메뉴 건너뛰기




Volumn 282, Issue 1-2, 1998, Pages 120-126

Evolution of cooperativity in hemoglobins: What can invertebrate hemoglobins tell us?

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; ARENICOLA; BIVALVIA; CAUDINA ARENICOLA; ECHINODERMATA; INVERTEBRATA; SCAPHARCA; VERTEBRATA;

EID: 3542999857     PISSN: 0022104X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-010x(199809/10)282:1/2<120::aid-jez13>3.0.co;2-y     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0020694467 scopus 로고
    • The seal myoglobin gene: An unusually long globin gene
    • Blanchetot, A., V. Wilson, D. Wood, and A.J. Jeffreys (1983) The seal myoglobin gene: An unusually long globin gene. Nature, 301:732-734.
    • (1983) Nature , vol.301 , pp. 732-734
    • Blanchetot, A.1    Wilson, V.2    Wood, D.3    Jeffreys, A.J.4
  • 2
    • 0017138003 scopus 로고
    • Functional consequences of ligand-linked dissociation in hemoglobin from the sea cucumber Molpadia arenicola
    • Bonaventura, C., J. Bonaventura, G.B. Kitto, M. Brunori, and E. Antonini (1976) Functional consequences of ligand-linked dissociation in hemoglobin from the sea cucumber Molpadia arenicola. Biochim. Biophys. Acta, 428:779-786.
    • (1976) Biochim. Biophys. Acta , vol.428 , pp. 779-786
    • Bonaventura, C.1    Bonaventura, J.2    Kitto, G.B.3    Brunori, M.4    Antonini, E.5
  • 3
    • 0018787005 scopus 로고
    • Preliminary crystallographic data on monomeric and dimeric hemoglobins from the sea cucumber Molpadia arenicola
    • Carson, W.M., T.R. Bowers, G.B. Kitto, and M.L. Hackert (1979) Preliminary crystallographic data on monomeric and dimeric hemoglobins from the sea cucumber Molpadia arenicola. J. Biol. Chem., 254:7400-7402.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7400-7402
    • Carson, W.M.1    Bowers, T.R.2    Kitto, G.B.3    Hackert, M.L.4
  • 4
    • 84970609705 scopus 로고
    • Amino acid sequence of the α-chain of the tetrameric haemoglobin of the bivalve mollusc Anadara trapezia
    • Como, P.F., and E.O.P. Thompson (1980) Amino acid sequence of the α-chain of the tetrameric haemoglobin of the bivalve mollusc Anadara trapezia. Austra. J. Biol. Sci., 33:653-664.
    • (1980) Austra. J. Biol. Sci. , vol.33 , pp. 653-664
    • Como, P.F.1    Thompson, E.O.P.2
  • 7
    • 0010717714 scopus 로고
    • Evolution of globin gene families
    • R.K. Selander, A.G. Clark, and T.S. Whitman, eds. Sinauer, Sunderland, MA
    • Hardison, R.C. (1991) Evolution of globin gene families. In: Evolution at the Molecular Level. R.K. Selander, A.G. Clark, and T.S. Whitman, eds. Sinauer, Sunderland, MA, pp. 272-290.
    • (1991) Evolution at the Molecular Level , pp. 272-290
    • Hardison, R.C.1
  • 8
    • 0020530850 scopus 로고
    • Transcription terminates in yeast distal to a control sequence
    • Henikoff, S., J.D. Kelly, and E.H. Cohen (1983) Transcription terminates in yeast distal to a control sequence. Cell, 33:607-614.
    • (1983) Cell , vol.33 , pp. 607-614
    • Henikoff, S.1    Kelly, J.D.2    Cohen, E.H.3
  • 9
    • 0024971745 scopus 로고
    • The structure of the gene encoding chain c of the hemoglobin of the earthworm, Lumbricus terrestris
    • Jhiang, S.M., and A.F. Riggs (1989) The structure of the gene encoding chain c of the hemoglobin of the earthworm, Lumbricus terrestris. J. Biol. Chem., 264:19003-19008.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19003-19008
    • Jhiang, S.M.1    Riggs, A.F.2
  • 10
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis
    • Joshi, C.P. (1987) Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis. Nucleic Acids Res., 15:9627-9640.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 9627-9640
    • Joshi, C.P.1
  • 11
    • 0017121395 scopus 로고
    • N-terminal substitution of some sea cucumber hemoglobins
    • Kitto, G.B., D. Erwin, R. West, and J. Omnaas (1976) N-terminal substitution of some sea cucumber hemoglobins. Comp. Biochem. Physiol., 55B:105-107.
    • (1976) Comp. Biochem. Physiol. , vol.55 B , pp. 105-107
    • Kitto, G.B.1    Erwin, D.2    West, R.3    Omnaas, J.4
  • 14
    • 0028353744 scopus 로고
    • Structural analysis of Urechis caupo hemoglobin
    • Kolatkar, P.R., M.L. Hackert, and A.F. Riggs (1994) Structural analysis of Urechis caupo hemoglobin. J. Mol. Biol., 237:87-97.
    • (1994) J. Mol. Biol. , vol.237 , pp. 87-97
    • Kolatkar, P.R.1    Hackert, M.L.2    Riggs, A.F.3
  • 15
    • 0014962912 scopus 로고
    • The amino acid sequence of hemoglobin V from the lamprey, Petromyzon marinus
    • Li, S.L., and A. Riggs (1970) The amino acid sequence of hemoglobin V from the lamprey, Petromyzon marinus. J. Biol. Chem., 245:6149-6169.
    • (1970) J. Biol. Chem. , vol.245 , pp. 6149-6169
    • Li, S.L.1    Riggs, A.2
  • 17
    • 0025764014 scopus 로고
    • Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola
    • Mauri, F., J. Omnaas, L. Davidson, C. Whitfill, and G.B. Kitto (1991) Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola. Biochim. Biophys. Acta, 1078:63-67.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 63-67
    • Mauri, F.1    Omnaas, J.2    Davidson, L.3    Whitfill, C.4    Kitto, G.B.5
  • 19
    • 0025298218 scopus 로고
    • Glycosylation of invertebrate hemoglobins
    • McDonald, G.D., and G.B. Kitto (1990) Glycosylation of invertebrate hemoglobins. Comp. Biochem. Physiol., 96B:235-237.
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 235-237
    • McDonald, G.D.1    Kitto, G.B.2
  • 20
    • 0026582235 scopus 로고
    • Amino acid sequence of the coelomic C globin from the sea cucumber Caudina (Molpadia) arenicola
    • McDonald, G.D., L. Davidson, and G.B. Kitto (1992) Amino acid sequence of the coelomic C globin from the sea cucumber Caudina (Molpadia) arenicola. J. Protein Chem., 11:29-37.
    • (1992) J. Protein Chem. , vol.11 , pp. 29-37
    • McDonald, G.D.1    Davidson, L.2    Kitto, G.B.3
  • 21
    • 0028813887 scopus 로고
    • Three-dimensional structure of a hemichrome hemoglobin from Caudina arenicola
    • Mitchell, D.T., S.R. Ernst, W.-X. Wu, and M.L. Hackert (1995a) Three-dimensional structure of a hemichrome hemoglobin from Caudina arenicola. Acta Crystallogr., D51:641-653.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 641-653
    • Mitchell, D.T.1    Ernst, S.R.2    Wu, W.-X.3    Hackert, M.L.4
  • 22
    • 0029146246 scopus 로고
    • Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola
    • Mitchell, D.T., G.B. Kitto, and M.L. Hackert (1995b) Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola. J. Mol. Biol., 251:421-431.
    • (1995) J. Mol. Biol. , vol.251 , pp. 421-431
    • Mitchell, D.T.1    Kitto, G.B.2    Hackert, M.L.3
  • 23
    • 0028852589 scopus 로고
    • X-ray structure determination of a dimeric hemoglobin from Caudina arenicola
    • Mitchell, D.T., S.R. Ernst, and M.L. Hackert (1995c) X-ray structure determination of a dimeric hemoglobin from Caudina arenicola. Acta Crystallogr., D51:760-766.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 760-766
    • Mitchell, D.T.1    Ernst, S.R.2    Hackert, M.L.3
  • 25
    • 0016937963 scopus 로고
    • Haemoglobins of the shark, Heterodontus portusjacksoni. II. Amino acid sequence of the α-chain
    • Nash, A., W. Fisher, and E.O.P. Thompson (1976) Haemoglobins of the shark, Heterodontus portusjacksoni. II. Amino acid sequence of the α-chain. Aust. J. Biol. Sci., 29:73-97.
    • (1976) Aust. J. Biol. Sci. , vol.29 , pp. 73-97
    • Nash, A.1    Fisher, W.2    Thompson, E.O.P.3
  • 28
    • 0024854847 scopus 로고
    • The 2.4 Å crystal structure of Scapharca dimeric hemoglobin
    • Royer, W.E. Jr., W.A. Hendrickson, and E. Chiancone (1989) The 2.4 Å crystal structure of Scapharca dimeric hemoglobin. J. Biol. Chem., 264:21052-21061.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21052-21061
    • Royer Jr., W.E.1    Hendrickson, W.A.2    Chiancone, E.3
  • 29
    • 0028009317 scopus 로고
    • High resolution crystallographic analysis of a co-operative dimeric hemoglobin
    • Royer, W.E. Jr. (1994) High resolution crystallographic analysis of a co-operative dimeric hemoglobin. J. Mol. Biol., 235:657-681.
    • (1994) J. Mol. Biol. , vol.235 , pp. 657-681
    • Royer Jr., W.E.1
  • 30
    • 0024974111 scopus 로고
    • Amino acid sequences of a major globin from the sea cucumber Paracaudina chilensis
    • Suzuki, T. (1989a) Amino acid sequences of a major globin from the sea cucumber Paracaudina chilensis. Biochim. Biophys. Acta, 998:292-296.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 292-296
    • Suzuki, T.1
  • 31
    • 0024975146 scopus 로고
    • Amino acid sequence of the monomer subunit of the giant multisubunit hemoglobin from the earthworm Pheretima sieboldi
    • Suzuki, T. (1989b) Amino acid sequence of the monomer subunit of the giant multisubunit hemoglobin from the earthworm Pheretima sieboldi. Eur. J. Biochem., 185:127-134.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 127-134
    • Suzuki, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.