The Root effect - a structural and evolutionary perspective (251 views)
Antarctic Science (ISSN: 0954-1020), 2007 Jun; 19(2): 271-278.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.265, 5-year impact factor: 1.683
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-34249044116&partnerID=40&md5=fa6ef6d89dd1c3b7dafd1fa7bb692c57
Keywords: Antarctica, Evolution, Fish, Haemoglobin, Ph-Regulation, Structure, Amphibian, Chemical Property, Teleost, Trematomus Newnesi, Vertebrata,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia, I-80126, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy
References:
BALDWIN, J., CHOTHIA, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) Journal of Molecular Biology, 129, pp. 175-22
BERENBRINK, M., KOLDKJÆR, 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
BRITTAIN, T., Root effect hemoglobins (2005) Journal of Inorganic Biochemistry, 99, pp. 120-129
BRUNORI, M., BOSSA, F., BONAVENTURA, C., GIARDINA, B., ANTONINI, E., Hemoglobins from trout: Structural and functional properties (1973) Molecular and Cellular Biochemistry, 1, pp. 189-196
BONAVENTURA, J., GILLEN, R.G., RIGGS, A., The hemoglobin of the Crosspterygian fish, Latimeria chalumnae (Smith) (1974) Archives of Biochemistry and Biophysics, 163, pp. 728-734
BONAVENTURA, C., SULLIVAN, B., BONAVENTURA, J., BRUNORI, M., Spot hemoglobin. Studies on the Root effect hemoglobin of a marine teleost (1976) Journal of Biological Chemistry, 251, pp. 1871-1876
CAMARDELLA, L., CARUSO, C., D'AVINO, R., DI PRISCO, G., RUTIGLIANO, B., TAMBURRINI, M., FERMI, G. & PERUTZ, M. F. 1992. Haemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. Journal of Molecular Biology, 224, 449-460D'AVINO, R., CARUSO, C., TAMBURRINI, M., ROMANO, M., RUTIGLIANO, B., POLVERINO DE LAURETO, P., CAMARDELLA, L., CARRATORE, V. & DI PRISCO, G. 1994. Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. Journal of Biological Chemistry, 269, 9675-9681DETTAÏ, A., LECOINTRE, G., In search for notothenioid (Teleostei) relatives (2004) Antarctic Science, 16, pp. 71-85
EASTMAN, J.T., Aspects of the morphology of phyletically basal bovichtid fishes of the Antarctic suborder Notothenioidei (Perciformes) (2006) Polar Biology, 29, pp. 754-763
FAGO, A., BENDIXEN, E., MALTE, H., WEBER, R.E., The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a Root effect haemoglobin (1997) Journal of Biological Chemistry, 272, pp. 15628-15635
GERVASIO, F.L., PROCACCI, P., CARDINI, G., GUARNA, A., GIOLITTI, A., SCHETTINO, V., Interaction between aromatic residues. Molecular dynamics and ab initio exploration of the potential energy surface of the tryptophan-histidine pair (2000) Journal of Physical Chemistry, B104, pp. 1108-1114
HARATA, K., MURAKI, M., JIGAMI, Y., Role of Arg115 in the catalytic action of human lysozyme. X ray structure of His115 and Glu115 mutants (1993) Journal of Molecular Biology, 233, pp. 524-535
HUBER, F., BRAUNITZER, G., The primary structure of electric ray haemoglobin (Torpedo marmorata). Bohr effect and phosphate interaction (1989) Biological Chemistry Hoppe-Seyler, 370, pp. 831-838
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) Journal of Molecular Biology, 250, pp. 648-658
KENDREW, J.C., BODO, G., DINTZIS, H.M., PARRISH, R.G., WYCKOFF, H., PHILLIPS, D.C., A three-dimensional model of the myoglobin molecule obtained by X-ray analysis (1958) Nature, 181, pp. 662-666
MAZZARELLA, L., D'AVINO, R., DI PRISCO, G., SAVINO, C., VITAGLIANO, L., MOODY, C.E. & ZAGARI, A. 1999. Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question. Journal of Molecular Biology, 287, 897-906MAZZARELLA, L., BONOMI, G., LUBRANO, M., MERLINO, A., RICCIO, A., VERGARA, A., VITAGLIANO, L., DI PRISCO, G., Minimal structural requirements for Root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi (2006) Proteins, 62, pp. 316-321
MAZZARELLA, L., VERGARA, A., VITAGLIANO, L., MERLINO, A., BONOMI, G., SCALA, S., VERDE, C., DI PRISCO, G., High-resolution crystal structure of deoxy haemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the Root effect (2006) Proteins, 65, pp. 490-498
MONOD, J., WYMAN, J., CHANGEUX, J.P., On the nature of allosteric transitions: A plausible model (1965) Journal of Molecular Biology, 12, pp. 88-118
MORRIS, R.J., NEKAMEYER, W.S., GIBSON, Q.H., Multiple T-state conformations in a fish hemoglobin. Carbon monoxide binding to hemoglobin of Thunnus thynnus (1981) Journal of Biological Chemistry, 256, pp. 4596-4603
MYLVAGANAM, S.E., BONAVENTURA, C., BONAVENTURA, J., GETZOFF, E.D., Structural basis for the Root effect in haemoglobin (1996) Nature Structural Biology, 3, pp. 275-283
NOBLE, R.W., KWIATKOWSKI, L.D., DE YOUNG, A., DAVIS, B.J., HAEDRICH, R.L., TAM, L.T., RIGGS, A.F., Functional properties of hemoglobins from deep-sea fish: Correlations with depth distribution and presence of a swimbladder (1986) Biochimica and Biophysica Acta, 870, pp. 552-563
NOBLE, R.W., PARKHURST, L.J., GIBSON, Q.H., The effect of pH on the reactions of oxygen and carbon monoxide with the hemoglobin of the carp (1970) Cyprinus carpio. Journal of Biological Chemistry, 245, pp. 6628-6633
PAOLI, M., LIDDINGTON, R., TAME, J., WILKINSON, A., DODSON, G., Crystal structure of T-state haemoglobin with oxygen bound at all four haems (1996) Journal of Molecular Biology, 256, pp. 775-792
PELSTER, B., Buoyancy at depth (1997) Deep-sea fish, pp. 195-237. , RANDALL, D. & FARRELL, A.P, eds, San Diego, CA: Academic Press
PERUTZ, M.F., Species adaptation in a protein molecule (1983) Molecular Biology and Evolution, 1, pp. 1-28
PERUTZ, M.F., BRUNORI, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature, 229, pp. 421-442
PERUTZ, M.F., KENDREW, J.C., WATSON, H.C., Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence (1965) Journal of Molecular Biology, 13, pp. 669-678
PERUTZ, M.F., FERMI, G., LUISI, B., SHANAN, B., LIDDINGTON, R.C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Accounts of Chemical Research, 20, pp. 309-321
RIGGS, A., The Bohr effect (1988) Annual Review of Physiology, 50, pp. 181-204
RUUD, J.T., Vertebrates without erythrocytes and blood pigment (1954) Nature, 173, pp. 848-850
SAMUNI, U., DANTSKER, D., JUSZCZAK, L.J., BETTATI, S., RONDA, L., MOZZARELLI, A., FRIEDMAN, J.M., Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels (2004) Biochemistry, 43, pp. 13 674-13 682
SAMUNI, U., ROCHE, C.J., DANTSKER, D., JUSZCZAK, L.J., FRIEDMAN, J.M., Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: The combined use of mutagenesis and sol-gel encapsulation (2006) Biochemistry, 45, pp. 2820-2835
TAME, J.R.H., WILSON, J.C. & WEBER, R.E. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. 1996. Journal of Molecular Biology, 259, 749-760VERDE, C., DE ROSA, M.C., GIORDANO, D., MOSCA, D., DE PASCALE, D., RAIOLA, L., COCCA, E., DI PRISCO, G., Structure, function and molecular adaptations of haemoglobins of the polar cartilaginous fish Bathyraja eatonii and Raja hyperborea (2005) Biochemical Journal, 389, pp. 297-306
WITTENBERG, J.B., HAEDRICH, R.L., The choroid rete mirabile of the fish eye. II. Distribution and relation to the pseudobranch and to the swimbladder rete mirabile (1974) Biological Bulletin, 146, pp. 137-156
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) Journal of Biological Chemistry, 279, pp. 28632-28640
YONETANI, T., PARK, S., TSUNESHIGE, A., IMAI, K., KANAORI, K., Global allostery model of hemoglobin (2002) Journal of Biological Chemistry, 277, pp. 34 508-34 520
EASTMAN, J. T., Aspects of the morphology of phyletically basal bovichtid fishes of the Antarctic suborder Notothenioidei (Perciformes) (2006) Polar Biology, 29, pp. 754-763
GERVASIO, F. L., PROCACCI, P., CARDINI, G., GUARNA, A., GIOLITTI, A., SCHETTINO, V., Interaction between aromatic residues. Molecular dynamics and ab initio exploration of the potential energy surface of the tryptophan-histidine pair (2000) Journal of Physical Chemistry, B104, pp. 1108-1114
KENDREW, J. C., BODO, G., DINTZIS, H. M., PARRISH, R. G., WYCKOFF, H., PHILLIPS, D. C., A three-dimensional model of the myoglobin molecule obtained by X-ray analysis (1958) Nature, 181, pp. 662-666
MORRIS, R. J., NEKAMEYER, W. S., GIBSON, Q. H., Multiple T-state conformations in a fish hemoglobin. Carbon monoxide binding to hemoglobin of Thunnus thynnus (1981) Journal of Biological Chemistry, 256, pp. 4596-4603
MYLVAGANAM, S. E., BONAVENTURA, C., BONAVENTURA, J., GETZOFF, E. D., Structural basis for the Root effect in haemoglobin (1996) Nature Structural Biology, 3, pp. 275-283
NOBLE, R. W., KWIATKOWSKI, L. D., DE YOUNG, A., DAVIS, B. J., HAEDRICH, R. L., TAM, L. T., RIGGS, A. F., Functional properties of hemoglobins from deep-sea fish: Correlations with depth distribution and presence of a swimbladder (1986) Biochimica and Biophysica Acta, 870, pp. 552-563
NOBLE, R. W., PARKHURST, L. J., GIBSON, Q. H., The effect of pH on the reactions of oxygen and carbon monoxide with the hemoglobin of the carp (1970) Cyprinus carpio. Journal of Biological Chemistry, 245, pp. 6628-6633
PERUTZ, M. F., Species adaptation in a protein molecule (1983) Molecular Biology and Evolution, 1, pp. 1-28
PERUTZ, M. F., BRUNORI, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature, 229, pp. 421-442
PERUTZ, M. F., KENDREW, J. C., WATSON, H. C., Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence (1965) Journal of Molecular Biology, 13, pp. 669-678
PERUTZ, M. F., FERMI, G., LUISI, B., SHANAN, B., LIDDINGTON, R. C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Accounts of Chemical Research, 20, pp. 309-321
RUUD, J. T., Vertebrates without erythrocytes and blood pigment (1954) Nature, 173, pp. 848-850
TAME, J. R. H., WILSON, J. C. & WEBER, R. E. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. 1996. Journal of Molecular Biology, 259, 749-760VERDE, C., DE ROSA, M. C., GIORDANO, D., MOSCA, D., DE PASCALE, D., RAIOLA, L., COCCA, E., DI PRISCO, G., Structure, function and molecular adaptations of haemoglobins of the polar cartilaginous fish Bathyraja eatonii and Raja hyperborea (2005) Biochemical Journal, 389, pp. 297-306
WITTENBERG, J. B., HAEDRICH, R. L., The choroid rete mirabile of the fish eye. II. Distribution and relation to the pseudobranch and to the swimbladder rete mirabile (1974) Biological Bulletin, 146, pp. 137-156
Antarctic Science (ISSN: 0954-1020), 2007 Jun; 19(2): 271-278.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.265, 5-year impact factor: 1.683
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-34249044116&partnerID=40&md5=fa6ef6d89dd1c3b7dafd1fa7bb692c57
Keywords: Antarctica, Evolution, Fish, Haemoglobin, Ph-Regulation, Structure, Amphibian, Chemical Property, Teleost, Trematomus Newnesi, Vertebrata,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia, I-80126, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy
References:
BALDWIN, J., CHOTHIA, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) Journal of Molecular Biology, 129, pp. 175-22
BERENBRINK, M., KOLDKJÆR, 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
BRITTAIN, T., Root effect hemoglobins (2005) Journal of Inorganic Biochemistry, 99, pp. 120-129
BRUNORI, M., BOSSA, F., BONAVENTURA, C., GIARDINA, B., ANTONINI, E., Hemoglobins from trout: Structural and functional properties (1973) Molecular and Cellular Biochemistry, 1, pp. 189-196
BONAVENTURA, J., GILLEN, R.G., RIGGS, A., The hemoglobin of the Crosspterygian fish, Latimeria chalumnae (Smith) (1974) Archives of Biochemistry and Biophysics, 163, pp. 728-734
BONAVENTURA, C., SULLIVAN, B., BONAVENTURA, J., BRUNORI, M., Spot hemoglobin. Studies on the Root effect hemoglobin of a marine teleost (1976) Journal of Biological Chemistry, 251, pp. 1871-1876
CAMARDELLA, L., CARUSO, C., D'AVINO, R., DI PRISCO, G., RUTIGLIANO, B., TAMBURRINI, M., FERMI, G. & PERUTZ, M. F. 1992. Haemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. Journal of Molecular Biology, 224, 449-460D'AVINO, R., CARUSO, C., TAMBURRINI, M., ROMANO, M., RUTIGLIANO, B., POLVERINO DE LAURETO, P., CAMARDELLA, L., CARRATORE, V. & DI PRISCO, G. 1994. Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. Journal of Biological Chemistry, 269, 9675-9681DETTAÏ, A., LECOINTRE, G., In search for notothenioid (Teleostei) relatives (2004) Antarctic Science, 16, pp. 71-85
EASTMAN, J.T., Aspects of the morphology of phyletically basal bovichtid fishes of the Antarctic suborder Notothenioidei (Perciformes) (2006) Polar Biology, 29, pp. 754-763
FAGO, A., BENDIXEN, E., MALTE, H., WEBER, R.E., The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a Root effect haemoglobin (1997) Journal of Biological Chemistry, 272, pp. 15628-15635
GERVASIO, F.L., PROCACCI, P., CARDINI, G., GUARNA, A., GIOLITTI, A., SCHETTINO, V., Interaction between aromatic residues. Molecular dynamics and ab initio exploration of the potential energy surface of the tryptophan-histidine pair (2000) Journal of Physical Chemistry, B104, pp. 1108-1114
HARATA, K., MURAKI, M., JIGAMI, Y., Role of Arg115 in the catalytic action of human lysozyme. X ray structure of His115 and Glu115 mutants (1993) Journal of Molecular Biology, 233, pp. 524-535
HUBER, F., BRAUNITZER, G., The primary structure of electric ray haemoglobin (Torpedo marmorata). Bohr effect and phosphate interaction (1989) Biological Chemistry Hoppe-Seyler, 370, pp. 831-838
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) Journal of Molecular Biology, 250, pp. 648-658
KENDREW, J.C., BODO, G., DINTZIS, H.M., PARRISH, R.G., WYCKOFF, H., PHILLIPS, D.C., A three-dimensional model of the myoglobin molecule obtained by X-ray analysis (1958) Nature, 181, pp. 662-666
MAZZARELLA, L., D'AVINO, R., DI PRISCO, G., SAVINO, C., VITAGLIANO, L., MOODY, C.E. & ZAGARI, A. 1999. Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question. Journal of Molecular Biology, 287, 897-906MAZZARELLA, L., BONOMI, G., LUBRANO, M., MERLINO, A., RICCIO, A., VERGARA, A., VITAGLIANO, L., DI PRISCO, G., Minimal structural requirements for Root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi (2006) Proteins, 62, pp. 316-321
MAZZARELLA, L., VERGARA, A., VITAGLIANO, L., MERLINO, A., BONOMI, G., SCALA, S., VERDE, C., DI PRISCO, G., High-resolution crystal structure of deoxy haemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the Root effect (2006) Proteins, 65, pp. 490-498
MONOD, J., WYMAN, J., CHANGEUX, J.P., On the nature of allosteric transitions: A plausible model (1965) Journal of Molecular Biology, 12, pp. 88-118
MORRIS, R.J., NEKAMEYER, W.S., GIBSON, Q.H., Multiple T-state conformations in a fish hemoglobin. Carbon monoxide binding to hemoglobin of Thunnus thynnus (1981) Journal of Biological Chemistry, 256, pp. 4596-4603
MYLVAGANAM, S.E., BONAVENTURA, C., BONAVENTURA, J., GETZOFF, E.D., Structural basis for the Root effect in haemoglobin (1996) Nature Structural Biology, 3, pp. 275-283
NOBLE, R.W., KWIATKOWSKI, L.D., DE YOUNG, A., DAVIS, B.J., HAEDRICH, R.L., TAM, L.T., RIGGS, A.F., Functional properties of hemoglobins from deep-sea fish: Correlations with depth distribution and presence of a swimbladder (1986) Biochimica and Biophysica Acta, 870, pp. 552-563
NOBLE, R.W., PARKHURST, L.J., GIBSON, Q.H., The effect of pH on the reactions of oxygen and carbon monoxide with the hemoglobin of the carp (1970) Cyprinus carpio. Journal of Biological Chemistry, 245, pp. 6628-6633
PAOLI, M., LIDDINGTON, R., TAME, J., WILKINSON, A., DODSON, G., Crystal structure of T-state haemoglobin with oxygen bound at all four haems (1996) Journal of Molecular Biology, 256, pp. 775-792
PELSTER, B., Buoyancy at depth (1997) Deep-sea fish, pp. 195-237. , RANDALL, D. & FARRELL, A.P, eds, San Diego, CA: Academic Press
PERUTZ, M.F., Species adaptation in a protein molecule (1983) Molecular Biology and Evolution, 1, pp. 1-28
PERUTZ, M.F., BRUNORI, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature, 229, pp. 421-442
PERUTZ, M.F., KENDREW, J.C., WATSON, H.C., Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence (1965) Journal of Molecular Biology, 13, pp. 669-678
PERUTZ, M.F., FERMI, G., LUISI, B., SHANAN, B., LIDDINGTON, R.C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Accounts of Chemical Research, 20, pp. 309-321
RIGGS, A., The Bohr effect (1988) Annual Review of Physiology, 50, pp. 181-204
RUUD, J.T., Vertebrates without erythrocytes and blood pigment (1954) Nature, 173, pp. 848-850
SAMUNI, U., DANTSKER, D., JUSZCZAK, L.J., BETTATI, S., RONDA, L., MOZZARELLI, A., FRIEDMAN, J.M., Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels (2004) Biochemistry, 43, pp. 13 674-13 682
SAMUNI, U., ROCHE, C.J., DANTSKER, D., JUSZCZAK, L.J., FRIEDMAN, J.M., Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: The combined use of mutagenesis and sol-gel encapsulation (2006) Biochemistry, 45, pp. 2820-2835
TAME, J.R.H., WILSON, J.C. & WEBER, R.E. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. 1996. Journal of Molecular Biology, 259, 749-760VERDE, C., DE ROSA, M.C., GIORDANO, D., MOSCA, D., DE PASCALE, D., RAIOLA, L., COCCA, E., DI PRISCO, G., Structure, function and molecular adaptations of haemoglobins of the polar cartilaginous fish Bathyraja eatonii and Raja hyperborea (2005) Biochemical Journal, 389, pp. 297-306
WITTENBERG, J.B., HAEDRICH, R.L., The choroid rete mirabile of the fish eye. II. Distribution and relation to the pseudobranch and to the swimbladder rete mirabile (1974) Biological Bulletin, 146, pp. 137-156
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) Journal of Biological Chemistry, 279, pp. 28632-28640
YONETANI, T., PARK, S., TSUNESHIGE, A., IMAI, K., KANAORI, K., Global allostery model of hemoglobin (2002) Journal of Biological Chemistry, 277, pp. 34 508-34 520
EASTMAN, J. T., Aspects of the morphology of phyletically basal bovichtid fishes of the Antarctic suborder Notothenioidei (Perciformes) (2006) Polar Biology, 29, pp. 754-763
GERVASIO, F. L., PROCACCI, P., CARDINI, G., GUARNA, A., GIOLITTI, A., SCHETTINO, V., Interaction between aromatic residues. Molecular dynamics and ab initio exploration of the potential energy surface of the tryptophan-histidine pair (2000) Journal of Physical Chemistry, B104, pp. 1108-1114
KENDREW, J. C., BODO, G., DINTZIS, H. M., PARRISH, R. G., WYCKOFF, H., PHILLIPS, D. C., A three-dimensional model of the myoglobin molecule obtained by X-ray analysis (1958) Nature, 181, pp. 662-666
MORRIS, R. J., NEKAMEYER, W. S., GIBSON, Q. H., Multiple T-state conformations in a fish hemoglobin. Carbon monoxide binding to hemoglobin of Thunnus thynnus (1981) Journal of Biological Chemistry, 256, pp. 4596-4603
MYLVAGANAM, S. E., BONAVENTURA, C., BONAVENTURA, J., GETZOFF, E. D., Structural basis for the Root effect in haemoglobin (1996) Nature Structural Biology, 3, pp. 275-283
NOBLE, R. W., KWIATKOWSKI, L. D., DE YOUNG, A., DAVIS, B. J., HAEDRICH, R. L., TAM, L. T., RIGGS, A. F., Functional properties of hemoglobins from deep-sea fish: Correlations with depth distribution and presence of a swimbladder (1986) Biochimica and Biophysica Acta, 870, pp. 552-563
NOBLE, R. W., PARKHURST, L. J., GIBSON, Q. H., The effect of pH on the reactions of oxygen and carbon monoxide with the hemoglobin of the carp (1970) Cyprinus carpio. Journal of Biological Chemistry, 245, pp. 6628-6633
PERUTZ, M. F., Species adaptation in a protein molecule (1983) Molecular Biology and Evolution, 1, pp. 1-28
PERUTZ, M. F., BRUNORI, M., Stereochemistry of cooperative effects in fish and amphibian hemoglobins (1982) Nature, 229, pp. 421-442
PERUTZ, M. F., KENDREW, J. C., WATSON, H. C., Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence (1965) Journal of Molecular Biology, 13, pp. 669-678
PERUTZ, M. F., FERMI, G., LUISI, B., SHANAN, B., LIDDINGTON, R. C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Accounts of Chemical Research, 20, pp. 309-321
RUUD, J. T., Vertebrates without erythrocytes and blood pigment (1954) Nature, 173, pp. 848-850
TAME, J. R. H., WILSON, J. C. & WEBER, R. E. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. 1996. Journal of Molecular Biology, 259, 749-760VERDE, C., DE ROSA, M. C., GIORDANO, D., MOSCA, D., DE PASCALE, D., RAIOLA, L., COCCA, E., DI PRISCO, G., Structure, function and molecular adaptations of haemoglobins of the polar cartilaginous fish Bathyraja eatonii and Raja hyperborea (2005) Biochemical Journal, 389, pp. 297-306
WITTENBERG, J. B., HAEDRICH, R. L., The choroid rete mirabile of the fish eye. II. Distribution and relation to the pseudobranch and to the swimbladder rete mirabile (1974) Biological Bulletin, 146, pp. 137-156
The Root effect - a structural and evolutionary perspective
Haemoglobin carries oxygen from the environment to tissues; in vertebrates, it is contained in specialized cells, called erythrocytes. Over the last century, the study of the chemical properties of this haernoprotein has provided a wealth of information. One of its most important and ancient physiological features is the Root effect, found in many teleost fish (and some amphibians). The Root effect corresponds to an extreme pH sensitivity and can be described as an exaggerated Bohr effect: it dictates to what extent the oxygen tension can be raised in acid-producing tissues. It is likely that the eye choroid rete represents the most ancient anatomical structure associated with the presence of Root effect haemoglobins. This review describes our overall understanding of the molecular properties, biological occurrence, physiological role and evolutionary origin of Root effect haemoglobins. The current knowledge of the structural properties of Root effect haemoglobins is discussed in the light of recent results obtained on the haemoglobins of the cold-adapted notothenioids Trematomus newnesi and T. bernacchii.
Haemoglobin carries oxygen from the environment to tissues; in vertebrates, it is contained in specialized cells, called erythrocytes. Over the last century, the study of the chemical properties of this haernoprotein has provided a wealth of information. One of its most important and ancient physiological features is the Root effect, found in many teleost fish (and some amphibians). The Root effect corresponds to an extreme pH sensitivity and can be described as an exaggerated Bohr effect: it dictates to what extent the oxygen tension can be raised in acid-producing tissues. It is likely that the eye choroid rete represents the most ancient anatomical structure associated with the presence of Root effect haemoglobins. This review describes our overall understanding of the molecular properties, biological occurrence, physiological role and evolutionary origin of Root effect haemoglobins. The current knowledge of the structural properties of Root effect haemoglobins is discussed in the light of recent results obtained on the haemoglobins of the cold-adapted notothenioids Trematomus newnesi and T. bernacchii.
The Root effect - a structural and evolutionary perspective
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The Root effect - a structural and evolutionary perspective
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Merlino A, Vergara A, Vitagliano L
* Comments on Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1. 9 angstrom resolution by P. Ramesh et al. (2013). J. Synchrotron Rad. 20, 843-847 (282 views)
J Synchrotron Radiat (ISSN: 0909-0495), 2014 Jul; 21: N/D-N/D.
Impact Factor: 2.794
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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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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 (544 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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (360 views)
Br J Haematol (ISSN: 0007-1048, 0007-1048linking, 1365-2141electronic), 2012 Sep; 158(3): 415-418.
Impact Factor: 4.942
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (543 views)
J Struct Biol (ISSN: 1047-8477, 1047-8477linking), 2010 Dec; 172(3): 343-352.
Impact Factor: 3.5
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (434 views)
Polar Science (ISSN: 1873-9652), 2010 Sep; 4(2): 295-308.
Impact Factor: 31.477
View Export to BibTeX Export to EndNote
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 (416 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
View Export to BibTeX Export to EndNote
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 (407 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2009 Sep 5; 97(3): 866-874.
Impact Factor: 4.39
View Export to BibTeX Export to EndNote
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 (709 views)
Febs Journal (ISSN: 1742-464x), 2009 Apr; 276(8): 2266-2277.
Impact Factor: 3.042
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (417 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
View Export to BibTeX Export to EndNote
Vergara A, Verde C, Di Prisco G, Mazzarella L
* Bis-histidyl Ferric Adducts in Tetrameric Haemoglobins (187 views)
Protein Reviews, 2008; 9: N/D-N/D.
Impact Factor: 0
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (507 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 1; 62(2): 316-321.
Impact Factor: 3.73
View Export to BibTeX Export to EndNote
Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L
* The oxidation process of Antarctic fish hemoglobins (454 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 May; 271(9): 1651-1659.
Impact Factor: 3.26
View Export to BibTeX Export to EndNote
Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (553 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2002 Jul 23; 99(15): 9801-9806.
Impact Factor: 10.7
View Export to BibTeX Export to EndNote
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 (401 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Sep; 57: 1144-1146.
Impact Factor: 2.124
View Export to BibTeX Export to EndNote
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 (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Apr 16; 287(5): 897-906.
Impact Factor: 5.501
View Export to BibTeX Export to EndNote
* Comments on Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1. 9 angstrom resolution by P. Ramesh et al. (2013). J. Synchrotron Rad. 20, 843-847 (282 views)
J Synchrotron Radiat (ISSN: 0909-0495), 2014 Jul; 21: N/D-N/D.
Impact Factor: 2.794
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
Ronda L, Merlino A, Bettati S, Verde C, Balsamo A, Mazzarella L, Mozzarelli A, Vergara A
* Role of tertiary structures on the Root effect in fish hemoglobins (544 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Sep; 1834(9): 1885-1893.
Impact Factor: 3.191
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (360 views)
Br J Haematol (ISSN: 0007-1048, 0007-1048linking, 1365-2141electronic), 2012 Sep; 158(3): 415-418.
Impact Factor: 4.942
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (543 views)
J Struct Biol (ISSN: 1047-8477, 1047-8477linking), 2010 Dec; 172(3): 343-352.
Impact Factor: 3.5
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (434 views)
Polar Science (ISSN: 1873-9652), 2010 Sep; 4(2): 295-308.
Impact Factor: 31.477
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Howes BD, Verde C, Di Prisco G, Smulevich G, Sica F, Vergara A
* Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins (416 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
View Export to BibTeX Export to EndNote
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 (407 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2009 Sep 5; 97(3): 866-874.
Impact Factor: 4.39
View Export to BibTeX Export to EndNote
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 (709 views)
Febs Journal (ISSN: 1742-464x), 2009 Apr; 276(8): 2266-2277.
Impact Factor: 3.042
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (417 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
View Export to BibTeX Export to EndNote
Vergara A, Verde C, Di Prisco G, Mazzarella L
* Bis-histidyl Ferric Adducts in Tetrameric Haemoglobins (187 views)
Protein Reviews, 2008; 9: N/D-N/D.
Impact Factor: 0
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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
View Export to BibTeX Export to EndNote
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 (507 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 1; 62(2): 316-321.
Impact Factor: 3.73
View Export to BibTeX Export to EndNote
Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L
* The oxidation process of Antarctic fish hemoglobins (454 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 May; 271(9): 1651-1659.
Impact Factor: 3.26
View Export to BibTeX Export to EndNote
Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (553 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2002 Jul 23; 99(15): 9801-9806.
Impact Factor: 10.7
View Export to BibTeX Export to EndNote
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 (401 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Sep; 57: 1144-1146.
Impact Factor: 2.124
View Export to BibTeX Export to EndNote
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 (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Apr 16; 287(5): 897-906.
Impact Factor: 5.501
View Export to BibTeX Export to EndNote
26 Records (24 excluding Abstracts).
Total impact factor: 129.003 (126.209 excluding Abstracts).
Total 5 year impact factor: 144.295 (141.628 excluding Abstracts).
Total impact factor: 129.003 (126.209 excluding Abstracts).
Total 5 year impact factor: 144.295 (141.628 excluding Abstracts).
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