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Volumn 76, Issue 6, 2007, Pages 926-935

Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins

Author keywords

Atherosclerosis; Developmental biology; Gametogenesis; Hemostasis; Lipoprotein; Lipovitellin; Oocyte development; Von Willebrand factor

Indexed keywords

ADHESIN; ARGINYLGLYCYLASPARTIC ACID; BLOOD CLOTTING FACTOR 8; CYSTEINE; INTEGRIN; LIPOPHORIN; LIPOVITELLIN; MONOMER; MUCIN; PHOSVITIN; PROTEIN PRECURSOR; SERINE; VITELLOGENIN; VON WILLEBRAND FACTOR;

EID: 34249689094     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.106.059766     Document Type: Short Survey
Times cited : (135)

References (120)
  • 1
    • 0022163146 scopus 로고
    • Vitellogenesis and oocyte growth in nonmammalian vertebrates
    • Browder LW ed, New York: Plenum Press;
    • Wallace RA. Vitellogenesis and oocyte growth in nonmammalian vertebrates. In: Browder LW (ed.). Developmental Biology, vol. I. New York: Plenum Press; 1985:127-177.
    • (1985) Developmental Biology , vol.1 , pp. 127-177
    • Wallace, R.A.1
  • 3
    • 0030934540 scopus 로고    scopus 로고
    • Extensive sequence conservation among insect, nematode, and vertebrate vitellogenins reveals ancient common ancestry
    • Chen JS, Sappington TW, Raikhel AS. Extensive sequence conservation among insect, nematode, and vertebrate vitellogenins reveals ancient common ancestry. J Mol Evol 1997; 44:440-451.
    • (1997) J Mol Evol , vol.44 , pp. 440-451
    • Chen, J.S.1    Sappington, T.W.2    Raikhel, A.S.3
  • 4
    • 0032078463 scopus 로고    scopus 로고
    • Molecular characteristics of insect vitellogenins and vitellogenin receptors
    • Sappington TW, Raikhel AS. Molecular characteristics of insect vitellogenins and vitellogenin receptors. Insect Biochem Mol Biol 1998; 28:277-300.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 277-300
    • Sappington, T.W.1    Raikhel, A.S.2
  • 5
    • 34249725019 scopus 로고    scopus 로고
    • The maturational disassembly and differential proteolysis of paralogous vitellogenins in a marine pelagophil teleost: A conserved mechanism of oocyte hydration
    • Finn RN. The maturational disassembly and differential proteolysis of paralogous vitellogenins in a marine pelagophil teleost: a conserved mechanism of oocyte hydration. Biol Reprod 2002; 76:936-948.
    • (2002) Biol Reprod , vol.76 , pp. 936-948
    • Finn, R.N.1
  • 6
    • 34249733664 scopus 로고    scopus 로고
    • Vertebrate vitellogenin gene duplication in relation to the "3R Hypothesis": Correlation to the pelagic egg and the oceanic radiation of teleosts
    • Finn RN, Kristoffersen BA. Vertebrate vitellogenin gene duplication in relation to the "3R Hypothesis": correlation to the pelagic egg and the oceanic radiation of teleosts. PLoS ONE 2007; 2:e169.
    • (2007) PLoS ONE , vol.2
    • Finn, R.N.1    Kristoffersen, B.A.2
  • 8
    • 0014249302 scopus 로고
    • Comparative chromatography of the yolk proteins of teleosts
    • Jared DW, Wallace RA. Comparative chromatography of the yolk proteins of teleosts. Comp Biochem Physiol 1968; 24:437-443.
    • (1968) Comp Biochem Physiol , vol.24 , pp. 437-443
    • Jared, D.W.1    Wallace, R.A.2
  • 9
    • 0000922861 scopus 로고
    • Egg proteins of coho salmon (Oncorhynchus kisutch): Chromatographic separation and molecular weights of the major proteins in the high density fraction and their presence in salmon plasma
    • Markert JR, Vanstone WE. Egg proteins of coho salmon (Oncorhynchus kisutch): chromatographic separation and molecular weights of the major proteins in the high density fraction and their presence in salmon plasma. J Fish Res Bd Can 1971; 28:1853-1856.
    • (1971) J Fish Res Bd Can , vol.28 , pp. 1853-1856
    • Markert, J.R.1    Vanstone, W.E.2
  • 10
    • 0025015440 scopus 로고
    • Ultrastructural aspects of oogenesis and oocyte growth in fish and amphibians
    • Wallace RA, Selman K. Ultrastructural aspects of oogenesis and oocyte growth in fish and amphibians. J Electron Microsc Tech 1990; 16:175-201.
    • (1990) J Electron Microsc Tech , vol.16 , pp. 175-201
    • Wallace, R.A.1    Selman, K.2
  • 11
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL. Regulated portals of entry into the cell. Nature 2003; 422:37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 12
    • 3142583466 scopus 로고    scopus 로고
    • Cargo recognition during clathrin-mediated endocytosis: A team effort
    • Sorkin A. Cargo recognition during clathrin-mediated endocytosis: a team effort. Curr Opin Cell Biol 2004; 16:392-399.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 392-399
    • Sorkin, A.1
  • 13
    • 28444456720 scopus 로고    scopus 로고
    • Cell biology: Protein choreography
    • Duncan MC, Payne GS. Cell biology: protein choreography. Nature 2005; 438:571-573.
    • (2005) Nature , vol.438 , pp. 571-573
    • Duncan, M.C.1    Payne, G.S.2
  • 14
    • 33744539316 scopus 로고    scopus 로고
    • Membrane traffic: Catching the lysosome express
    • Clague MJ, Hammond DE. Membrane traffic: catching the lysosome express. Curr Biol 2006; 16:R416-418.
    • (2006) Curr Biol , vol.16
    • Clague, M.J.1    Hammond, D.E.2
  • 15
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • Lakadamyalt M, Rust MJ, Zhuang X. Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 2006; 124:997-1009.
    • (2006) Cell , vol.124 , pp. 997-1009
    • Lakadamyalt, M.1    Rust, M.J.2    Zhuang, X.3
  • 16
    • 0021185179 scopus 로고
    • Endosomes transfer yolk proteins to lysosomes in the vitellogenic oocyte of the trout
    • Busson-Mabillot S. Endosomes transfer yolk proteins to lysosomes in the vitellogenic oocyte of the trout. Biol Cell 1984; 51:53-66.
    • (1984) Biol Cell , vol.51 , pp. 53-66
    • Busson-Mabillot, S.1
  • 17
    • 0029583839 scopus 로고
    • Regulation of yolk degradation, or how to make sleepy lysosomes
    • Fagotto F. Regulation of yolk degradation, or how to make sleepy lysosomes. J Cell Sci 1995; 108:3645-3647.
    • (1995) J Cell Sci , vol.108 , pp. 3645-3647
    • Fagotto, F.1
  • 18
    • 0035421972 scopus 로고    scopus 로고
    • Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes
    • Selman K, Wallace RA, Cerdà J. Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes. J Exp Zool 2001; 290:265-278.
    • (2001) J Exp Zool , vol.290 , pp. 265-278
    • Selman, K.1    Wallace, R.A.2    Cerdà, J.3
  • 20
    • 0028023542 scopus 로고
    • Cathepsin D activity in the vitellogenesis of Xenopus laevis
    • Yoshizaki N, Yonezawa S. Cathepsin D activity in the vitellogenesis of Xenopus laevis. Dev Growth Differ 1994; 36:299-306.
    • (1994) Dev Growth Differ , vol.36 , pp. 299-306
    • Yoshizaki, N.1    Yonezawa, S.2
  • 21
    • 21944456030 scopus 로고    scopus 로고
    • Specific proteolysis of vitellogenin to egg yolk proteins in white spotted-charr Salvelinus leucomaenis
    • Hiramatsu N, Hara A. Specific proteolysis of vitellogenin to egg yolk proteins in white spotted-charr Salvelinus leucomaenis. Nippon Suisan Gakkaishi 1997; 63:701-708.
    • (1997) Nippon Suisan Gakkaishi , vol.63 , pp. 701-708
    • Hiramatsu, N.1    Hara, A.2
  • 22
    • 0032918875 scopus 로고    scopus 로고
    • Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: Involvement of two lysosomal proteinases
    • Carnevali O, Carletta R, Cambi A, Vita A, Bromage N. Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: involvement of two lysosomal proteinases. Biol Reprod 1999; 60:140-146.
    • (1999) Biol Reprod , vol.60 , pp. 140-146
    • Carnevali, O.1    Carletta, R.2    Cambi, A.3    Vita, A.4    Bromage, N.5
  • 24
    • 0036006819 scopus 로고    scopus 로고
    • Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids
    • Hiramatsu N, Ichikawa N, Fukada H, Fujita T, Sullivan CV, Hara A. Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J Exp Zool 2002; 292:11-25.
    • (2002) J Exp Zool , vol.292 , pp. 11-25
    • Hiramatsu, N.1    Ichikawa, N.2    Fukada, H.3    Fujita, T.4    Sullivan, C.V.5    Hara, A.6
  • 25
    • 0942265428 scopus 로고    scopus 로고
    • Fabra M, Cerdà J. Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation. Mol Reprod Dev S 2004; 67:282-294.
    • Fabra M, Cerdà J. Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation. Mol Reprod Dev S 2004; 67:282-294.
  • 28
    • 0029123767 scopus 로고
    • Fundulus heteroclitus vitellogenin: The deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein
    • LaFleur GJ Jr, Byrne BM, Kanungo J, Nelson LD, Greenberg RM, Wallace RA. Fundulus heteroclitus vitellogenin: the deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein. J Mol Evol 1995; 41:505-521.
    • (1995) J Mol Evol , vol.41 , pp. 505-521
    • LaFleur Jr, G.J.1    Byrne, B.M.2    Kanungo, J.3    Nelson, L.D.4    Greenberg, R.M.5    Wallace, R.A.6
  • 29
    • 25144498370 scopus 로고    scopus 로고
    • Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus
    • LaFleur GJ Jr, Raldúa D, Fabra M, Carnevali O, Denslow N, Wallace RA, Cerdà J. Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus. Biol Reprod 2005; 73:815-824.
    • (2005) Biol Reprod , vol.73 , pp. 815-824
    • LaFleur Jr, G.J.1    Raldúa, D.2    Fabra, M.3    Carnevali, O.4    Denslow, N.5    Wallace, R.A.6    Cerdà, J.7
  • 30
    • 0033199056 scopus 로고    scopus 로고
    • Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs
    • Matsubara T, Ohkubo N, Andoh T, Sullivan CV, Hara A. Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs. Dev Biol 1999; 213: 18-32.
    • (1999) Dev Biol , vol.213 , pp. 18-32
    • Matsubara, T.1    Ohkubo, N.2    Andoh, T.3    Sullivan, C.V.4    Hara, A.5
  • 32
    • 0033835317 scopus 로고    scopus 로고
    • Trichet V, Buisine N, Mouchel N, Moran P, Pendas AM, Le Pennec JP, Wolff J. Genomic analysis of the vitellogenin locus in rainbow trout (Oncorhynchus mykiss) reveals a complex history of gene amplification and retroposon activity. Mol Gen Genet S 2000; 263:828-837.
    • Trichet V, Buisine N, Mouchel N, Moran P, Pendas AM, Le Pennec JP, Wolff J. Genomic analysis of the vitellogenin locus in rainbow trout (Oncorhynchus mykiss) reveals a complex history of gene amplification and retroposon activity. Mol Gen Genet S 2000; 263:828-837.
  • 33
    • 0035870296 scopus 로고    scopus 로고
    • Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus)
    • Reith M, Munholland J, Kelly J, Finn RN, Fyhn HJ. Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus). J Exp Zool 2001; 291:58-67.
    • (2001) J Exp Zool , vol.291 , pp. 58-67
    • Reith, M.1    Munholland, J.2    Kelly, J.3    Finn, R.N.4    Fyhn, H.J.5
  • 34
    • 0036456018 scopus 로고    scopus 로고
    • Complex evolution of vitellogenin genes in salmonid fishes
    • Buisine N, Trichet V, Wolff J. Complex evolution of vitellogenin genes in salmonid fishes. Mol Genet Genomics 2002; 268:535-542.
    • (2002) Mol Genet Genomics , vol.268 , pp. 535-542
    • Buisine, N.1    Trichet, V.2    Wolff, J.3
  • 37
    • 0344088420 scopus 로고    scopus 로고
    • Development of enzyme-linked immunosorbent assays for two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus)
    • Ohkubo N, Mochida K, Adachi S, Hara A, Hotta K, Nakamura Y, Matsubara T. Development of enzyme-linked immunosorbent assays for two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus). Gen Comp Endocrinol 2003; 131:353-364.
    • (2003) Gen Comp Endocrinol , vol.131 , pp. 353-364
    • Ohkubo, N.1    Mochida, K.2    Adachi, S.3    Hara, A.4    Hotta, K.5    Nakamura, Y.6    Matsubara, T.7
  • 38
    • 1942535909 scopus 로고    scopus 로고
    • Deduced primary structure of two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus)
    • Ohkubo N, Andoh T, Mochida K, Adachi S, Hara A, Matsubara T. Deduced primary structure of two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus). Gen Comp Endocrinol 2004; 137:19-28.
    • (2004) Gen Comp Endocrinol , vol.137 , pp. 19-28
    • Ohkubo, N.1    Andoh, T.2    Mochida, K.3    Adachi, S.4    Hara, A.5    Matsubara, T.6
  • 39
    • 24644470532 scopus 로고    scopus 로고
    • De novo' sequencing of Atlantic cod vitellogenin tryptic peptides by matrix-assisted laser desorption/ ionization quadrupole time-of-flight tandem mass spectrometry: Similarities with haddock vitellogenin
    • Cohen AM, Mansour AA, Banoub JH. 'De novo' sequencing of Atlantic cod vitellogenin tryptic peptides by matrix-assisted laser desorption/ ionization quadrupole time-of-flight tandem mass spectrometry: similarities with haddock vitellogenin. Rapid Commun Mass Spectrom 2005; 19:2454-2460.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 2454-2460
    • Cohen, A.M.1    Mansour, A.A.2    Banoub, J.H.3
  • 40
    • 23844552247 scopus 로고    scopus 로고
    • Purification of two lipovitellins and development of immunoassays for two forms of their precursors (vitellogenins) in medaka (Oryzias latipes)
    • Fujiwara Y, Fukada H, Shimizu M, Hara A. Purification of two lipovitellins and development of immunoassays for two forms of their precursors (vitellogenins) in medaka (Oryzias latipes). Gen Comp Endocrinol 2005; 143:267-277.
    • (2005) Gen Comp Endocrinol , vol.143 , pp. 267-277
    • Fujiwara, Y.1    Fukada, H.2    Shimizu, M.3    Hara, A.4
  • 41
    • 23844471566 scopus 로고    scopus 로고
    • Hepatic and extrahepatic expression of vitellogenin genes in the zebrafish. Danio rerio
    • Wang H, Tan JT, Emelyanov A, Korzh V, Gong Z. Hepatic and extrahepatic expression of vitellogenin genes in the zebrafish. Danio rerio. Gene 2005; 356:91-100.
    • (2005) Gene , vol.356 , pp. 91-100
    • Wang, H.1    Tan, J.T.2    Emelyanov, A.3    Korzh, V.4    Gong, Z.5
  • 42
    • 15544368550 scopus 로고    scopus 로고
    • Multiple vitellogenins (Vgs) in mosquitofish (Gambusia affinis): Identification and characterization of three functional Vg genes and their circulating and yolk protein products
    • Sawaguchi S, Koya Y, Yoshizaki N, Ohkubo N, Andoh T, Hiramatsu N, Sullivan CV, Hara A, Matsubara T. Multiple vitellogenins (Vgs) in mosquitofish (Gambusia affinis): identification and characterization of three functional Vg genes and their circulating and yolk protein products. Biol Reprod 2005; 72:1045-1060.
    • (2005) Biol Reprod , vol.72 , pp. 1045-1060
    • Sawaguchi, S.1    Koya, Y.2    Yoshizaki, N.3    Ohkubo, N.4    Andoh, T.5    Hiramatsu, N.6    Sullivan, C.V.7    Hara, A.8    Matsubara, T.9
  • 43
    • 22544475931 scopus 로고    scopus 로고
    • Incorporation and utilization of multiple forms of vitellogenin and their derivative yolk proteins during vitellogenesis and embryonic development in the mosquitofish. Gambusia affinis
    • Sawaguchi S, Ohkubo N, Koya Y, Matsubara T. Incorporation and utilization of multiple forms of vitellogenin and their derivative yolk proteins during vitellogenesis and embryonic development in the mosquitofish. Gambusia affinis. Zool Sci 2005; 22:701-710.
    • (2005) Zool Sci , vol.22 , pp. 701-710
    • Sawaguchi, S.1    Ohkubo, N.2    Koya, Y.3    Matsubara, T.4
  • 44
    • 33646441137 scopus 로고    scopus 로고
    • Molecular characterization of three forms of vitellogenin and their yolk protein products during oocyte growth and maturation in red seabream (Pagrus major), a marine teleost spawning pelagic eggs
    • Sawaguchi S, Kagawa H, Ohkubo N, Hiramatsu N, Sullivan CV, Matsubara T. Molecular characterization of three forms of vitellogenin and their yolk protein products during oocyte growth and maturation in red seabream (Pagrus major), a marine teleost spawning pelagic eggs. Mol Reprod Dev 2006; 73:719-736.
    • (2006) Mol Reprod Dev , vol.73 , pp. 719-736
    • Sawaguchi, S.1    Kagawa, H.2    Ohkubo, N.3    Hiramatsu, N.4    Sullivan, C.V.5    Matsubara, T.6
  • 45
    • 33644559375 scopus 로고    scopus 로고
    • Expression of two vitellogenin genes (vg1 and vg3) in fathead minnow (Pimephales promelas) liver in response to exposure to steroidal estrogens and androgens
    • Miracle A, Ankley G, Lattier D. Expression of two vitellogenin genes (vg1 and vg3) in fathead minnow (Pimephales promelas) liver in response to exposure to steroidal estrogens and androgens. Ecotoxicol Environ Saf 2006; 63:337-342.
    • (2006) Ecotoxicol Environ Saf , vol.63 , pp. 337-342
    • Miracle, A.1    Ankley, G.2    Lattier, D.3
  • 46
    • 0017712492 scopus 로고    scopus 로고
    • Lipid and polypeptde components of the crystalline yolk system from Xenopus laevis
    • Ohlendorf DH, Barbarash GR, Trout A, Kent C, Banaszak LJ. Lipid and polypeptde components of the crystalline yolk system from Xenopus laevis. J Biol Chem 1997; 252:7992-8001.
    • (1997) J Biol Chem , vol.252 , pp. 7992-8001
    • Ohlendorf, D.H.1    Barbarash, G.R.2    Trout, A.3    Kent, C.4    Banaszak, L.J.5
  • 48
    • 0016137783 scopus 로고
    • Precursor-product relationship between amphibian vitellogenin and the yolk proteins, lipovitellin and phosvitin
    • Bergink EW, Wallace RA. Precursor-product relationship between amphibian vitellogenin and the yolk proteins, lipovitellin and phosvitin. J Biol Chem 1974; 249:2897-2903.
    • (1974) J Biol Chem , vol.249 , pp. 2897-2903
    • Bergink, E.W.1    Wallace, R.A.2
  • 49
    • 0025281491 scopus 로고
    • Placement of small lipovitellin subunits within the vitellogenin precursor in Xenopus laevis
    • Wallace RA, Hoch KL, Carnevali O. Placement of small lipovitellin subunits within the vitellogenin precursor in Xenopus laevis. J Mol Biol 1990; 213:407-409.
    • (1990) J Mol Biol , vol.213 , pp. 407-409
    • Wallace, R.A.1    Hoch, K.L.2    Carnevali, O.3
  • 51
    • 0018908112 scopus 로고
    • Identificiation, purification, and characterization of two distinct avian vitellogenins
    • Wang SY, Williams DL. Identificiation, purification, and characterization of two distinct avian vitellogenins. Biochemistry 1980; 19:1557-1563.
    • (1980) Biochemistry , vol.19 , pp. 1557-1563
    • Wang, S.Y.1    Williams, D.L.2
  • 52
    • 0000985335 scopus 로고
    • Purification of avian vitellogenin III: Comparison with vitellogenins I and II
    • Wang SY, Smith DE, Williams DL. Purification of avian vitellogenin III: comparison with vitellogenins I and II. Biochemistry 1983; 22:6206-6212.
    • (1983) Biochemistry , vol.22 , pp. 6206-6212
    • Wang, S.Y.1    Smith, D.E.2    Williams, D.L.3
  • 53
    • 0023660763 scopus 로고    scopus 로고
    • van het Schip FD, Samallo J, Broos J, Ophuis J, Mojet M, Gruber M, Ab G. Nucleotide sequence of a chicken vitellogenin gene and derived amino acid sequence of the encoded yolk precursor protein. J Mol Biol 1987; 196:245-260.
    • van het Schip FD, Samallo J, Broos J, Ophuis J, Mojet M, Gruber M, Ab G. Nucleotide sequence of a chicken vitellogenin gene and derived amino acid sequence of the encoded yolk precursor protein. J Mol Biol 1987; 196:245-260.
  • 54
    • 0024345781 scopus 로고
    • The major and minor chicken vitellogenin genes are each adjacent to partially deleted pseudogene copies of the other
    • Silva R, Fischer AH, Burch JB. The major and minor chicken vitellogenin genes are each adjacent to partially deleted pseudogene copies of the other. Mol Cell Biol 1989; 9:3557-3562.
    • (1989) Mol Cell Biol , vol.9 , pp. 3557-3562
    • Silva, R.1    Fischer, A.H.2    Burch, J.B.3
  • 55
    • 0019888345 scopus 로고
    • The structure of vitellogenin. Multiple vitellogenins in Xenopus laevis give rise to multiple forms of the yolk proteins
    • Wiley HS, Wallace RA. The structure of vitellogenin. Multiple vitellogenins in Xenopus laevis give rise to multiple forms of the yolk proteins. J Biol Chem 1981; 256:8626-8634.
    • (1981) J Biol Chem , vol.256 , pp. 8626-8634
    • Wiley, H.S.1    Wallace, R.A.2
  • 56
    • 0021760617 scopus 로고    scopus 로고
    • Byrne BM, van het Schip AD, van de Klundert JA, Arnberg AC, Gruber M, Ab G. Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene. Biochemistry 1984; 23:4275-4279.
    • Byrne BM, van het Schip AD, van de Klundert JA, Arnberg AC, Gruber M, Ab G. Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene. Biochemistry 1984; 23:4275-4279.
  • 57
    • 0022868429 scopus 로고
    • Chromatographic resolution of chicken phosvitin. Multiple macromolecular species in a classic vitellogenin-derived phosphoprotein
    • Wallace RA, Morgan JP. Chromatographic resolution of chicken phosvitin. Multiple macromolecular species in a classic vitellogenin-derived phosphoprotein. Biochem J 1986; 240:871-878.
    • (1986) Biochem J , vol.240 , pp. 871-878
    • Wallace, R.A.1    Morgan, J.P.2
  • 58
    • 0022549434 scopus 로고
    • Isolation of phosvitin: Retention of small molecular weight species and staining characteristics on electrophoretic gels
    • Wallace RA, Morgan JP. Isolation of phosvitin: retention of small molecular weight species and staining characteristics on electrophoretic gels. Anal Biochem 1986; 157:256-261.
    • (1986) Anal Biochem , vol.157 , pp. 256-261
    • Wallace, R.A.1    Morgan, J.P.2
  • 59
    • 0028886111 scopus 로고
    • Proteolysis of Japanese quail and chicken plasma apolipoprotein B and vitellogenin by cathepsin D: Similarity of the resulting protein fragments with egg yolk polypeptides
    • Elkin RG, Freed MB, Danetz SA, Bidwell CA. Proteolysis of Japanese quail and chicken plasma apolipoprotein B and vitellogenin by cathepsin D: similarity of the resulting protein fragments with egg yolk polypeptides. Comp Biochem Physiol B Biochem Mol Biol 1995; 112: 191-196.
    • (1995) Comp Biochem Physiol B Biochem Mol Biol , vol.112 , pp. 191-196
    • Elkin, R.G.1    Freed, M.B.2    Danetz, S.A.3    Bidwell, C.A.4
  • 61
    • 0021881554 scopus 로고
    • The primary structure of avian Phosvitins. Contributions through the Edman degradation of methylmercaptovitins prepared from the constituent phosphoproteins
    • Clark RC. The primary structure of avian Phosvitins. Contributions through the Edman degradation of methylmercaptovitins prepared from the constituent phosphoproteins. Int J Biochem 1985; 17:983-988.
    • (1985) Int J Biochem , vol.17 , pp. 983-988
    • Clark, R.C.1
  • 62
    • 0034535161 scopus 로고    scopus 로고
    • Subunit composition of the zinc proteins alpha- and beta-lipovitellin from chicken
    • Groche D, Rashkovetsky LG, Falchuk KH, Auld DS. Subunit composition of the zinc proteins alpha- and beta-lipovitellin from chicken. J Protein Chem 2000; 19:379-387.
    • (2000) J Protein Chem , vol.19 , pp. 379-387
    • Groche, D.1    Rashkovetsky, L.G.2    Falchuk, K.H.3    Auld, D.S.4
  • 63
    • 0028867345 scopus 로고
    • Characterization of yolk proteins during oocyte development of tilapia, Oreochromis mossambicus
    • Johanning KM, Specker JL. Characterization of yolk proteins during oocyte development of tilapia, Oreochromis mossambicus. Comp Biochem Physiol 1995; 112B:177-189.
    • (1995) Comp Biochem Physiol , vol.112 B , pp. 177-189
    • Johanning, K.M.1    Specker, J.L.2
  • 64
    • 0032527992 scopus 로고    scopus 로고
    • The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein
    • Anderson TA, Levitt DG, Banaszak LJ. The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein. Structure 1998; 6:895-909.
    • (1998) Structure , vol.6 , pp. 895-909
    • Anderson, T.A.1    Levitt, D.G.2    Banaszak, L.J.3
  • 65
    • 0036321923 scopus 로고    scopus 로고
    • In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus); proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx
    • Finn RN, Ostby GC, Norberg B, Fyhn HJ. In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus); proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx. J Exp Biol 2002; 205:211-224.
    • (2002) J Exp Biol , vol.205 , pp. 211-224
    • Finn, R.N.1    Ostby, G.C.2    Norberg, B.3    Fyhn, H.J.4
  • 67
    • 0035904464 scopus 로고    scopus 로고
    • Sequence analysis of a fish vitellogenin cDNA with a large phosvitin domain
    • Lim EH, Teo BY, Lam TJ, Ding JL. Sequence analysis of a fish vitellogenin cDNA with a large phosvitin domain. Gene 2001; 277:175-186.
    • (2001) Gene , vol.277 , pp. 175-186
    • Lim, E.H.1    Teo, B.Y.2    Lam, T.J.3    Ding, J.L.4
  • 68
    • 0028361969 scopus 로고
    • Analysis of mosquito vitellogenin cDNA. Similarity with venebrate phosvitins and arthropod serum proteins
    • Chen JS, Cho WL, Raikhel AS. Analysis of mosquito vitellogenin cDNA. Similarity with venebrate phosvitins and arthropod serum proteins. J Mol Biol 1994; 237:641-647.
    • (1994) J Mol Biol , vol.237 , pp. 641-647
    • Chen, J.S.1    Cho, W.L.2    Raikhel, A.S.3
  • 69
    • 0037199420 scopus 로고    scopus 로고
    • Lipid-protein interactions in lipovitellin
    • Thompson JR, Banaszak LJ. Lipid-protein interactions in lipovitellin. Biochemistry 2002; 41:9398-9409.
    • (2002) Biochemistry , vol.41 , pp. 9398-9409
    • Thompson, J.R.1    Banaszak, L.J.2
  • 70
    • 0027449086 scopus 로고
    • Comparative studies of phosvitin from chicken and salmon egg yolk
    • Losso JN, Bogumil R, Nakai S. Comparative studies of phosvitin from chicken and salmon egg yolk. Comp Biochem Physiol B 1993; 106:919-923.
    • (1993) Comp Biochem Physiol B , vol.106 , pp. 919-923
    • Losso, J.N.1    Bogumil, R.2    Nakai, S.3
  • 71
    • 0023708536 scopus 로고
    • Is vitellogenin an ancestor of apolipoprotein B-100 of human low-density lipoprotein and human lipoprotein lipase?
    • Baker ME. Is vitellogenin an ancestor of apolipoprotein B-100 of human low-density lipoprotein and human lipoprotein lipase? Biochem J 1988; 255:1057-1060.
    • (1988) Biochem J , vol.255 , pp. 1057-1060
    • Baker, M.E.1
  • 72
    • 0033050294 scopus 로고    scopus 로고
    • Apolipophorin II/I, apolipoprotein B, vitellogenin, and microsomal triglyceride transfer protein genes are derived from a common ancestor
    • Babin PJ, Bogerd J, Kooiman FP, Van Marrewijk WJ, Van der Horst DJ. Apolipophorin II/I, apolipoprotein B, vitellogenin, and microsomal triglyceride transfer protein genes are derived from a common ancestor. J Mol Evol 1999; 49:150-160.
    • (1999) J Mol Evol , vol.49 , pp. 150-160
    • Babin, P.J.1    Bogerd, J.2    Kooiman, F.P.3    Van Marrewijk, W.J.4    Van der Horst, D.J.5
  • 74
    • 0030913589 scopus 로고    scopus 로고
    • Evolution of processes and regulators of lipoprotein synthesis: From birds to mammals
    • Davis RA. Evolution of processes and regulators of lipoprotein synthesis: from birds to mammals. J Nutr 1997; 127:795S-800S.
    • (1997) J Nutr , vol.127
    • Davis, R.A.1
  • 76
    • 13444281988 scopus 로고    scopus 로고
    • Limited proteolysis and biophysical characterization of the lipovitellin homology region in apolipoprotein B
    • Jiang ZG, Carraway M, McKnight CJ. Limited proteolysis and biophysical characterization of the lipovitellin homology region in apolipoprotein B. Biochemistry 2005; 44:1163-1173.
    • (2005) Biochemistry , vol.44 , pp. 1163-1173
    • Jiang, Z.G.1    Carraway, M.2    McKnight, C.J.3
  • 77
    • 4544328500 scopus 로고    scopus 로고
    • Apolipoprotein B-containing lipoprotein particle assembly: Lipid capacity of the nascent lipoprotein particle
    • Manchekar M, Richardson PE, Forte TM, Datta G, Segrest JP, Dashti N. Apolipoprotein B-containing lipoprotein particle assembly: lipid capacity of the nascent lipoprotein particle. J Biol Chem 2004; 279:39757-39766.
    • (2004) J Biol Chem , vol.279 , pp. 39757-39766
    • Manchekar, M.1    Richardson, P.E.2    Forte, T.M.3    Datta, G.4    Segrest, J.P.5    Dashti, N.6
  • 78
    • 0037018919 scopus 로고    scopus 로고
    • The N-terminal 1000 residues of apolipoprotein B associate with microsomal triglyceride transfer protein to create a lipid transfer pocket required for lipoprotein assembly
    • Dashti N, Gandhi M, Liu X, Lin X, Segrest JP. The N-terminal 1000 residues of apolipoprotein B associate with microsomal triglyceride transfer protein to create a lipid transfer pocket required for lipoprotein assembly. Biochemistry 2002; 41:6978-6987.
    • (2002) Biochemistry , vol.41 , pp. 6978-6987
    • Dashti, N.1    Gandhi, M.2    Liu, X.3    Lin, X.4    Segrest, J.P.5
  • 80
    • 0032797263 scopus 로고    scopus 로고
    • N-terminal domain of apolipoprotein B has structural homology to lipovitellin and microsomal triglyceride transfer protein: A "lipid pocket" model for self-assembly of apob-containing lipoprotein particles
    • Segrest JP, Jones MK, Dashti N. N-terminal domain of apolipoprotein B has structural homology to lipovitellin and microsomal triglyceride transfer protein: a "lipid pocket" model for self-assembly of apob-containing lipoprotein particles. J Lipid Res 1999; 40:1401-1416.
    • (1999) J Lipid Res , vol.40 , pp. 1401-1416
    • Segrest, J.P.1    Jones, M.K.2    Dashti, N.3
  • 81
    • 0035655157 scopus 로고    scopus 로고
    • Structure of apolipoprotein B-100 in low density lipoproteins
    • Segrest JP, Jones MK, De Loof H, Dashti N. Structure of apolipoprotein B-100 in low density lipoproteins. J Lipid Res 2001; 42:1346-1367.
    • (2001) J Lipid Res , vol.42 , pp. 1346-1367
    • Segrest, J.P.1    Jones, M.K.2    De Loof, H.3    Dashti, N.4
  • 82
    • 0005048104 scopus 로고    scopus 로고
    • Vitellogenesis in teleost fish
    • Göteborg, Sweden: University of Göteborg;, Thesis
    • Silversand C. Vitellogenesis in teleost fish. A study of vitellogenin and egg lipids. Göteborg, Sweden: University of Göteborg; 1996. Thesis.
    • (1996) A study of vitellogenin and egg lipids
    • Silversand, C.1
  • 83
    • 0021779490 scopus 로고
    • Induction, isolation and a characterization of the lipid content of plasma vitellogenin from two Salmo species: Rainbow trout (Salmo gairdneri) and sea trout (Salmo trutta)
    • Norberg B, Haux C. Induction, isolation and a characterization of the lipid content of plasma vitellogenin from two Salmo species: rainbow trout (Salmo gairdneri) and sea trout (Salmo trutta). Comp Biochem Physiol B 1985; 81:869-876.
    • (1985) Comp Biochem Physiol B , vol.81 , pp. 869-876
    • Norberg, B.1    Haux, C.2
  • 84
    • 0030270960 scopus 로고    scopus 로고
    • The sequence of catabolic substrate oxidation and enthalpy balance of developing embryos and yolk-sac larvae of turbot (Scophthalmus maximus L.)
    • Finn RN, Fyhn HJ, Henderson RJ, Evjen MS. The sequence of catabolic substrate oxidation and enthalpy balance of developing embryos and yolk-sac larvae of turbot (Scophthalmus maximus L.). Comp Biochem Physiol 1996; 115A:133-151.
    • (1996) Comp Biochem Physiol , vol.115 A , pp. 133-151
    • Finn, R.N.1    Fyhn, H.J.2    Henderson, R.J.3    Evjen, M.S.4
  • 85
    • 0036941770 scopus 로고    scopus 로고
    • Sequential utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of barfin flounder Verasper moseri
    • Ohkubo N, Matsubara T. Sequential utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of barfin flounder Verasper moseri. Mar Biol 2002; 140:187-196.
    • (2002) Mar Biol , vol.140 , pp. 187-196
    • Ohkubo, N.1    Matsubara, T.2
  • 86
    • 33745048986 scopus 로고    scopus 로고
    • Utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of walleye pollock Theragra chalcogramma
    • Ohkubo N, Sawaguchi S, Hamatsu T, Matsubara T. Utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of walleye pollock Theragra chalcogramma. Fish Sci 2006; 76: 620-630.
    • (2006) Fish Sci , vol.76 , pp. 620-630
    • Ohkubo, N.1    Sawaguchi, S.2    Hamatsu, T.3    Matsubara, T.4
  • 87
    • 84990504952 scopus 로고
    • Compartmental changes in total lipid, lipid classes and their associated fatty acids of developing yolk-sac larvae of Atlantic halibut (Hippoglossus hippoglossus L.)
    • Rønnestad I, Finn RN, Lein I, Lie Ø. Compartmental changes in total lipid, lipid classes and their associated fatty acids of developing yolk-sac larvae of Atlantic halibut (Hippoglossus hippoglossus L.). Aquaculture Nutrition 1995; 1:119-130.
    • (1995) Aquaculture Nutrition , vol.1 , pp. 119-130
    • Rønnestad, I.1    Finn, R.N.2    Lein, I.3    Lie, O.4
  • 88
    • 0035184222 scopus 로고    scopus 로고
    • Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss)
    • Kwon JY, Prat F, Randall C, Tyler CR. Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss). Biol Reprod 2001; 65:1701-1709.
    • (2001) Biol Reprod , vol.65 , pp. 1701-1709
    • Kwon, J.Y.1    Prat, F.2    Randall, C.3    Tyler, C.R.4
  • 89
    • 8844236823 scopus 로고    scopus 로고
    • The role of lipoprotein lipase (LPL) in the incorporation of neutral lipids into the oocytes of the European sea bass (Dicentrarchus labrax L.) during gonadal development
    • Ibañez AJ, Peinado-Onsurbe J, Sanchez E, Prat F. The role of lipoprotein lipase (LPL) in the incorporation of neutral lipids into the oocytes of the European sea bass (Dicentrarchus labrax L.) during gonadal development. Fish Physiol Biochem 2003; 28:291-293.
    • (2003) Fish Physiol Biochem , vol.28 , pp. 291-293
    • Ibañez, A.J.1    Peinado-Onsurbe, J.2    Sanchez, E.3    Prat, F.4
  • 90
    • 33646036692 scopus 로고    scopus 로고
    • Regulation of lipoprotein lipase activity in rainbow trout (Oncorhynchus mykiss) tissues
    • Albalat A, Sanchez-Gurmaches J, Gutierrez J, Navarro I. Regulation of lipoprotein lipase activity in rainbow trout (Oncorhynchus mykiss) tissues. Gen Comp Endocrinol 2006; 146:226-235.
    • (2006) Gen Comp Endocrinol , vol.146 , pp. 226-235
    • Albalat, A.1    Sanchez-Gurmaches, J.2    Gutierrez, J.3    Navarro, I.4
  • 91
    • 0023129635 scopus 로고
    • Iron binding by Phosvitins: Variable mechanism of iron release by phosvitins of diverse species characterized by different degrees of phosphorylation
    • Grogan J, Taborsky G. Iron binding by Phosvitins: variable mechanism of iron release by phosvitins of diverse species characterized by different degrees of phosphorylation. J Inorg Biochem 1987; 29:33-47.
    • (1987) J Inorg Biochem , vol.29 , pp. 33-47
    • Grogan, J.1    Taborsky, G.2
  • 93
    • 24344475974 scopus 로고    scopus 로고
    • Evolution of the transferrin family: Conservation of residues associated with iron and anion binding
    • Lambert LA, Perri H, Halbrooks PJ, Mason AB. Evolution of the transferrin family: conservation of residues associated with iron and anion binding. Comp Biochem Physiol B Biochem Mol Biol 2005; 142: 129-141.
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.142 , pp. 129-141
    • Lambert, L.A.1    Perri, H.2    Halbrooks, P.J.3    Mason, A.B.4
  • 94
    • 28944441827 scopus 로고    scopus 로고
    • Vitellogenin is a novel player in defense reactions
    • Shi X, Zhang S, Pang Q. Vitellogenin is a novel player in defense reactions. Fish Shellfish Immunol 2006; 20:769-772.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 769-772
    • Shi, X.1    Zhang, S.2    Pang, Q.3
  • 95
    • 0030917010 scopus 로고    scopus 로고
    • Liang Z, Sottrup-Jensen L, Aspan A, Hall M, Soderhall K. Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain. Proc Natl Acad Sci U S A 1997; 94:6682-6687.
    • Liang Z, Sottrup-Jensen L, Aspan A, Hall M, Soderhall K. Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain. Proc Natl Acad Sci U S A 1997; 94:6682-6687.
  • 96
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 1998; 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 97
    • 22944485726 scopus 로고    scopus 로고
    • Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion
    • Reese C, Heise F, Mayer A. Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion. Nature 2005; 436:410-414.
    • (2005) Nature , vol.436 , pp. 410-414
    • Reese, C.1    Heise, F.2    Mayer, A.3
  • 98
    • 33747192046 scopus 로고    scopus 로고
    • Membrane fusion in cells: Molecular machinery and mechanisms
    • Leabu M. Membrane fusion in cells: molecular machinery and mechanisms. J Cell Mol Med 2006; 10:423-427.
    • (2006) J Cell Mol Med , vol.10 , pp. 423-427
    • Leabu, M.1
  • 99
    • 0024289536 scopus 로고
    • Invertebrate vitellogenin is homologous to human von Willebrand factor
    • Baker ME. Invertebrate vitellogenin is homologous to human von Willebrand factor. Biochem J 1988; 256:1059-1061.
    • (1988) Biochem J , vol.256 , pp. 1059-1061
    • Baker, M.E.1
  • 100
    • 0029061297 scopus 로고
    • Precursor-product relationship between chicken vitellogenin and the yolk proteins: The 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine-rich domain of vitellogenin II
    • Yamamura J, Adachi T, Aoki N, Nakajima H, Nakamura R, Matsuda T. Precursor-product relationship between chicken vitellogenin and the yolk proteins: the 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine-rich domain of vitellogenin II. Biochim Biophys Acta 1995; 1244:384-394.
    • (1995) Biochim Biophys Acta , vol.1244 , pp. 384-394
    • Yamamura, J.1    Adachi, T.2    Aoki, N.3    Nakajima, H.4    Nakamura, R.5    Matsuda, T.6
  • 101
    • 0034601707 scopus 로고    scopus 로고
    • A zebrafish vitellogenin gene (vg3) encodes a novel vitellogenin without a phosvitin domain and may represent a primitive vertebrate vitellogenin gene
    • Wang H, Yan T, Tan JT, Gong Z. A zebrafish vitellogenin gene (vg3) encodes a novel vitellogenin without a phosvitin domain and may represent a primitive vertebrate vitellogenin gene. Gene 2000; 256:303-310.
    • (2000) Gene , vol.256 , pp. 303-310
    • Wang, H.1    Yan, T.2    Tan, J.T.3    Gong, Z.4
  • 102
    • 84993891062 scopus 로고
    • Stages of oocyte development in the zebrafish Brachydanio rerio
    • Selman K, Wallace RA, Sarka A, Qi X. Stages of oocyte development in the zebrafish Brachydanio rerio. J Morphol 1993; 218:203-224.
    • (1993) J Morphol , vol.218 , pp. 203-224
    • Selman, K.1    Wallace, R.A.2    Sarka, A.3    Qi, X.4
  • 103
    • 0018855487 scopus 로고
    • Characterization of an estradiol-induced protein from rainbow trout serum as vitellogenin by the composition and radioimmunological cross reactivity to ovarian yolk fractions
    • Campbell CM, Idler DR. Characterization of an estradiol-induced protein from rainbow trout serum as vitellogenin by the composition and radioimmunological cross reactivity to ovarian yolk fractions. Biol Reprod 1980; 22:605-617.
    • (1980) Biol Reprod , vol.22 , pp. 605-617
    • Campbell, C.M.1    Idler, D.R.2
  • 104
    • 0011954177 scopus 로고
    • Characterization of egg yolk proteins from rainbow trout Salmo gairdneri (Rich.)
    • Riazi A, Fremont L, Gozzelino MT. Characterization of egg yolk proteins from rainbow trout Salmo gairdneri (Rich.). Comp Biochem Physiol 1988; 89B:399-407.
    • (1988) Comp Biochem Physiol , vol.89 B , pp. 399-407
    • Riazi, A.1    Fremont, L.2    Gozzelino, M.T.3
  • 107
    • 0022764677 scopus 로고
    • Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit
    • Verweij CL, Diergaarde PJ, Hart M, Pannekoek H. Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit. EMBO J 1986; 5: 1839-1847.
    • (1986) EMBO J , vol.5 , pp. 1839-1847
    • Verweij, C.L.1    Diergaarde, P.J.2    Hart, M.3    Pannekoek, H.4
  • 108
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler JE. Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem 1998; 67:395-424.
    • (1998) Annu Rev Biochem , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 109
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984; 309:30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 111
    • 31744437770 scopus 로고    scopus 로고
    • The physiological function of von Willebrand's factor depends on its tubular storage in endothelial Weibel-Palade bodies
    • Michaux G, Abbitt KB, Collinson LM, Haberichter SL, Norman KE, Cutler DF. The physiological function of von Willebrand's factor depends on its tubular storage in endothelial Weibel-Palade bodies. Dev Cell 2006; 10:223-232.
    • (2006) Dev Cell , vol.10 , pp. 223-232
    • Michaux, G.1    Abbitt, K.B.2    Collinson, L.M.3    Haberichter, S.L.4    Norman, K.E.5    Cutler, D.F.6
  • 112
    • 0030987009 scopus 로고    scopus 로고
    • Primary structure of the propeptide and factor VIII-binding domain of bovine von Willebrand factor
    • Janel N, Ribba AS, Cherel G, Kerbiriou-Nabias D, Meyer D. Primary structure of the propeptide and factor VIII-binding domain of bovine von Willebrand factor. Biochim Biophys Acta 1997; 1339:4-8.
    • (1997) Biochim Biophys Acta , vol.1339 , pp. 4-8
    • Janel, N.1    Ribba, A.S.2    Cherel, G.3    Kerbiriou-Nabias, D.4    Meyer, D.5
  • 115
    • 0031010118 scopus 로고    scopus 로고
    • The carboxyl-terminal sequence of the human secretory mucin, MUC6. Analysis of the primary amino acid sequence
    • Toribara NW, Ho SB, Gum E, Gum JRJ, Lau P, Kim YS. The carboxyl-terminal sequence of the human secretory mucin, MUC6. Analysis of the primary amino acid sequence. J Biol Chem 1997; 272:16398-16403.
    • (1997) J Biol Chem , vol.272 , pp. 16398-16403
    • Toribara, N.W.1    Ho, S.B.2    Gum, E.3    Gum, J.R.J.4    Lau, P.5    Kim, Y.S.6
  • 118
    • 0037941100 scopus 로고    scopus 로고
    • Vitellogenin in carp (Cyprinus carpio) and perch (Perca fluviatilis): Purification, characterization and development of an ELISA for the detection of estrogenic effects
    • Hennies M, Wiesmann M, Allner B, Sauerwein H. Vitellogenin in carp (Cyprinus carpio) and perch (Perca fluviatilis): purification, characterization and development of an ELISA for the detection of estrogenic effects. Sci Total Environ 2003; 309:93-103.
    • (2003) Sci Total Environ , vol.309 , pp. 93-103
    • Hennies, M.1    Wiesmann, M.2    Allner, B.3    Sauerwein, H.4
  • 120
    • 0037474268 scopus 로고    scopus 로고
    • Receptor-ligand interaction between vitellogenin receptor (VtgR) and vitellogenin (Vtg), implications on low density lipoprotein receptor and apolipoprotein B/E. The first three ligand-binding repeats of VtgR interact with the amino-terminal region of Vtg
    • Li A, Sadasivam M, Ding JL. Receptor-ligand interaction between vitellogenin receptor (VtgR) and vitellogenin (Vtg), implications on low density lipoprotein receptor and apolipoprotein B/E. The first three ligand-binding repeats of VtgR interact with the amino-terminal region of Vtg. J Biol Chem 2003; 278:2799-2806.
    • (2003) J Biol Chem , vol.278 , pp. 2799-2806
    • Li, A.1    Sadasivam, M.2    Ding, J.L.3


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