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Volumn 6, Issue 7, 2011, Pages

Identification of genes directly involved in shell formation and their functions in pearl oyster, pinctada fucata

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BIOMINERALIZATION; CONTROLLED STUDY; CRYSTALLIZATION; DEVELOPMENTAL STAGE; GENE EXPRESSION; GENE FUNCTION; GENE IDENTIFICATION; GENE ISOLATION; GENE SEQUENCE; IN SITU HYBRIDIZATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PINCTADA; PINCTADA FUCATA; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SUPPRESSION SUBTRACTIVE HYBRIDIZATION; TANDEM REPEAT; UNINDEXED SEQUENCE; ANIMAL; GENETICS; HISTOLOGY; METABOLISM; MOLECULAR GENETICS; RNA INTERFERENCE;

EID: 79959806595     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021860     Document Type: Article
Times cited : (104)

References (91)
  • 1
    • 0019392575 scopus 로고
    • Minerals formed by organisms
    • Lowenstam H, (1981) Minerals formed by organisms. Science 211: 1126.
    • (1981) Science , vol.211 , pp. 1126
    • Lowenstam, H.1
  • 4
    • 31344456451 scopus 로고    scopus 로고
    • Mollusk shell formation: a source of new concepts for understanding biomineralization processes
    • Addadi L, Joester D, Nudelman F, Weiner S, (2006) Mollusk shell formation: a source of new concepts for understanding biomineralization processes. Chemistry- A European Journal 12: 980-987.
    • (2006) Chemistry - A European Journal , vol.12 , pp. 980-987
    • Addadi, L.1    Joester, D.2    Nudelman, F.3    Weiner, S.4
  • 5
    • 79959788753 scopus 로고    scopus 로고
    • Control of crystal phase switching and orientation by soluble mollusc-shell proteins
    • Belcher A, Wu X, Christensen R, Hansma P, Stucky G, et al. (1996) Control of crystal phase switching and orientation by soluble mollusc-shell proteins.
    • (1996)
    • Belcher, A.1    Wu, X.2    Christensen, R.3    Hansma, P.4    Stucky, G.5
  • 9
    • 0029667586 scopus 로고    scopus 로고
    • Control of aragonite or calcite polymorphism by mollusk shell macromolecules
    • Falini G, Albeck S, Weiner S, Addadi L, (1996) Control of aragonite or calcite polymorphism by mollusk shell macromolecules. Science 271: 67-69.
    • (1996) Science , vol.271 , pp. 67-69
    • Falini, G.1    Albeck, S.2    Weiner, S.3    Addadi, L.4
  • 10
    • 0029669273 scopus 로고    scopus 로고
    • Control of crystal phase switching and orientation by soluble mollusc-shell proteins
    • Belcher AM, Wu XH, Christensen RJ, Hansma PK, Stucky GD, et al. (1996) Control of crystal phase switching and orientation by soluble mollusc-shell proteins. Nature 381: 56-58.
    • (1996) Nature , vol.381 , pp. 56-58
    • Belcher, A.M.1    Wu, X.H.2    Christensen, R.J.3    Hansma, P.K.4    Stucky, G.D.5
  • 11
    • 0037560726 scopus 로고    scopus 로고
    • Mollusk shell acidic proteins: In search of individual functions
    • Gotliv B, Addadi L, Weiner S, (2003) Mollusk shell acidic proteins: In search of individual functions. ChemBioChem 4: 522-529.
    • (2003) ChemBioChem , vol.4 , pp. 522-529
    • Gotliv, B.1    Addadi, L.2    Weiner, S.3
  • 13
    • 0032712041 scopus 로고    scopus 로고
    • A new matrix protein family related to the nacreous layer formation of Pinctada fucata
    • Samata T, Hayashi N, Kono M, Hasegawa K, Horita C, et al. (1999) A new matrix protein family related to the nacreous layer formation of Pinctada fucata. Febs Letters 462: 225-229.
    • (1999) Febs Letters , vol.462 , pp. 225-229
    • Samata, T.1    Hayashi, N.2    Kono, M.3    Hasegawa, K.4    Horita, C.5
  • 14
    • 33846219553 scopus 로고    scopus 로고
    • A Novel Matrix Protein p10 from the Nacre of Pearl Oyster (Pinctada fucata) and Its Effects on Both CaCO3 Crystal Formation and Mineralogenic Cells
    • Zhang C, Li S, Ma Z, Xie L, Zhang R, (2006) A Novel Matrix Protein p10 from the Nacre of Pearl Oyster (Pinctada fucata) and Its Effects on Both CaCO3 Crystal Formation and Mineralogenic Cells. Marine Biotechnology 8: 624-633.
    • (2006) Marine Biotechnology , vol.8 , pp. 624-633
    • Zhang, C.1    Li, S.2    Ma, Z.3    Xie, L.4    Zhang, R.5
  • 16
    • 70249111462 scopus 로고    scopus 로고
    • An Acidic Matrix Protein, Pif, Is a Key Macromolecule for Nacre Formation
    • Suzuki M, Saruwatari K, Kogure T, Yamamoto Y, Nishimura T, et al. (2009) An Acidic Matrix Protein, Pif, Is a Key Macromolecule for Nacre Formation. Science 325: 1388-1390.
    • (2009) Science , vol.325 , pp. 1388-1390
    • Suzuki, M.1    Saruwatari, K.2    Kogure, T.3    Yamamoto, Y.4    Nishimura, T.5
  • 18
    • 4344712499 scopus 로고    scopus 로고
    • Characterization of Prismalin-14, a novel matrix protein from the prismatic layer of the Japanese pearl oyster (Pinctada fucata)
    • Suzuki M, Murayama E, Inoue H, Ozaki N, Tohse H, et al. (2004) Characterization of Prismalin-14, a novel matrix protein from the prismatic layer of the Japanese pearl oyster (Pinctada fucata). Biochemical Journal 382: 205-213.
    • (2004) Biochemical Journal , vol.382 , pp. 205-213
    • Suzuki, M.1    Murayama, E.2    Inoue, H.3    Ozaki, N.4    Tohse, H.5
  • 20
    • 33646157963 scopus 로고    scopus 로고
    • A novel matrix protein family participating in the prismatic layer framework formation of pearl oyster, Pinctada fucata
    • Zhang C, Xie L, Huang J, Liu X, Zhang R, (2006) A novel matrix protein family participating in the prismatic layer framework formation of pearl oyster, Pinctada fucata. Biochemical and Biophysical Research Communications 344: 735-740.
    • (2006) Biochemical and Biophysical Research Communications , vol.344 , pp. 735-740
    • Zhang, C.1    Xie, L.2    Huang, J.3    Liu, X.4    Zhang, R.5
  • 21
    • 67449106984 scopus 로고    scopus 로고
    • Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata
    • Kong Y, Jing G, Yan Z, Li C, Gong N, et al. (2009) Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata. Journal of Biological Chemistry 284: 10841-10854.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 10841-10854
    • Kong, Y.1    Jing, G.2    Yan, Z.3    Li, C.4    Gong, N.5
  • 22
    • 77952063125 scopus 로고    scopus 로고
    • Prismin: A New Matrix Protein Family in the Japanese Pearl Oyster (Pinctada fucata) Involved in Prismatic Layer Formation
    • Takagi R, Miyashita T, (2010) Prismin: A New Matrix Protein Family in the Japanese Pearl Oyster (Pinctada fucata) Involved in Prismatic Layer Formation. Zoological Science 27: 416-426.
    • (2010) Zoological Science , vol.27 , pp. 416-426
    • Takagi, R.1    Miyashita, T.2
  • 24
    • 0001398629 scopus 로고    scopus 로고
    • Occurrence of mineralization disturbances in nacreous layers of cultivated pearls produced by Pinctada margaritifera var. cumingi from French Polynesia. Comparison with reported shell alterations
    • Cuif J-P, Dauphin Y, (1996) Occurrence of mineralization disturbances in nacreous layers of cultivated pearls produced by Pinctada margaritifera var. cumingi from French Polynesia. Comparison with reported shell alterations. Aquat Living Resour 9: 187-193.
    • (1996) Aquat Living Resour , vol.9 , pp. 187-193
    • Cuif, J.-P.1    Dauphin, Y.2
  • 25
    • 63649117154 scopus 로고    scopus 로고
    • Nucleation and growth of aragonite crystals at the growth front of nacres in pearl oyster, Pinctada fucata
    • Saruwatari K, Matsui T, Mukai H, Nagasawa H, Kogure T, (2009) Nucleation and growth of aragonite crystals at the growth front of nacres in pearl oyster, Pinctada fucata. Biomaterials 30: 3028-3034.
    • (2009) Biomaterials , vol.30 , pp. 3028-3034
    • Saruwatari, K.1    Matsui, T.2    Mukai, H.3    Nagasawa, H.4    Kogure, T.5
  • 26
    • 41149174600 scopus 로고    scopus 로고
    • Structure and composition of the nacre-prisms transition in the shell of Pinctada margaritifera (Mollusca, Bivalvia)
    • Dauphin Y, Ball A, Cotte M, Cuif J-P, Meibom A, et al. (2008) Structure and composition of the nacre-prisms transition in the shell of Pinctada margaritifera (Mollusca, Bivalvia). Analytical and Bioanalytical Chemistry 390: 1659-1669.
    • (2008) Analytical and Bioanalytical Chemistry , vol.390 , pp. 1659-1669
    • Dauphin, Y.1    Ball, A.2    Cotte, M.3    Cuif, J.-P.4    Meibom, A.5
  • 28
    • 35348886006 scopus 로고    scopus 로고
    • Molluscan shell proteins: Primary structure, origin, and evolution
    • San Diego, Elsevier Academic Press Inc
    • Marin F, Luquet G, Marie B, Medakovic D, (2008) Molluscan shell proteins: Primary structure, origin, and evolution. Current Topics in Developmental Biology, Vol 80 San Diego Elsevier Academic Press Inc pp. 209-276.
    • (2008) Current Topics in Developmental Biology , vol.80 , pp. 209-276
    • Marin, F.1    Luquet, G.2    Marie, B.3    Medakovic, D.4
  • 29
    • 33644990126 scopus 로고    scopus 로고
    • The chitin synthase involved in marine bivalve mollusk shell formation contains a myosin domain
    • Weiss IM, Schönitzer V, Eichner N, Sumper M, (2006) The chitin synthase involved in marine bivalve mollusk shell formation contains a myosin domain. FEBS Letters 580: 1846-1852.
    • (2006) FEBS Letters , vol.580 , pp. 1846-1852
    • Weiss, I.M.1    Schönitzer, V.2    Eichner, N.3    Sumper, M.4
  • 30
    • 0038010062 scopus 로고    scopus 로고
    • Development of calcareous skeletal elements in invertebrates
    • Wilt FH, Killian CE, Livingston BT, (2003) Development of calcareous skeletal elements in invertebrates. Differentiation 71: 237-250.
    • (2003) Differentiation , vol.71 , pp. 237-250
    • Wilt, F.H.1    Killian, C.E.2    Livingston, B.T.3
  • 31
    • 0042316895 scopus 로고
    • PURIFICATION AND CHARACTERIZATION OF CALCIUM-BINDING CONCHIOLIN SHELL PEPTIDES FROM THE MOLLUSK, HALIOTIS-RUFESCENS, AS A FUNCTION OF DEVELOPMENT
    • Cariolou MA, Morse DE, (1988) PURIFICATION AND CHARACTERIZATION OF CALCIUM-BINDING CONCHIOLIN SHELL PEPTIDES FROM THE MOLLUSK, HALIOTIS-RUFESCENS, AS A FUNCTION OF DEVELOPMENT. Journal of Comparative Physiology B-Biochemical Systemic and Environmental Physiology 157: 717-729.
    • (1988) Journal of Comparative Physiology B-Biochemical Systemic and Environmental Physiology , vol.157 , pp. 717-729
    • Cariolou, M.A.1    Morse, D.E.2
  • 32
    • 0018629874 scopus 로고
    • ASPARTIC ACID-RICH PROTEINS - MAJOR COMPONENTS OF THE SOLUBLE ORGANIC MATRIX OF MOLLUSK SHELLS
    • Weiner S, (1979) ASPARTIC ACID-RICH PROTEINS- MAJOR COMPONENTS OF THE SOLUBLE ORGANIC MATRIX OF MOLLUSK SHELLS. Calcified Tissue International 29: 163-167.
    • (1979) Calcified Tissue International , vol.29 , pp. 163-167
    • Weiner, S.1
  • 33
    • 34548187477 scopus 로고    scopus 로고
    • A Novel Extrapallial Fluid Protein Controls the Morphology of Nacre Lamellae in the Pearl Oyster, Pinctada fucata
    • Ma Z, Huang J, Sun J, Wang G, Li C, et al. (2007) A Novel Extrapallial Fluid Protein Controls the Morphology of Nacre Lamellae in the Pearl Oyster, Pinctada fucata. Journal of Biological Chemistry 282: 23253-23263.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 23253-23263
    • Ma, Z.1    Huang, J.2    Sun, J.3    Wang, G.4    Li, C.5
  • 35
    • 0028094036 scopus 로고
    • Larval and Spat Culture of the Western-Australian Silverlip or Goldlip Pearl Oyster, Pinctada-Maxima Jameson (Mollusca, Pteriidae)
    • Rose RA, Baker SB, (1994) Larval and Spat Culture of the Western-Australian Silverlip or Goldlip Pearl Oyster, Pinctada-Maxima Jameson (Mollusca, Pteriidae). Aquaculture 126: 35-50.
    • (1994) Aquaculture , vol.126 , pp. 35-50
    • Rose, R.A.1    Baker, S.B.2
  • 37
    • 35349000604 scopus 로고    scopus 로고
    • Dynamic expression of ancient and novel molluscan shell genes during ecological transitions
    • Jackson D, Worheide G, Degnan B, (2007) Dynamic expression of ancient and novel molluscan shell genes during ecological transitions. Bmc Evolutionary Biology 7: 160.
    • (2007) Bmc Evolutionary Biology , vol.7 , pp. 160
    • Jackson, D.1    Worheide, G.2    Degnan, B.3
  • 38
    • 78650970565 scopus 로고    scopus 로고
    • Larval Connectivity in an Effective Network of Marine Protected Areas
    • Christie MR, Tissot BN, Albins MA, Beets JP, Jia Y, et al. (2010) Larval Connectivity in an Effective Network of Marine Protected Areas. PLoS ONE 5: e15715.
    • (2010) PLoS ONE , vol.5
    • Christie, M.R.1    Tissot, B.N.2    Albins, M.A.3    Beets, J.P.4    Jia, Y.5
  • 39
  • 40
    • 77956273436 scopus 로고    scopus 로고
    • Molecules Clarify a Cnidarian Life Cycle - The "Hydrozoan" Microhydrula limopsicola Is an Early Life Stage of the Staurozoan Haliclystus antarcticus
    • Miranda LS, Collins AG, Marques AC, (2010) Molecules Clarify a Cnidarian Life Cycle - The "Hydrozoan" Microhydrula limopsicola Is an Early Life Stage of the Staurozoan Haliclystus antarcticus. PLoS ONE 5: e10182.
    • (2010) PLoS ONE , vol.5
    • Miranda, L.S.1    Collins, A.G.2    Marques, A.C.3
  • 41
    • 33748607987 scopus 로고    scopus 로고
    • Comparative phylogeography of coastal limpets across a marine disjunction in New Zealand
    • Goldstien SJ, Schiel DR, Gemmell NJ, (2006) Comparative phylogeography of coastal limpets across a marine disjunction in New Zealand. Molecular Ecology 15: 3259-3268.
    • (2006) Molecular Ecology , vol.15 , pp. 3259-3268
    • Goldstien, S.J.1    Schiel, D.R.2    Gemmell, N.J.3
  • 42
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research
    • Conesa A, Götz S, García-Gómez JM, Terol J, Talón M, et al. Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics 21: 3674-3676.
    • Bioinformatics , vol.21 , pp. 3674-3676
    • Conesa, A.1    Götz, S.2    García-Gómez, J.M.3    Terol, J.4    Talón, M.5
  • 44
    • 58849135305 scopus 로고    scopus 로고
    • Using functional genomics to explore the effects of ocean acidification on calcifying marine organisms
    • Hofmann GE, O'Donnell MJ, Todgham AE, (2008) Using functional genomics to explore the effects of ocean acidification on calcifying marine organisms. Marine Ecology-Progress Series 373: 219-225.
    • (2008) Marine Ecology-Progress Series , vol.373 , pp. 219-225
    • Hofmann, G.E.1    O'Donnell, M.J.2    Todgham, A.E.3
  • 45
    • 34548417129 scopus 로고    scopus 로고
    • Identification of chitin in the prismatic layer of the shell and a chitin synthase gene from the Japanese pearl oyster, Pinctada fucata
    • Suzuki M, Sakuda S, Nagasawa H, (2007) Identification of chitin in the prismatic layer of the shell and a chitin synthase gene from the Japanese pearl oyster, Pinctada fucata. Bioscience Biotechnology and Biochemistry 71: 1735-1744.
    • (2007) Bioscience Biotechnology and Biochemistry , vol.71 , pp. 1735-1744
    • Suzuki, M.1    Sakuda, S.2    Nagasawa, H.3
  • 46
    • 39049142881 scopus 로고    scopus 로고
    • The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
    • Schonitzer V, Weiss IM, (2007) The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z. Bmc Structural Biology 7.
    • (2007) Bmc Structural Biology , vol.7
    • Schonitzer, V.1    Weiss, I.M.2
  • 47
    • 33644990126 scopus 로고    scopus 로고
    • The chitin synthase involved in marine bivalve mollusk shell formation contains a myosin domain
    • Weiss IM, Schonitzer V, Eichner N, Sumper M, (2006) The chitin synthase involved in marine bivalve mollusk shell formation contains a myosin domain. Febs Letters 580: 1846-1852.
    • (2006) Febs Letters , vol.580 , pp. 1846-1852
    • Weiss, I.M.1    Schonitzer, V.2    Eichner, N.3    Sumper, M.4
  • 48
    • 32544461746 scopus 로고    scopus 로고
    • The distribution of chitin in larval shells of the bivalve mollusk Mytilus galloprovincialis
    • Weiss IM, Schonitzer V, (2006) The distribution of chitin in larval shells of the bivalve mollusk Mytilus galloprovincialis. Journal of Structural Biology 153: 264-277.
    • (2006) Journal of Structural Biology , vol.153 , pp. 264-277
    • Weiss, I.M.1    Schonitzer, V.2
  • 49
    • 20544452200 scopus 로고    scopus 로고
    • Four differentially expressed cDNAs in Callinectes sapidus containing the Rebers-Riddiford consensus sequence
    • Wynn A, Shafer TH, (2005) Four differentially expressed cDNAs in Callinectes sapidus containing the Rebers-Riddiford consensus sequence. Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology 141: 294-306.
    • (2005) Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology , vol.141 , pp. 294-306
    • Wynn, A.1    Shafer, T.H.2
  • 51
    • 77953963182 scopus 로고    scopus 로고
    • Mineralisation of reconstituted collagen using polyvinylphosphonic acid/polyacrylic acid templating matrix protein analogues in the presence of calcium, phosphate and hydroxyl ions
    • Kim YK, Gu LS, Bryan TE, Kim JR, Chen LA, et al. (2010) Mineralisation of reconstituted collagen using polyvinylphosphonic acid/polyacrylic acid templating matrix protein analogues in the presence of calcium, phosphate and hydroxyl ions. Biomaterials 31: 6618-6627.
    • (2010) Biomaterials , vol.31 , pp. 6618-6627
    • Kim, Y.K.1    Gu, L.S.2    Bryan, T.E.3    Kim, J.R.4    Chen, L.A.5
  • 52
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink JD, Beniash E, Stupp SI, (2001) Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 294: 1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 54
    • 0022515323 scopus 로고
    • The organic matrix of the skeletal spicule of sea-urchin embryos
    • Benson SC, Benson NC, Wilt F, (1986) The organic matrix of the skeletal spicule of sea-urchin embryos. Journal of Cell Biology 102: 1878-1886.
    • (1986) Journal of Cell Biology , vol.102 , pp. 1878-1886
    • Benson, S.C.1    Benson, N.C.2    Wilt, F.3
  • 56
    • 1242284204 scopus 로고    scopus 로고
    • Ostrich (Struthio camelus) eggshell matrix contains two different C-type lectin-like proteins. Isolation, amino acid sequence, and posttranslational modifications
    • Mann K, Siedler F, (2004) Ostrich (Struthio camelus) eggshell matrix contains two different C-type lectin-like proteins. Isolation, amino acid sequence, and posttranslational modifications. Biochimica Et Biophysica Acta-Proteins and Proteomics 1696: 41-50.
    • (2004) Biochimica Et Biophysica Acta-Proteins and Proteomics , vol.1696 , pp. 41-50
    • Mann, K.1    Siedler, F.2
  • 57
    • 12244259068 scopus 로고    scopus 로고
    • Identification and developmental expression of new biomineralization proteins in the sea urchin Strongylocentrotus purpuratus
    • Illies MR, Peeler MT, Dechtiaruk AM, Ettensohn CA, (2002) Identification and developmental expression of new biomineralization proteins in the sea urchin Strongylocentrotus purpuratus. Development Genes and Evolution 212: 419-431.
    • (2002) Development Genes and Evolution , vol.212 , pp. 419-431
    • Illies, M.R.1    Peeler, M.T.2    Dechtiaruk, A.M.3    Ettensohn, C.A.4
  • 58
    • 0034614599 scopus 로고    scopus 로고
    • Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata
    • Weiss IM, Kaufmann S, Mann K, Fritz M, (2000) Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata. Biochemical and Biophysical Research Communications 267: 17-21.
    • (2000) Biochemical and Biophysical Research Communications , vol.267 , pp. 17-21
    • Weiss, I.M.1    Kaufmann, S.2    Mann, K.3    Fritz, M.4
  • 60
    • 34547131564 scopus 로고    scopus 로고
    • Formation of hydroxyapatite provides a tunable protein reservoir within porous polyester membranes by an improved soaking process
    • Watanabe J, Akashi M, (2007) Formation of hydroxyapatite provides a tunable protein reservoir within porous polyester membranes by an improved soaking process. Biomacromolecules 8: 2288-2293.
    • (2007) Biomacromolecules , vol.8 , pp. 2288-2293
    • Watanabe, J.1    Akashi, M.2
  • 61
    • 0036230097 scopus 로고    scopus 로고
    • Effect of albumin and fibrinogen on calcium phosphate formation on sol-gel-derived titania coatings in vitro
    • Areva S, Peltola T, Sailynoja E, Laajalehto K, Linden M, et al. (2002) Effect of albumin and fibrinogen on calcium phosphate formation on sol-gel-derived titania coatings in vitro. Chemistry of Materials 14: 1614-1621.
    • (2002) Chemistry of Materials , vol.14 , pp. 1614-1621
    • Areva, S.1    Peltola, T.2    Sailynoja, E.3    Laajalehto, K.4    Linden, M.5
  • 63
    • 42549158036 scopus 로고    scopus 로고
    • Localization of calmodulin and calmodulin-like protein and their functions in biomineralization in P. fucata
    • Fang Z, Yan ZG, Li S, Wang Q, Cao WZ, et al. (2008) Localization of calmodulin and calmodulin-like protein and their functions in biomineralization in P. fucata. Progress in Natural Science 18: 405-412.
    • (2008) Progress in Natural Science , vol.18 , pp. 405-412
    • Fang, Z.1    Yan, Z.G.2    Li, S.3    Wang, Q.4    Cao, W.Z.5
  • 66
    • 3142638636 scopus 로고    scopus 로고
    • Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (Pinctada fucata)
    • Li S, Xie LP, Zhang C, Zhang Y, Gu MZ, et al. (2004) Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (Pinctada fucata). Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology 138: 235-243.
    • (2004) Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology , vol.138 , pp. 235-243
    • Li, S.1    Xie, L.P.2    Zhang, C.3    Zhang, Y.4    Gu, M.Z.5
  • 68
    • 0035423282 scopus 로고    scopus 로고
    • Fabrication of a two-dimensional array of nano-particles using ferritin molecule
    • Yamashita I, (2001) Fabrication of a two-dimensional array of nano-particles using ferritin molecule. Thin Solid Films 393: 12-18.
    • (2001) Thin Solid Films , vol.393 , pp. 12-18
    • Yamashita, I.1
  • 69
    • 0030286437 scopus 로고    scopus 로고
    • Biomimetic synthesis of cadmium sulfide-ferritin nanocomposites
    • Wong KKW, Mann S, (1996) Biomimetic synthesis of cadmium sulfide-ferritin nanocomposites. Advanced Materials 8: 928-&.
    • (1996) Advanced Materials , vol.8 , pp. 928
    • Wong, K.K.W.1    Mann, S.2
  • 70
    • 0030020621 scopus 로고    scopus 로고
    • Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres
    • Santambrogio P, Levi S, Cozzi A, Corsi B, Arosio P, (1996) Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres. Biochemical Journal 314: 139-144.
    • (1996) Biochemical Journal , vol.314 , pp. 139-144
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Corsi, B.4    Arosio, P.5
  • 71
    • 0000647993 scopus 로고
    • Synthesis, structure, and electronic-properties of a mixed-valent dodecairon oxo complex, a model for the biomineralization of ferritin
    • Taft KL, Papaefthymiou GC, Lippard SJ, (1994) Synthesis, structure, and electronic-properties of a mixed-valent dodecairon oxo complex, a model for the biomineralization of ferritin. Inorganic Chemistry 33: 1510-1520.
    • (1994) Inorganic Chemistry , vol.33 , pp. 1510-1520
    • Taft, K.L.1    Papaefthymiou, G.C.2    Lippard, S.J.3
  • 73
    • 40749102414 scopus 로고    scopus 로고
    • XSTREAM: A practical algorithm for identification and architecture modeling of tandem repeats in protein sequences
    • Newman A, Cooper J, (2007) XSTREAM: A practical algorithm for identification and architecture modeling of tandem repeats in protein sequences. BMC Bioinformatics 8: 382.
    • (2007) BMC Bioinformatics , vol.8 , pp. 382
    • Newman, A.1    Cooper, J.2
  • 74
    • 77953125691 scopus 로고    scopus 로고
    • Insights into shell deposition in the Antarctic bivalve Laternula elliptica: gene discovery in the mantle transcriptome using 454 pyrosequencing
    • Clark MS, Thorne MAS, Vieira FA, Cardoso JCR, Power DM, et al. (2010) Insights into shell deposition in the Antarctic bivalve Laternula elliptica: gene discovery in the mantle transcriptome using 454 pyrosequencing. Bmc Genomics 11.
    • (2010) Bmc Genomics , vol.11
    • Clark, M.S.1    Thorne, M.A.S.2    Vieira, F.A.3    Cardoso, J.C.R.4    Power, D.M.5
  • 76
  • 77
    • 34250015780 scopus 로고    scopus 로고
    • Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon
    • Leu J-H, Chang C-C, Wu J-L, Hsu C-W, Hirono I, et al. (2007) Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon. Bmc Genomics 8: 120.
    • (2007) Bmc Genomics , vol.8 , pp. 120
    • Leu, J.-H.1    Chang, C.-C.2    Wu, J.-L.3    Hsu, C.-W.4    Hirono, I.5
  • 79
    • 79959810436 scopus 로고    scopus 로고
    • Functional characterization of KRMP-3, a shell matrix protein of Pinctada fucata Tsinghua University
    • Jian L, (2009) Functional characterization of KRMP-3, a shell matrix protein of Pinctada fucata Tsinghua University.
    • (2009)
    • Jian, L.1
  • 80
    • 2442647473 scopus 로고    scopus 로고
    • Evolution of hard-tissue mineralization: comparison of the inner skeletal system and the outer shell system
    • Matsushiro A, Miyashita T, (2004) Evolution of hard-tissue mineralization: comparison of the inner skeletal system and the outer shell system. Journal of Bone and Mineral Metabolism 22: 163-169.
    • (2004) Journal of Bone and Mineral Metabolism , vol.22 , pp. 163-169
    • Matsushiro, A.1    Miyashita, T.2
  • 82
    • 4344712499 scopus 로고    scopus 로고
    • Characterization of Prismalin-14, a novel matrix protein from the prismatic layer of the Japanese pearl oyster (Pinctada fucata)
    • Suzuki M, Murayama E, Inoue H, Ozaki N, Tohse H, et al. (2004) Characterization of Prismalin-14, a novel matrix protein from the prismatic layer of the Japanese pearl oyster (Pinctada fucata). Biochemical Journal 382: 205.
    • (2004) Biochemical Journal , vol.382 , pp. 205
    • Suzuki, M.1    Murayama, E.2    Inoue, H.3    Ozaki, N.4    Tohse, H.5
  • 83
    • 0036638632 scopus 로고    scopus 로고
    • Identical carbonic anhydrase contributes to nacreous or prismatic layer formation in Pinctada fucata (Mollusca: Bivalvia)
    • Miyashita T, Takagi R, Miyamoto H, Matsushiro A, (2002) Identical carbonic anhydrase contributes to nacreous or prismatic layer formation in Pinctada fucata (Mollusca: Bivalvia). The Veliger 45: 250-255.
    • (2002) The Veliger , vol.45 , pp. 250-255
    • Miyashita, T.1    Takagi, R.2    Miyamoto, H.3    Matsushiro, A.4
  • 84
    • 51549108284 scopus 로고    scopus 로고
    • Immunolocalization of matrix proteins in nacre lamellae and their in vivo effects on aragonitic tablet growth
    • Gong N, Shangguan J, Liu X, Yan Z, Ma Z, et al. (2008) Immunolocalization of matrix proteins in nacre lamellae and their in vivo effects on aragonitic tablet growth. Journal of Structural Biology 164: 33-40.
    • (2008) Journal of Structural Biology , vol.164 , pp. 33-40
    • Gong, N.1    Shangguan, J.2    Liu, X.3    Yan, Z.4    Ma, Z.5
  • 85
    • 0037460985 scopus 로고    scopus 로고
    • TIGR Gene Indices clustering tools (TGICL): a software system for fast clustering of large EST datasets
    • Pertea G, Huang X, Liang F, Antonescu V, Sultana R, et al. (2003) TIGR Gene Indices clustering tools (TGICL): a software system for fast clustering of large EST datasets. Bioinformatics 19: 651-652.
    • (2003) Bioinformatics , vol.19 , pp. 651-652
    • Pertea, G.1    Huang, X.2    Liang, F.3    Antonescu, V.4    Sultana, R.5
  • 86
    • 0033290515 scopus 로고    scopus 로고
    • ESTScan: a program for detecting, evaluating, and reconstructing potential coding regions in EST sequences
    • Iseli C, Jongeneel CV, Bucher P, (1999) ESTScan: a program for detecting, evaluating, and reconstructing potential coding regions in EST sequences. Proc Int Conf Intell Syst Mol Biol pp. 138-148.
    • (1999) Proc Int Conf Intell Syst Mol Biol , pp. 138-148
    • Iseli, C.1    Jongeneel, C.V.2    Bucher, P.3
  • 88
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G, (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. Journal of Molecular Biology 300: 1005-1016.
    • (2000) Journal of Molecular Biology , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 89
    • 0033600935 scopus 로고    scopus 로고
    • Prediction of potential GPI-modification sites in proprotein sequences
    • Eisenhaber B, Bork P, Eisenhaber F, (1999) Prediction of potential GPI-modification sites in proprotein sequences. Journal of Molecular Biology 292: 741-758.
    • (1999) Journal of Molecular Biology , vol.292 , pp. 741-758
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 90
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H, (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protocols 2: 953-971.
    • (2007) Nat Protocols , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 91
    • 0035793844 scopus 로고    scopus 로고
    • Immunohistochemical and in situ hybridization studies of gonadotropin releasing hormone (GnRH) and its receptor in rat digestive tract
    • Weiquan H, Bing Y, Lan S, RuoLei P, Lei W, et al. (2001) Immunohistochemical and in situ hybridization studies of gonadotropin releasing hormone (GnRH) and its receptor in rat digestive tract. Life Sciences 68: 1727-1734.
    • (2001) Life Sciences , vol.68 , pp. 1727-1734
    • Weiquan, H.1    Bing, Y.2    Lan, S.3    RuoLei, P.4    Lei, W.5


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