaro F, Russo M, Palumbo R
* Antioxidant effect of red wine anthocyanins in normal and catalase-inactive human erythrocytes (897 views)
J Nutr Biochem (ISSN: 0955-2863), 2001 Sep; 12(9): 505-511.
Impact Factor: 1.039
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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 (392 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Sep; 57: 1144-1146.
Impact Factor: 2.124
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Tedesco I, Russo M, Russo P, Iacomino G, Russo GL, Carraturo A, Faruolo C, Moio L, Palumbo R
Antioxidant effect of red wine polyphenols on red blood cells (564 views)
J Nutr Biochem (ISSN: 0955-2863), 2000 Feb; 11(2): 114-119.
Impact Factor: 1.083
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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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Pacelli R, Taira J, Cook JA, Wink DA, Krishna MC
Hydroxyurea reacts with heme proteins to generate nitric oxide [6] (334 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
View Export to BibTeX Export to EndNote
Bonomo RP, De Flora A, Rizzarelli E, Santoro AM, Tabbì G, Tonetti M
Copper(II) complexes encapsulated in human red blood cells (587 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Sep; 59(4): 773-784.
Impact Factor: 1.342
View Export to BibTeX Export to EndNote
Manna R, Salvatore M, Di Leo MA, Scuderi F, Greco AV, Ghirlanda G, Gambassi G
Relationship between urinary neopterin excretion and islet cell antibodies in type 1 (insulin-dependent) diabetes (432 views)
Diabetes Res (ISSN: 0265-5985), 1991 May; 17(1): 33-36.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Salvati AM, d'Onofrio G, Berti P, Cappabianca MP, Marsili G, De Philippis C, Cossa L, Quarantelli M, Zini G, Mango G
An assessment of the operating characteristics of Coulter Counter model S-Plus STKR (585 views)
Haematologica (ISSN: 0390-6078, 0006-4971, 0006-6497), 1991 Mar; 76(2): 94-103.
Impact Factor: 2.56
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60 Records (56 excluding Abstracts).
Total impact factor: 278.35 (243.817 excluding Abstracts).
Total 5 year impact factor: 328.029 (270.289 excluding Abstracts).
Total impact factor: 278.35 (243.817 excluding Abstracts).
Total 5 year impact factor: 328.029 (270.289 excluding Abstracts).
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