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Volumn 11, Issue 4, 1998, Pages 277-295

Classification and evolution of EF-hand proteins

Author keywords

Aequorin; BM 40; Calbindin; Calcineurin; Calmodulin; Calpain; Chimera; Classification; Congruence; Dendrogram; Diacylglycerol; Domain; Ef hand; Eukaryote; Evolution; Gene duplication; Gene fusion; Homology; Light chain of myosin; Parvalbumin; Phospholipase C; Recoverin; S100; Sorcin; Troponin C

Indexed keywords

CALBINDIN; CALCIUM BINDING PROTEIN; CALMODULIN; IMMUNOGLOBULIN LIGHT CHAIN; PROTEIN S 100; TROPONIN C;

EID: 0032454584     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1009282307967     Document Type: Article
Times cited : (314)

References (75)
  • 1
    • 0002367729 scopus 로고    scopus 로고
    • MOLPHY Version 2.3: Programs for molecular phylogenetics based on maximum likelihood
    • Institute of Statistical Mathematics, Tokyo
    • Adachi J, Hasegawa M. 1996 MOLPHY Version 2.3: Programs for molecular phylogenetics based on maximum likelihood. Computer Science Monographs, 28, 1-150. Institute of Statistical Mathematics, Tokyo.
    • (1996) Computer Science Monographs , vol.28 , pp. 1-150
    • Adachi, J.1    Hasegawa, M.2
  • 2
    • 0027446396 scopus 로고
    • The calmodulin-ubiquitin associated genes of Trypanosoma cruzi: Their identification and transcription
    • Ajioka J, Swindle J. 1993 The calmodulin-ubiquitin associated genes of Trypanosoma cruzi: their identification and transcription. Mol. Biochem. Parasitol. 57, 127-136.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 127-136
    • Ajioka, J.1    Swindle, J.2
  • 4
    • 0028922345 scopus 로고
    • Amino-terminal myristoylation induces cooperative calcium binding to recoverin
    • Ames JB, Porumb T, Tanaka T, Ikura M, Stryer L. 1995 Amino-terminal myristoylation induces cooperative calcium binding to recoverin. J. Biol. Chem. 270, 4526-4533.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4526-4533
    • Ames, J.B.1    Porumb, T.2    Tanaka, T.3    Ikura, M.4    Stryer, L.5
  • 6
    • 0027622908 scopus 로고
    • Arabidopsis thaliana cDNA encoding a novel member of the EF-Hand superfamily of calcium-binding proteins
    • Bartling D, Bülter H, Weiler EW. 1993 Arabidopsis thaliana cDNA encoding a novel member of the EF-Hand superfamily of calcium-binding proteins. Plant Physiol. 102, 1059-1060.
    • (1993) Plant Physiol. , vol.102 , pp. 1059-1060
    • Bartling, D.1    Bülter, H.2    Weiler, E.W.3
  • 8
    • 0027285585 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. V. The genes encoding EF-hand proteins are not clustered in mammalian genomes
    • Berchtold MW. 1993 Evolution of EF-hand calcium-modulated proteins. V. The genes encoding EF-hand proteins are not clustered in mammalian genomes. J. Mol. Evol. 36, 489-496.
    • (1993) J. Mol. Evol. , vol.36 , pp. 489-496
    • Berchtold, M.W.1
  • 9
    • 0028198960 scopus 로고
    • Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole body
    • Biggins S, Ros, MD. 1994 Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole body. J. Cell Biol. 125, 843-852.
    • (1994) J. Cell Biol. , vol.125 , pp. 843-852
    • Biggins, S.1    Ros, M.D.2
  • 11
    • 0028232768 scopus 로고
    • Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence of EF-hand calcium-binding domains
    • Brown LJ, MacDonald MJ, Lehn DA, Moran SM. 1994 Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence of EF-hand calcium-binding domains. J. Biol. Chem. 269, 14363-14366.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14363-14366
    • Brown, L.J.1    MacDonald, M.J.2    Lehn, D.A.3    Moran, S.M.4
  • 12
    • 0030875859 scopus 로고    scopus 로고
    • Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII)
    • Brownawell AM, Creutz CE. 1997 Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII). J. Biol. Chem. 272, 22182-22190.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22182-22190
    • Brownawell, A.M.1    Creutz, C.E.2
  • 13
    • 0013577468 scopus 로고    scopus 로고
    • Structural aspects of calcium-binding proteins of the EF-hand type
    • this issue
    • Chazin WJ. 1998 Structural aspects of calcium-binding proteins of the EF-hand type. BioMetals this issue.
    • (1998) BioMetals
    • Chazin, W.J.1
  • 14
    • 0027122748 scopus 로고
    • One thousand families for the molecular biologist
    • Chothia C. 1992 One thousand families for the molecular biologist. Nature 357, 543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 15
    • 0026056925 scopus 로고
    • Three-dimensional structure of a sarcoplasmic calcium-binding protein from Nereis divesicolor
    • Cook WJ, Ealik SE, Babu YS, Cox JA, Vijay Kumar S. 1991 Three-dimensional structure of a sarcoplasmic calcium-binding protein from Nereis divesicolor. J. Biol. Chem. 266, 652-656.
    • (1991) J. Biol. Chem. , vol.266 , pp. 652-656
    • Cook, W.J.1    Ealik, S.E.2    Babu, Y.S.3    Cox, J.A.4    Vijay Kumar, S.5
  • 16
    • 0027463062 scopus 로고
    • Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution
    • Cook WJ, Jeffrey LC, Cox JA, Vijay Kumar S. 1993 Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution. J. Mol. Biol. 229, 461-471.
    • (1993) J. Mol. Biol. , vol.229 , pp. 461-471
    • Cook, W.J.1    Jeffrey, L.C.2    Cox, J.A.3    Vijay Kumar, S.4
  • 17
    • 0025039011 scopus 로고
    • Comparative molecular modeling of Amphioxus calcium vector protein with calmodulin and troponin C
    • Cox JA, Alard P, Schaad O. 1990 Comparative molecular modeling of Amphioxus calcium vector protein with calmodulin and troponin C. Prot. Engineering 4, 23-32.
    • (1990) Prot. Engineering , vol.4 , pp. 23-32
    • Cox, J.A.1    Alard, P.2    Schaad, O.3
  • 18
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A, Ikura M. 1995 Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 19
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelatin proteins
    • de Arruda MV, Watson S, Lin C-S, Leavitt J, Matsudaira P. 1990 Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelatin proteins. J. Cell Biol. 111, 1069-1079.
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • De Arruda, M.V.1    Watson, S.2    Lin, C.-S.3    Leavitt, J.4    Matsudaira, P.5
  • 20
    • 0024235163 scopus 로고
    • Repetitive nucleotide sequence insertions into a novel calmodulin-related gene and its processed pseudogene
    • Deka N, Wong E, Matera AG, Kraft R, Leinwand LA, Schmid CW. 1988 Repetitive nucleotide sequence insertions into a novel calmodulin-related gene and its processed pseudogene. Gene 71, 123-134.
    • (1988) Gene , vol.71 , pp. 123-134
    • Deka, N.1    Wong, E.2    Matera, A.G.3    Kraft, R.4    Leinwand, L.A.5    Schmid, C.W.6
  • 21
    • 0028948501 scopus 로고
    • Human S100b protein: Formation of a tetramer from synthetic calcium-binding site peptides
    • Donaldson C, Barber KR, Kay CM, Shaw GS. 1995 Human S100b protein: Formation of a tetramer from synthetic calcium-binding site peptides. Protein Sci. 4, 765-772.
    • (1995) Protein Sci. , vol.4 , pp. 765-772
    • Donaldson, C.1    Barber, K.R.2    Kay, C.M.3    Shaw, G.S.4
  • 23
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide specific phospholipase Cδ
    • Essen L-O, Perisic O, Cheung R, Katan M, Williams RL. 1996 Crystal structure of a mammalian phosphoinositide specific phospholipase Cδ. Nature 380, 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 24
    • 0029643789 scopus 로고
    • The evolving model of calmodulin structure, function and activation
    • Finn BE, Forsén S. 1995 The evolving model of calmodulin structure, function and activation. Structure 3, 7-11.
    • (1995) Structure , vol.3 , pp. 7-11
    • Finn, B.E.1    Forsén, S.2
  • 25
    • 0027429963 scopus 로고
    • Three dimensional structure of recoverin, a calcium sensor in vision
    • Flaherty KM, Zozulys S, Stryer L, McKay DB. 1993 Three dimensional structure of recoverin, a calcium sensor in vision. Cell 75, 709-716.
    • (1993) Cell , vol.75 , pp. 709-716
    • Flaherty, K.M.1    Zozulys, S.2    Stryer, L.3    McKay, D.B.4
  • 26
    • 0027573380 scopus 로고
    • Identification of a cDNA clone coding for a novel calcium-binding protein from potato tuber
    • Gellatly KS, Lefebvre DD 1993 Identification of a cDNA clone coding for a novel calcium-binding protein from potato tuber. Plant Physiol. 101, 1405-1406.
    • (1993) Plant Physiol. , vol.101 , pp. 1405-1406
    • Gellatly, K.S.1    Lefebvre, D.D.2
  • 29
    • 0032492721 scopus 로고    scopus 로고
    • 2+ bind to the catalytic domain, but not the C2 domain
    • 2+ bind to the catalytic domain, but not the C2 domain. Biochemistry 37, 5020-5028.
    • (1998) Biochemistry , vol.37 , pp. 5020-5028
    • Grobler, J.A.1    Hurley, J.H.2
  • 30
    • 0024278916 scopus 로고
    • Spec2 genes of Strongylocentrotus purpuratus. Structure and differential expression in embryonic aboral ectoderm cells
    • Hardin PE, Angerer LM, Hardin SH, Angerer RC, Klein WH. 1988 Spec2 genes of Strongylocentrotus purpuratus. Structure and differential expression in embryonic aboral ectoderm cells. J. Mol. Biol. 202, 417-431.
    • (1988) J. Mol. Biol. , vol.202 , pp. 417-431
    • Hardin, P.E.1    Angerer, L.M.2    Hardin, S.H.3    Angerer, R.C.4    Klein, W.H.5
  • 31
    • 0024961944 scopus 로고
    • Amino acid sequence of a low molecular weight, high affinity calcium-binding protein from the optic lobe of the squid, Loligo pealei
    • Head JF. 1989 Amino acid sequence of a low molecular weight, high affinity calcium-binding protein from the optic lobe of the squid, Loligo pealei. J. Biol. Chem. 264, 7202-7209.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7202-7209
    • Head, J.F.1
  • 34
    • 0029643912 scopus 로고    scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2 Å resolution: Implications for regulation
    • Houdusse A, Cohen C. 1996 Structure of the regulatory domain of scallop myosin at 2 Å resolution: Implications for regulation. Structure 4, 21-32.
    • (1996) Structure , vol.4 , pp. 21-32
    • Houdusse, A.1    Cohen, C.2
  • 35
  • 37
    • 0015511197 scopus 로고
    • Gene triplication deduced from the tertiary structure of a muscle calcium binding protein
    • Kretsinger RH. 1972 Gene triplication deduced from the tertiary structure of a muscle calcium binding protein. Nature New Biology 240, 85-88.
    • (1972) Nature New Biology , vol.240 , pp. 85-88
    • Kretsinger, R.H.1
  • 39
    • 0024829783 scopus 로고
    • The nucleotide sequence of a developmentally regulated cDNA from Physarum polysephalum
    • Laroche A, Lemieux G, Pallotta D. 1989 The nucleotide sequence of a developmentally regulated cDNA from Physarum polysephalum. Nucleic Acids Res. 17, 10502-10502.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10502
    • Laroche, A.1    Lemieux, G.2    Pallotta, D.3
  • 41
    • 0027195421 scopus 로고
    • The structure of human trichohyalin. Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein
    • Lee S-C, Kim I-G, Marekov LN, O'Keefe EJ, Parry DAD, Steinert PM. 1993 The structure of human trichohyalin. Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein. J. Biol. Chem. 268, 12164-12176.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12164-12176
    • Lee, S.-C.1    Kim, I.-G.2    Marekov, L.N.3    O'Keefe, E.J.4    Parry, D.A.D.5    Steinert, P.M.6
  • 42
    • 0028221820 scopus 로고
    • Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney
    • Lin CS, Shen W, Chen ZP, Tu YH, Matsudaira P. 1994 Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney. Mol. Cell. Biol. 14, 2457-2467.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2457-2467
    • Lin, C.S.1    Shen, W.2    Chen, Z.P.3    Tu, Y.H.4    Matsudaira, P.5
  • 43
    • 0029981094 scopus 로고    scopus 로고
    • A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange
    • Lin X, Barber DL. 1996 A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange. Proc. Natl. Acad. Sci. 93, 12631-12636.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 12631-12636
    • Lin, X.1    Barber, D.L.2
  • 44
    • 0027597441 scopus 로고
    • Isolation of an Arabidopsis cDNA sequence encoding a 22 kDa calcium-binding protein (CaBP-22) related to calmodulin
    • Ling V, Zielinski RE. 1993 Isolation of an Arabidopsis cDNA sequence encoding a 22 kDa calcium-binding protein (CaBP-22) related to calmodulin. Plant Mol. Biol. 22, 207-214.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 207-214
    • Ling, V.1    Zielinski, R.E.2
  • 47
    • 0030910248 scopus 로고    scopus 로고
    • Calcium-binding mechanism of human nonerythroid α-spectrin EF-structures
    • Lundberg S, Buevich AV, Sethson I, Edlund U, Backman L. 1997 Calcium-binding mechanism of human nonerythroid α-spectrin EF-structures. Biochemistry 23, 7199-7208.
    • (1997) Biochemistry , vol.23 , pp. 7199-7208
    • Lundberg, S.1    Buevich, A.V.2    Sethson, I.3    Edlund, U.4    Backman, L.5
  • 50
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo CA, Jones, DT, Thornton JM. 1994 Protein superfamilies and domain superfolds. Nature 372, 631-634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 51
    • 0027439695 scopus 로고
    • 2+-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence
    • 2+-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J. Biol. Chem. 268, 699-705.
    • (1993) J. Biol. Chem. , vol.268 , pp. 699-705
    • Ozawa, M.1    Muramatsu, T.2
  • 52
    • 0023096432 scopus 로고
    • Sequence comparisons of complementary DNAs encoding aequorin isotypes
    • Prasher DC, McCann RO, Longiaru M, Cormier MJ. 1987 Sequence comparisons of complementary DNAs encoding aequorin isotypes. Biochemistry 26, 1326-1332.
    • (1987) Biochemistry , vol.26 , pp. 1326-1332
    • Prasher, D.C.1    McCann, R.O.2    Longiaru, M.3    Cormier, M.J.4
  • 53
    • 0026699150 scopus 로고
    • A novel 40-kDa membrane-associated EF-Hand calcium-binding protein in Plasmodium falciparum
    • Rawlings DJ, Kaslow DC. 1992 A novel 40-kDa membrane-associated EF-Hand calcium-binding protein in Plasmodium falciparum. J. Biol. Chem. 267 3976-3982.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3976-3982
    • Rawlings, D.J.1    Kaslow, D.C.2
  • 55
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads A, Friedberg F. 1997 Sequence motifs for calmodulin recognition. FASEB J. 11, 331-340.
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.1    Friedberg, F.2
  • 56
    • 0032539583 scopus 로고    scopus 로고
    • 2+-dependent interaction of S100B(ββ) with a peptide derived from p53
    • 2+-dependent interaction of S100B(ββ) with a peptide derived from p53. Biochemistry 37, 1951-1960.
    • (1998) Biochemistry , vol.37 , pp. 1951-1960
    • Rustandi, R.R.1    Drohat, A.C.2    Weber, D.J.3
  • 57
    • 0031058855 scopus 로고    scopus 로고
    • cDNA cloning and prokaryotic expression of maize calcium-dependent protein kinases
    • Saijo Y, Hata S, Sheen J, Izui K. 1997 cDNA cloning and prokaryotic expression of maize calcium-dependent protein kinases. Biochim. Biophys. Acta 1350, 109-114.
    • (1997) Biochim. Biophys. Acta , vol.1350 , pp. 109-114
    • Saijo, Y.1    Hata, S.2    Sheen, J.3    Izui, K.4
  • 58
    • 0023042567 scopus 로고
    • A novel calmodulin-like gene from the nematode Caenorhabditis elegans
    • Salvato M, Sulston J, Albertson D, Brenner S. 1986 A novel calmodulin-like gene from the nematode Caenorhabditis elegans. J. Mol. Biol. 190, 281-289.
    • (1986) J. Mol. Biol. , vol.190 , pp. 281-289
    • Salvato, M.1    Sulston, J.2    Albertson, D.3    Brenner, S.4
  • 59
    • 0028985241 scopus 로고
    • 2+-binding protein from abdominal muscle of crustaceans with similarity to calcyphosine from dog thyrodea
    • 2+-binding protein from abdominal muscle of crustaceans with similarity to calcyphosine from dog thyrodea. Eur. J. Biochem 227, 97-101.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 97-101
    • Sauter, A.1    Staudenmann, W.2    Hughes, G.J.3    Heizmann, C.W.4
  • 60
    • 0028987554 scopus 로고
    • Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: Rationale for a new nomenclature of the S100 calcium-binding protein family
    • Schäfer BW, Wicki R, Engelkamp D, Mattei M-G, Heizmann CW. 1995 Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: Rationale for a new nomenclature of the S100 calcium-binding protein family. Genomics 25, 638-643.
    • (1995) Genomics , vol.25 , pp. 638-643
    • Schäfer, B.W.1    Wicki, R.2    Engelkamp, D.3    Mattei, M.-G.4    Heizmann, C.W.5
  • 61
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schäfer BW, Heizmann CW. 1996 The S100 family of EF-hand calcium-binding proteins: functions and pathology. TIBS 21, 134-140.
    • (1996) TIBS , vol.21 , pp. 134-140
    • Schäfer, B.W.1    Heizmann, C.W.2
  • 62
    • 0032520214 scopus 로고    scopus 로고
    • A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form
    • Smith SP, Shaw GS. 1998 A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure 6, 211-222.
    • (1998) Structure , vol.6 , pp. 211-222
    • Smith, S.P.1    Shaw, G.S.2
  • 63
    • 0026724733 scopus 로고
    • Drosophila retinal degeneration C (rdgC) encodes a novel serine/threonine protein phosphatase
    • Steele FR, Washburn T, Rieger R, O'Tousa JE. 1992 Drosophila retinal degeneration C (rdgC) encodes a novel serine/threonine protein phosphatase. Cell 69, 669-676.
    • (1992) Cell , vol.69 , pp. 669-676
    • Steele, F.R.1    Washburn, T.2    Rieger, R.3    O'Tousa, J.E.4
  • 64
    • 0024470620 scopus 로고
    • Cloning, characterization, and heterologous expression of the Saccharopolyspora eythraea (Streptomyces erythraeus) gene encoding an EF-Hand calcium-binding protein
    • Swan DG, Cortes J, Hale RS, Leadlay PF. 1989 Cloning, characterization, and heterologous expression of the Saccharopolyspora eythraea (Streptomyces erythraeus) gene encoding an EF-Hand calcium-binding protein. J. Bacteriol. 171, 5614-5619.
    • (1989) J. Bacteriol. , vol.171 , pp. 5614-5619
    • Swan, D.G.1    Cortes, J.2    Hale, R.S.3    Leadlay, P.F.4
  • 66
    • 0025320808 scopus 로고
    • The third calmodulin family protein in Tetrahymena. Cloning of the cDNA for Tetrahymena calcium-binding protein of 23 kDa (TCBP-23)
    • Takemasa T, Takagi T, Kobayashi T, Konishi K, Watanabe Y. 1990 The third calmodulin family protein in Tetrahymena. Cloning of the cDNA for Tetrahymena calcium-binding protein of 23 kDa (TCBP-23). J. Biol. Chem. 265, 2514-2517.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2514-2517
    • Takemasa, T.1    Takagi, T.2    Kobayashi, T.3    Konishi, K.4    Watanabe, Y.5
  • 67
    • 0027474019 scopus 로고
    • Projection image of smooth muscle α-actinin from 2-D crystals formed on positively charged lipid layers
    • Taylor KA, Taylor DW. 1993 Projection image of smooth muscle α-actinin from 2-D crystals formed on positively charged lipid layers. J. Mol. Biol. 230, 196-205.
    • (1993) J. Mol. Biol. , vol.230 , pp. 196-205
    • Taylor, K.A.1    Taylor, D.W.2
  • 68
    • 0031441360 scopus 로고    scopus 로고
    • Plasmodium falciparum Pfs40, renamed Pf39, is localized to an intracellular membrane-bound compartment and is not sexual stage-specific
    • Templeton TJ, Fujioka H, Aikawa M, Parker KC. 1997 Plasmodium falciparum Pfs40, renamed Pf39, is localized to an intracellular membrane-bound compartment and is not sexual stage-specific. Mol. Biochem. Parasitol. 90, 359-365.
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 359-365
    • Templeton, T.J.1    Fujioka, H.2    Aikawa, M.3    Parker, K.C.4
  • 69
    • 0032574791 scopus 로고    scopus 로고
    • Crystal structure of troponin C in complex with troponin I fragment at 2.3 Å resolution
    • Vassylev DG, Takeda S, Wakatsuki S, Maeda K, Maeda Y. 1998 Crystal structure of troponin C in complex with troponin I fragment at 2.3 Å resolution. Proc. Natl. Acad. Sci. 95 4847-4852.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 4847-4852
    • Vassylev, D.G.1    Takeda, S.2    Wakatsuki, S.3    Maeda, K.4    Maeda, Y.5
  • 70
    • 0027396504 scopus 로고
    • Genomic and transcriptional control linkage of the genes for calmodulin, EF-hand 5 protein, and ubiquitin extension protein 52 in Trypanosoma brucei
    • Wong S, Morales TH, Neigel JE, Campbell DA. 1993 Genomic and transcriptional control linkage of the genes for calmodulin, EF-hand 5 protein, and ubiquitin extension protein 52 in Trypanosoma brucei. Mol. Cell. Biol. 13, 207-216.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 207-216
    • Wong, S.1    Morales, T.H.2    Neigel, J.E.3    Campbell, D.A.4
  • 71
    • 0029843769 scopus 로고    scopus 로고
    • Calcium transport and the localisation of calbindin D9k in the ruminant placenta during the second half of pregnancy
    • Wooding FBP, Morgan G, Jones GV, Care AD. 1996 Calcium transport and the localisation of calbindin D9k in the ruminant placenta during the second half of pregnancy. Cell Tissue Res. 285, 477-489.
    • (1996) Cell Tissue Res. , vol.285 , pp. 477-489
    • Wooding, F.B.P.1    Morgan, G.2    Jones, G.V.3    Care, A.D.4
  • 72
    • 0026793533 scopus 로고
    • The predominant calcimedins from Trypanosoma brucei comprise a family of flagellar EF-hand calcium-binding proteins
    • Wu Y, Haghighat NG, Ruben L. 1992 The predominant calcimedins from Trypanosoma brucei comprise a family of flagellar EF-hand calcium-binding proteins. Biochem. J. 287, 187-193.
    • (1992) Biochem. J. , vol.287 , pp. 187-193
    • Wu, Y.1    Haghighat, N.G.2    Ruben, L.3
  • 73
    • 0025851340 scopus 로고
    • Structure and promoter activity of the LpSI genes of Lytechinus pictus
    • Xiang M, Ge T, Tomlinson CR, Klein WH. 1991 Structure and promoter activity of the LpSI genes of Lytechinus pictus. J. Biol. Chem. 266, 10524-10533.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10524-10533
    • Xiang, M.1    Ge, T.2    Tomlinson, C.R.3    Klein, W.H.4
  • 74
    • 0031033007 scopus 로고    scopus 로고
    • EF-hand motifs of α, β and γ isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes
    • Yamada K, Sakane F, Matsushima N, Kanoh H. 1997 EF-hand motifs of α, β and γ isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes. Biochem. J. 321, 59-64.
    • (1997) Biochem. J. , vol.321 , pp. 59-64
    • Yamada, K.1    Sakane, F.2    Matsushima, N.3    Kanoh, H.4
  • 75
    • 0027416648 scopus 로고
    • Gene structure and expression of an unusual protein kinase from Plasmodium falciparum homologous at its carboxyl terminus with the EF Hand calcium-binding proteins
    • Zhao Y, Kappes B, Franklin RM. 1993 Gene structure and expression of an unusual protein kinase from Plasmodium falciparum homologous at its carboxyl terminus with the EF Hand calcium-binding proteins. J. Biol. Chem. 268, 4347-4354.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4347-4354
    • Zhao, Y.1    Kappes, B.2    Franklin, R.M.3


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