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Volumn 9, Issue 2, 2014, Pages

Quantitative proteomics study of larval settlement in the barnacle Balanus amphitrite

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EID: 84895815967     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0088744     Document Type: Article
Times cited : (36)

References (83)
  • 1
    • 0033562159 scopus 로고    scopus 로고
    • Larval settlement of polychaetes
    • Qian PY (1999) Larval settlement of polychaetes. Hydrobiologia 402: 239-253.
    • (1999) Hydrobiologia , vol.402 , pp. 239-253
    • Qian, P.Y.1
  • 3
    • 35548965629 scopus 로고    scopus 로고
    • Nitric oxide inhibits metamorphosis in larvae of Crepidula fornicata, the slippershell snail
    • Pechenik JA, Cochrane DE, Li W, West ET, Pires A, et al. (2007) Nitric oxide inhibits metamorphosis in larvae of Crepidula fornicata, the slippershell snail. Biol Bull 213: 160-171. (Pubitemid 350004409)
    • (2007) Biological Bulletin , vol.213 , Issue.2 , pp. 160-171
    • Pechenik, J.A.1    Cochrane, D.E.2    Li, W.3    West, E.T.4    Pires, A.5    Leppo, M.6
  • 4
    • 0035339386 scopus 로고    scopus 로고
    • Regulation of metamorphosis in ascidians involves NO/cGMP signaling and HSP90
    • DOI 10.1002/jez.1019
    • Bishop CD, Bates WR, Brandhorst BP (2001) Regulation of metamorphosis in ascidians involves NO/cGMP signaling and HSP90. J Exp Zool 289: 374-384. (Pubitemid 32437223)
    • (2001) Journal of Experimental Zoology , vol.289 , Issue.6 , pp. 374-384
    • Bishop, C.D.1    Bates, W.R.2    Brandhorst, B.P.3
  • 5
    • 79960901079 scopus 로고    scopus 로고
    • Toward an understanding of the molecular mechanisms of barnacle larval settlement: A comparative transcriptomic approach
    • Chen Z-F, Matsumura K, Wang H, Arellano SM, Yan X, et al. (2011) Toward an understanding of the molecular mechanisms of barnacle larval settlement: a comparative transcriptomic approach. PLoS One 6: e22913.
    • (2011) PLoS One , vol.6
    • Chen, Z.-F.1    Matsumura, K.2    Wang, H.3    Arellano, S.M.4    Yan, X.5
  • 6
    • 0006968375 scopus 로고
    • Early settlement and metamorphosis of the barnacle Balanus amphitrite niveus
    • Bernard FJ, Lane CE (1962) Early settlement and metamorphosis of the barnacle Balanus amphitrite niveus. J Morphol 110: 19-39.
    • (1962) J Morphol , vol.110 , pp. 19-39
    • Bernard, F.J.1    Lane, C.E.2
  • 7
    • 33750951419 scopus 로고    scopus 로고
    • Signaling mechanisms underlying metamorphic transitions in animals
    • DOI 10.1093/icb/icl023
    • Heyland A, Moroz LL (2006) Signaling mechanisms underlying metamorphic transitions in animals. Integr Comp Biol 46: 743-759. (Pubitemid 44736414)
    • (2006) Integrative and Comparative Biology , vol.46 , Issue.6 , pp. 743-759
    • Heyland, A.1    Moroz, L.L.2
  • 8
    • 0034732982 scopus 로고    scopus 로고
    • Structures of six cDNAs expressed specifically at cypris larvae of barnacles, Balanus amphitrite
    • DOI 10.1016/S0378-1119(00)00184-0, PII S0378111900001840
    • Okazaki Y, Shizuri Y (2000) Structures of six cDNAs expressed specifically at cypris larvae of barnacles, Balanus amphitrite . Gene 250: 127-135. (Pubitemid 30347487)
    • (2000) Gene , vol.250 , Issue.1-2 , pp. 127-135
    • Okazaki, Y.1    Shizuri, Y.2
  • 9
    • 77956012999 scopus 로고    scopus 로고
    • Response of cyprid specific genes to natural settlement cues in the barnacle Balanus (= Amphibalanus) amphitrite
    • Li H, Thiyagarajan V, Qian P-Y (2010) Response of cyprid specific genes to natural settlement cues in the barnacle Balanus (= Amphibalanus) amphitrite. J Exp Mar Biol Ecol 389: 45-52.
    • (2010) J Exp Mar Biol Ecol , vol.389 , pp. 45-52
    • Li, H.1    Thiyagarajan, V.2    Qian, P.-Y.3
  • 10
    • 49749105216 scopus 로고    scopus 로고
    • Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite
    • Thiyagarajan V, Qian PY (2008) Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite. Proteomics 8: 3164-3172.
    • (2008) Proteomics , vol.8 , pp. 3164-3172
    • Thiyagarajan, V.1    Qian, P.Y.2
  • 11
    • 77954617032 scopus 로고    scopus 로고
    • Comparative proteome and phosphoproteome analyses during cyprid development of the barnacle Balanus (= Amphibalanus) amphitrite
    • Zhang Y, Xu Y, Arellano SM, Xiao K, Qian P-Y (2010) Comparative proteome and phosphoproteome analyses during cyprid development of the barnacle Balanus (= Amphibalanus) amphitrite . J Proteome Res 9: 3146-3157.
    • (2010) J Proteome Res , vol.9 , pp. 3146-3157
    • Zhang, Y.1    Xu, Y.2    Arellano, S.M.3    Xiao, K.4    Qian, P.-Y.5
  • 13
    • 77955620945 scopus 로고    scopus 로고
    • Rapid transcriptome and proteome profiling of a non-model marine invertebrate, Bugula neritina
    • Wang H, Zhang H, Wong YH, Voolstra C, Ravasi T, et al. (2010) Rapid transcriptome and proteome profiling of a non-model marine invertebrate, Bugula neritina. Proteomics 10: 2972-2981.
    • (2010) Proteomics , vol.10 , pp. 2972-2981
    • Wang, H.1    Zhang, H.2    Wong, Y.H.3    Voolstra, C.4    Ravasi, T.5
  • 14
    • 58149129875 scopus 로고    scopus 로고
    • One-step procedure for peptide extraction from in-gel digestion sample for mass spectrometric analysis
    • Meng W, Zhang H, Guo T, Pandey C, Zhu Y, et al. (2008) One-step procedure for peptide extraction from in-gel digestion sample for mass spectrometric analysis. Anal Chem 80: 9797-9805.
    • (2008) Anal Chem , vol.80 , pp. 9797-9805
    • Meng, W.1    Zhang, H.2    Guo, T.3    Pandey, C.4    Zhu, Y.5
  • 15
    • 77955116989 scopus 로고    scopus 로고
    • Study of monocyte membrane proteome perturbation during lipopolysaccharide-induced tolerance using iTRAQ-based quantitative proteomic approach
    • Zhang H, Zhao C, Li X, Zhu Y, Gan CS, et al. (2010) Study of monocyte membrane proteome perturbation during lipopolysaccharide-induced tolerance using iTRAQ-based quantitative proteomic approach. Proteomics 10: 2780-2789.
    • (2010) Proteomics , vol.10 , pp. 2780-2789
    • Zhang, H.1    Zhao, C.2    Li, X.3    Zhu, Y.4    Gan, C.S.5
  • 16
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • DOI 10.1021/ac025747h
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74: 5383-5392. (Pubitemid 35215372)
    • (2002) Analytical Chemistry , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 17
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • DOI 10.1021/ac0341261
    • Nesvizhskii AI, Keller A, Kolker E, Aebersold R (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75: 4646-4658. (Pubitemid 37082259)
    • (2003) Analytical Chemistry , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 18
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • DOI 10.1038/nbt1270, PII NBT1270
    • Lu P, Vogel C, Wang R, Yao X, Marcotte EM (2007) Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25: 117-124. (Pubitemid 46087910)
    • (2007) Nature Biotechnology , vol.25 , Issue.1 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 19
    • 60649101258 scopus 로고    scopus 로고
    • The APEX quantitative proteomics tool: Generating protein quantitation estimates from LC-MS/MS proteomics results
    • Braisted JC, Kuntumalla S, Vogel C, Marcotte EM, Rodrigues AR, et al. (2008) The APEX quantitative proteomics tool: generating protein quantitation estimates from LC-MS/MS proteomics results. Bmc Bioinformatics 9: 529.
    • (2008) Bmc Bioinformatics , vol.9 , pp. 529
    • Braisted, J.C.1    Kuntumalla, S.2    Vogel, C.3    Marcotte, E.M.4    Rodrigues, A.R.5
  • 20
    • 79951533733 scopus 로고    scopus 로고
    • Quantitative proteomics identify molecular targets that are crucial in larval settlement and metamorphosis of Bugula neritina
    • Zhang H, Wong YH, Wang H, Chen Z, Arellano SM, et al. (2010) Quantitative proteomics identify molecular targets that are crucial in larval settlement and metamorphosis of Bugula neritina. J Proteome Res 10: 349-360.
    • (2010) J Proteome Res , vol.10 , pp. 349-360
    • Zhang, H.1    Wong, Y.H.2    Wang, H.3    Chen, Z.4    Arellano, S.M.5
  • 21
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Research 32: 1792-1797.
    • (2004) Nucleic Acids Research , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 23
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Rozen S, Skaletsky H (2000) Primer3 on the WWW for general users and for biologist programmers. Methods Mol Biol 132: 365-386.
    • (2000) Methods Mol Biol , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 24
    • 67651222479 scopus 로고    scopus 로고
    • Construction of an adult barnacle (Balanus amphitrite) cDNA library and selection of reference genes for quantitative RT-PCR studies
    • De Gregoris TB, Borra M, Biffali E, Bekel T, Burgess JG, et al. (2009) Construction of an adult barnacle (Balanus amphitrite) cDNA library and selection of reference genes for quantitative RT-PCR studies. BMC Mol Biol 10: 62.
    • (2009) BMC Mol Biol , vol.10 , pp. 62
    • De Gregoris, T.B.1    Borra, M.2    Biffali, E.3    Bekel, T.4    Burgess, J.G.5
  • 25
    • 0035710746 scopus 로고    scopus 로고
    • -DDCT method
    • DOI 10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 22DDct method. Methods 25: 402-408. (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 26
    • 84887994415 scopus 로고    scopus 로고
    • Inhibitory effect of sanguinarine on PKC-CPI-17 pathway mediating by muscarinic receptors in dispersed intestinal smooth muscle cells
    • Wang H, Yin G, Yu C, Wang Y, Sun Z (2013) Inhibitory effect of sanguinarine on PKC-CPI-17 pathway mediating by muscarinic receptors in dispersed intestinal smooth muscle cells. Res Vet Sci 95: 1125-1133.
    • (2013) Res Vet Sci , vol.95 , pp. 1125-1133
    • Wang, H.1    Yin, G.2    Yu, C.3    Wang, Y.4    Sun, Z.5
  • 27
    • 1942453616 scopus 로고    scopus 로고
    • Glycolysis and Gluconeogenesis
    • Chapter 16, 5th edition. New York: W H Freeman
    • Berg JM, Tymoczko JL, Stryer L (2002) Chapter 16, Glycolysis and Gluconeogenesis. Biochemistry. 5th edition. New York: W H Freeman.
    • (2002) Biochemistry
    • Berg, J.M.1    Tymoczko, J.L.2    Stryer, L.3
  • 28
    • 0001384212 scopus 로고
    • An energy budget for the free-swimming and metamorphosing larvae of Balanus balanoides (Crustacea: Cirripedia)
    • Lucas MI, Walker G, Holland DL, Crisp DJ (1979) An energy budget for the free-swimming and metamorphosing larvae of Balanus balanoides (Crustacea: Cirripedia). Mar Biol 55: 221-229.
    • (1979) Mar Biol , vol.55 , pp. 221-229
    • Lucas, M.I.1    Walker, G.2    Holland, D.L.3    Crisp, D.J.4
  • 29
    • 84862572540 scopus 로고    scopus 로고
    • Butenolide inhibits marine fouling by altering the primary metabolism of three target organisms
    • Zhang Y-F, Zhang H, He L, Liu C, Xu Y, et al. (2013) Butenolide inhibits marine fouling by altering the primary metabolism of three target organisms. ACS Chem Biol 7: 1049-1058.
    • (2013) ACS Chem Biol , vol.7 , pp. 1049-1058
    • Zhang, Y.-F.1    Zhang, H.2    He, L.3    Liu, C.4    Xu, Y.5
  • 31
    • 34848924320 scopus 로고    scopus 로고
    • The Arabidopsis 3-ketoacyl-CoA thiolase-2 (kat2-1) mutant exhibits increased flowering but reduced reproductive success
    • DOI 10.1093/jxb/erm146
    • Footitt S, Cornah JE, Pracharoenwattana I, Bryce JH, Smith SM (2007) The Arabidopsis 3-ketoacyl-CoA thiolase-2 (kat2-1) mutant exhibits increased flowering but reduced reproductive success. J Exp Bot 58: 2959-2968. (Pubitemid 47511750)
    • (2007) Journal of Experimental Botany , vol.58 , Issue.11 , pp. 2959-2968
    • Footitt, S.1    Cornah, J.E.2    Pracharoenwattana, I.3    Bryce, J.H.4    Smith, S.M.5
  • 32
    • 80052282796 scopus 로고    scopus 로고
    • The effect of butenolide on behavioral and morphological changes in two marine fouling species, the barnacle Balanus amphitrite and the bryozoan Bugula neritina
    • Zhang Y-F, Wang G-C, Ying X, Sougrat R, Qian P-Y (2011) The effect of butenolide on behavioral and morphological changes in two marine fouling species, the barnacle Balanus amphitrite and the bryozoan Bugula neritina. Biofouling 27: 467-475.
    • (2011) Biofouling , vol.27 , pp. 467-475
    • Zhang, Y.-F.1    Wang, G.-C.2    Ying, X.3    Sougrat, R.4    Qian, P.-Y.5
  • 33
    • 0030266324 scopus 로고    scopus 로고
    • Larval storage protein of the barnacle, Balanus amphitrite: Biochemical and immunological similarities to vitellin
    • Shimizu K, Satuito CG, Saikawa W, Fusetani N (1996) Larval storage protein of the barnacle, Balanus amphitrite : biochemical and immunological similarities to vitellin. J Exp Zool 276: 87-94.
    • (1996) J Exp Zool , vol.276 , pp. 87-94
    • Shimizu, K.1    Satuito, C.G.2    Saikawa, W.3    Fusetani, N.4
  • 34
    • 84877128000 scopus 로고    scopus 로고
    • iTRAQ-based proteomic profiling of the barnacle Balanus amphitrite in response to the antifouling compound meleagrin
    • Han Z, Sun J, Zhang Y, He F, Xu Y, et al. (2013) iTRAQ-based proteomic profiling of the barnacle Balanus amphitrite in response to the antifouling compound meleagrin. J Proteome Res 12: 2090-2100.
    • (2013) J Proteome Res , vol.12 , pp. 2090-2100
    • Han, Z.1    Sun, J.2    Zhang, Y.3    He, F.4    Xu, Y.5
  • 35
    • 0032708553 scopus 로고    scopus 로고
    • Morphology of the nervous system of the barnacle cypris larva (Balanus amphitrite Darwin) revealed by light and electron microscopy
    • Harrison DCS (1999) Morphology of the nervous system of the barnacle cypris larva (Balanus amphitrite Darwin) revealed by light and electron microscopy. Biol Bull 197: 144.
    • (1999) Biol Bull , vol.197 , pp. 144
    • Harrison, D.C.S.1
  • 36
    • 0029784607 scopus 로고    scopus 로고
    • Serotonin involvement in larval settlement of the barnacle, Balanus amphitrite
    • DOI 10.1002/(SICI)1097-010X(19960801)275:5<339
    • Yamamoto H, Tachibana A, Kawaii S, Matsumura K, Fusetani N (1996) Serotonin involvement in larval settlement fo the barnacle, Balanus amphitrite. J Exp Zool 275: 339-345. (Pubitemid 26311128)
    • (1996) Journal of Experimental Zoology , vol.275 , Issue.5 , pp. 339-345
    • Yamamoto, H.1    Tachibana, A.2    Kawaii, S.3    Matsumura, K.4    Fusetani, N.5
  • 38
    • 0346665635 scopus 로고    scopus 로고
    • Involvement of acetyl choline in settlement of Balanus amphitrite
    • DOI 10.1080/0892701021000044228
    • Faimali M, Falugi C, Gallus L, Piazza V, Tagliafierro G (2003) Involvement of acetyl choline in settlement of Balanus amphitrite . Biofouling 19: 213-220. (Pubitemid 36380375)
    • (2003) Biofouling , vol.19 , Issue.SUPPL. , pp. 213-220
    • Faimali, M.1    Falugi, C.2    Gallus, L.3    Piazza, V.4    Tagliafierro, G.5
  • 40
    • 0027184291 scopus 로고
    • N-acetylaspartylglutamate inhibits forskolin-stimulated cyclic AMP levels via a metabotropic glutamate receptor in cultured cerebellar granule cells
    • Wroblewska B, Wroblewski JT, Saab OH, Neale JH (1993) N-acetylaspartyl-glutamate inhibits forskolin-stimulated cyclic amp levels via a metabotropic glutamate receptor in cultured cerebellar granule cells. J Neurochem 61: 943-948. (Pubitemid 23241231)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.3 , pp. 943-948
    • Wroblewska, B.1    Wroblewski, J.T.2    Saab, O.H.3    Neale, J.H.4
  • 42
    • 0029158319 scopus 로고
    • Evidence for the involvement of cyclic AMP in the pheromonal modulation of barnacle settlement
    • Clare A, Thomas R, Rittschof D (1995) Evidence for the involvement of cyclic AMP in the pheromonal modulation of barnacle settlement. J Exp Biol 198: 655-664.
    • (1995) J Exp Biol , vol.198 , pp. 655-664
    • Clare, A.1    Thomas, R.2    Rittschof, D.3
  • 43
    • 70350770918 scopus 로고    scopus 로고
    • The GABAergic-like system in the cyprid of Balanus amphitrite (= Amphibalanus amphitrite) (Cirripedia, Crustacea)
    • Gallus L, Ferrando S, Gambardella C, Diaspro A, Bianchini P, et al. (2009) The GABAergic-like system in the cyprid of Balanus amphitrite (= Amphibalanus amphitrite) (Cirripedia, Crustacea). Biofouling 26: 155-165.
    • (2009) Biofouling , vol.26 , pp. 155-165
    • Gallus, L.1    Ferrando, S.2    Gambardella, C.3    Diaspro, A.4    Bianchini, P.5
  • 44
    • 30044445027 scopus 로고    scopus 로고
    • A conserved role for Drosophila Neuroglian and human L1-CAM in central-synapse formation
    • DOI 10.1016/j.cub.2005.11.062, PII S0960982205014715
    • Godenschwege TA, Kristiansen LV, Uthaman SB, Hortsch M, Murphey RK (2006) A conserved role for Drosophila neuroglian and human L1-Cam in central-synapse formation. Curr Biol 16: 12-23. (Pubitemid 43049882)
    • (2006) Current Biology , vol.16 , Issue.1 , pp. 12-23
    • Godenschwege, T.A.1    Kristiansen, L.V.2    Uthaman, S.B.3    Hortsch, M.4    Murphey, R.K.5
  • 45
    • 46149087537 scopus 로고    scopus 로고
    • The L1-CAM, neuroglian, functions in glial cells for Drosophila antennal lobe development
    • DOI 10.1002/dneu.20644
    • Chen W, Hing H (2008) The L1-CAM, Neuroglian, functions in glial cells for Drosophila antennal lobe development. Dev Neurobiol 68: 1029-1045. doi:10.1002/dneu.20644. (Pubitemid 351904925)
    • (2008) Developmental Neurobiology , vol.68 , Issue.8 , pp. 1029-1045
    • Chen, W.1    Hing, H.2
  • 46
    • 0035196439 scopus 로고    scopus 로고
    • A CUB-serine protease in the olfactory organ of the spiny lobster Panulirus argus
    • DOI 10.1002/neu.10010
    • Levine MZ, Harrison PJH, Walthall WW, Tai PC, Derby CD (2001) A CUB-serine protease in the olfactory organ of the spiny lobster Panulirus argus. J Neurobiol 49: 277-302. (Pubitemid 33104873)
    • (2001) Journal of Neurobiology , vol.49 , Issue.4 , pp. 277-302
    • Levine, M.Z.1    Harrison, P.J.H.2    William, W.W.3    Tai, P.C.4    Derby, C.D.5
  • 47
    • 0000867877 scopus 로고
    • Cilia from abalone larvae contain a receptor-dependent G-protein transduction system similar to that in mammals
    • Baxter GT, Morse DE (1992) Cilia from abalone larvae contain a receptor-dependent G-protein transduction system similar to that in mammals. Biol Bull 183: 147-154.
    • (1992) Biol Bull , vol.183 , pp. 147-154
    • Baxter, G.T.1    Morse, D.E.2
  • 48
    • 0030483271 scopus 로고    scopus 로고
    • Signal transduction in barnacle settlement: Calcium re-visited
    • Clare AS (1996) Signal transduction in barnacle settlement: calcium re-visited. Biofouling 10: 141-159.
    • (1996) Biofouling , vol.10 , pp. 141-159
    • Clare, A.S.1
  • 49
    • 0028890764 scopus 로고
    • Protein kinase c (PKC) signal transduction system involved in larval metamorphosis of the barnacle, Balanus amphitrite
    • Yamamoto H, Tachibana A, Matsumura K, Fusetani N (1995) Protein kinase c (PKC) signal transduction system involved in larval metamorphosis of the barnacle, Balanus amphitrite. Zool Sci 12: 391-396.
    • (1995) Zool Sci , vol.12 , pp. 391-396
    • Yamamoto, H.1    Tachibana, A.2    Matsumura, K.3    Fusetani, N.4
  • 50
    • 0027199816 scopus 로고
    • Genetic investigation of cAMP-dependent protein kinase function in Drosophila development
    • Lane ME, Kalderon D (1993) Genetic investigation of cAMP-dependent protein kinase function in Drosophila development. Genes Dev 7: 1229-1243. (Pubitemid 23207413)
    • (1993) Genes and Development , vol.7 , Issue.7 A , pp. 1229-1243
    • Lane, M.E.1    Kalderon, D.2
  • 51
    • 0028824480 scopus 로고
    • Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity
    • Labeit S, Kolmerer B (1995) Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity. Science 270: 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 52
    • 0036692739 scopus 로고    scopus 로고
    • The ultrastructure of two types of muscle fibre cells in the cyprid of Balanus amphitrite (Crustacea: Cirripedia)
    • Lagersson NC (2002) The ultrastructure of two types of muscle fibre cells in the cyprid of Balanus amphitrite (Crustacea: Cirripedia). J Mar Biol Ass 82: 573-578.
    • (2002) J Mar Biol Ass , vol.82 , pp. 573-578
    • Lagersson, N.C.1
  • 53
    • 0036937609 scopus 로고    scopus 로고
    • Settlement behavior and antennulary biomechanics in cypris larvae of Balanus amphitrite (Crustacea: Thecostraca: Cirripedia)
    • DOI 10.1007/s00227-002-0854-1
    • Lagersson NC, Høeg JT (2002) Settlement behavior and antennulary biomechanics in cypris larvae of Balanus amphitrite (Crustacea: Thecostraca: Cirripedia). Mar Biol 141: 513-526. (Pubitemid 36064293)
    • (2002) Marine Biology , vol.141 , Issue.3 , pp. 513-526
    • Lagersson, N.C.1    Hoeg, J.T.2
  • 54
    • 77954837047 scopus 로고    scopus 로고
    • Opsin co-expression in Limulus photoreceptors: Differential regulation by light and a circadian clock
    • Katti C, Kempler K, Porter ML, Legg A, Gonzalez R, et al. (2010) Opsin co-expression in Limulus photoreceptors: differential regulation by light and a circadian clock. J Exp Biol 213: 2589-2601.
    • (2010) J Exp Biol , vol.213 , pp. 2589-2601
    • Katti, C.1    Kempler, K.2    Porter, M.L.3    Legg, A.4    Gonzalez, R.5
  • 55
    • 77956010991 scopus 로고    scopus 로고
    • Larval development, sensory mechanisms and physiological adaptations in acorn barnacles with special reference to Balanus amphitrite
    • Anil AC, Khandeparker L, Desai DV, Baragi LV, Gaonkar CA (2010) Larval development, sensory mechanisms and physiological adaptations in acorn barnacles with special reference to Balanus amphitrite. J Exp Mar Biol Ecol 392: 89-98.
    • (2010) J Exp Mar Biol Ecol , vol.392 , pp. 89-98
    • Anil, A.C.1    Khandeparker, L.2    Desai, D.V.3    Baragi, L.V.4    Gaonkar, C.A.5
  • 57
    • 0030671248 scopus 로고    scopus 로고
    • Mitochondrial arginine kinase in the midgut of the tobacco hornworm (Manduca sexta)
    • Chamberlin M (1997) Mitochondrial arginine kinase in the midgut of the tobacco hornworm (Manduca sexta). J Exp Biol 200: 2789-2796.
    • (1997) J Exp Biol , vol.200 , pp. 2789-2796
    • Chamberlin, M.1
  • 58
    • 3042904467 scopus 로고
    • Separation of acetyl transfer enzymes in pigeon liver extract
    • Chou TC, Lipmann F (1952) Separation of acetyl transfer enzymes in pigeon liver extract. J Biol Chem 196: 89-103.
    • (1952) J Biol Chem , vol.196 , pp. 89-103
    • Chou, T.C.1    Lipmann, F.2
  • 59
    • 33947457185 scopus 로고
    • An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A1
    • Srere PA, Lipmann F (1953) An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A1. J Am Chem Soc 75: 4874-4874.
    • (1953) J Am Chem Soc , vol.75 , pp. 4874-4874
    • Srere, P.A.1    Lipmann, F.2
  • 60
    • 0027756154 scopus 로고
    • Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster
    • DOI 10.1083/jcb.123.6.1797
    • Lee JK, Coyne RS, Dubreuil RR, Goldstein LS, Branton D (1993) Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster. J Cell Biol 123: 1797-1809. (Pubitemid 24012935)
    • (1993) Journal of Cell Biology , vol.123 , Issue.6 II , pp. 1797-1809
    • Lee, J.K.1    Coyne, R.S.2    Dubreuil, R.R.3    Goldstein, L.S.B.4    Branton, D.5
  • 61
    • 84861600768 scopus 로고    scopus 로고
    • Metamorphosis in the cirripede crustacean Balanus amphitrite
    • Maruzzo D, Aldred N, Clare AS, Høeg JT (2012) Metamorphosis in the cirripede crustacean Balanus amphitrite. PLoS One 5: e37408.
    • (2012) PLoS One , vol.5
    • Maruzzo, D.1    Aldred, N.2    Clare, A.S.3    Høeg, J.T.4
  • 62
    • 0023979999 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation
    • Dreyfuss G, Swanson MS, Piñol-Roma S (1988) Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation. Trends Biochem Sci 13: 86-91.
    • (1988) Trends Biochem Sci , vol.13 , pp. 86-91
    • Dreyfuss, G.1    Swanson, M.S.2    Piñol-Roma, S.3
  • 63
    • 84874102994 scopus 로고    scopus 로고
    • Poly(A) binding proteins: Are they all created equal?
    • Goss DJ, Kleiman FE (2012) Poly(A) binding proteins: are they all created equal? WIREs RNA 4: 167-179.
    • (2012) WIREs RNA , vol.4 , pp. 167-179
    • Goss, D.J.1    Kleiman, F.E.2
  • 64
    • 0032583165 scopus 로고    scopus 로고
    • Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, vein, at the muscle- tendon junction site
    • DOI 10.1083/jcb.143.5.1259
    • Strumpf D, Volk T (1998) Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, Vein, at the muscle-tendon junction site. J Cell Biol 143: 1259-1270. (Pubitemid 28559827)
    • (1998) Journal of Cell Biology , vol.143 , Issue.5 , pp. 1259-1270
    • Strumpf, D.1    Volk, T.2
  • 65
    • 0015850905 scopus 로고
    • Microtubules and muscle attachment in the integument of the balanidae
    • Koulish S (1973) Microtubules and muscle attachment in the integument of the balanidae. J Morphol 140: 1-13.
    • (1973) J Morphol , vol.140 , pp. 1-13
    • Koulish, S.1
  • 66
    • 78649813933 scopus 로고    scopus 로고
    • The N-myc downstream regulated gene (NDRG) family: Diverse functions, multiple applications
    • Melotte V, Qu X, Ongenaert M, van Criekinge W, de Brüne AP, et al. (2010) The N-myc downstream regulated gene (NDRG) family: diverse functions, multiple applications. The FASEB Journal 24: 4153-4166.
    • (2010) The FASEB Journal , vol.24 , pp. 4153-4166
    • Melotte, V.1    Qu, X.2    Ongenaert, M.3    Van Criekinge, W.4    De Brüne, A.P.5
  • 67
    • 0025296934 scopus 로고
    • Expression of annexins as a function of cellular growth state
    • Schlaepfer DD, Haigler HT (1990) Expression of annexins as a function of cellular growth state. J Cell Biol 111: 229-238.
    • (1990) J Cell Biol , vol.111 , pp. 229-238
    • Schlaepfer, D.D.1    Haigler, H.T.2
  • 68
    • 33748041611 scopus 로고    scopus 로고
    • Developmental profile of annexin IX and its possible role in programmed cell death of the Bombyx mori anterior silk gland
    • DOI 10.2108/zsj.23.533
    • Kaneko Y, Takaki K, Iwami M, Sakurai S (2006) Developmental profile of annexin IX and its possible role in programmed cell death of the Bombyx mori anterior silk gland. Zool Sci 23: 533-542. (Pubitemid 44299303)
    • (2006) Zoological Science , vol.23 , Issue.6 , pp. 533-542
    • Kaneko, Y.1    Takaki, K.2    Iwami, M.3    Sakurai, S.4
  • 69
    • 0031373777 scopus 로고    scopus 로고
    • 20- Hydroxyecdysone regulates larval metamorphosis of the barnacle, Balanus amphitrite
    • Yamamoto H, Kawaii S, Yoshimura E, Tachibana A, Fusetani N (1997) 20- Hydroxyecdysone regulates larval metamorphosis of the barnacle, Balanus amphitrite. Zool Sci 14: 887-892.
    • (1997) Zool Sci , vol.14 , pp. 887-892
    • Yamamoto, H.1    Kawaii, S.2    Yoshimura, E.3    Tachibana, A.4    Fusetani, N.5
  • 70
    • 0242652960 scopus 로고
    • Effect of carbonic anhydrase inhibitors on shell development and growth of Balanus improvisus Darwin
    • Costlow JD (1959) Effect of carbonic anhydrase inhibitors on shell development and growth of Balanus improvisus Darwin. Physiol Zool 3: 177-184.
    • (1959) Physiol Zool , vol.3 , pp. 177-184
    • Costlow, J.D.1
  • 71
    • 0013093818 scopus 로고
    • Carbonic anhydrase activity in the integument of the crab Carcinus maenas during the intermolt cycle
    • Giraud M-M (1981) Carbonic anhydrase activity in the integument of the crab Carcinus maenas during the intermolt cycle. Comp Biochem Physiol A Mol Integr Physiol 69: 381-387.
    • (1981) Comp Biochem Physiol a Mol Integr Physiol , vol.69 , pp. 381-387
    • Giraud, M.-M.1
  • 72
    • 84878088278 scopus 로고    scopus 로고
    • Characterization of two 20kDa-cement protein (cp20k) homologues in Amphibalanus amphitrite
    • He L-S, Zhang G, Qian P-Y (2013) Characterization of two 20kDa-cement protein (cp20k) homologues in Amphibalanus amphitrite. PLoS One 8: e64130.
    • (2013) PLoS One , vol.8
    • He, L.-S.1    Zhang, G.2    Qian, P.-Y.3
  • 73
    • 0034282718 scopus 로고    scopus 로고
    • Barnacle cement proteins. Importance of disulfide bonds in their insolubility
    • Kamino K, Inoue K, Maruyama T, Takamatsu N, Harayama S, et al. (2000) Barnacle cement proteins. Importance of disulfide bonds in their insolubility. J Biol Chem 275: 27360-27365.
    • (2000) J Biol Chem , vol.275 , pp. 27360-27365
    • Kamino, K.1    Inoue, K.2    Maruyama, T.3    Takamatsu, N.4    Harayama, S.5
  • 74
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F (1996) Discovery of the heat shock response. Cell Stress Chapersones 1: 97-98.
    • (1996) Cell Stress Chapersones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 75
    • 0030766710 scopus 로고    scopus 로고
    • Heat shock protein gene expression during Xenopus development
    • DOI 10.1007/PL00000573
    • Heikkila JJ, Ohan N, Tam Y, Ali A (1997) Heat shock protein gene expression during Xenopus development. Cell Mol Life Sci 53: 114-121. (Pubitemid 27379380)
    • (1997) Cellular and Molecular Life Sciences , vol.53 , Issue.1 , pp. 114-121
    • Heikkila, J.J.1    Ohan, N.2    Tam, Y.3    Ali, A.4
  • 76
    • 22044434528 scopus 로고    scopus 로고
    • Expression patterns of three heat shock protein 70 genes among developmental stages of the red flour beetle, Tribolium castaneum (Coleoptera: Tenebrionidae)
    • DOI 10.1016/j.cbpb.2005.05.044, PII S1095643305001832
    • Mahroof R, Yan Zhu K, Neven L, Subramanyam B, Bai J (2005) Expression patterns of three heat shock protein 70 genes among developmental stages of the red flour beetle, Tribolium castaneum (Coleoptera: Tenebrionidae). Comp Biochem Physiol A Mol Integr Physiol 141: 247-256. (Pubitemid 40965759)
    • (2005) Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology , vol.141 , Issue.2 , pp. 247-256
    • Mahroof, R.1    Kun, Y.Z.2    Neven, L.3    Subramanyam, B.4    Bai, J.5
  • 77
    • 0035543255 scopus 로고    scopus 로고
    • NO/cGMP signaling and HSP90 activity represses metamorphosis in the sea urchin Lytechinus pictus
    • Bishop CD, Brandhorst BP (2001) No/Cgmp signaling and Hsp90 activity represses metamorphosis in the sea urchin Lytechinus Pictus. Biol Bull 201: 394-404. (Pubitemid 34057135)
    • (2001) Biological Bulletin , vol.201 , Issue.3 , pp. 394-404
    • Bishop, C.D.1    Brandhorst, B.P.2
  • 78
    • 0034737291 scopus 로고    scopus 로고
    • Molecular chaperones activate the Drosophila ecdysone receptor, an RXR heterodimer
    • Arbeitman MN, Hogness DS (2000) Molecular chaperones activate the Drosophila ecdysone receptor, an RXR heterodimer. Cell 101: 67-77.
    • (2000) Cell , vol.101 , pp. 67-77
    • Arbeitman, M.N.1    Hogness, D.S.2
  • 79
    • 35348827685 scopus 로고    scopus 로고
    • Developmental expression of Hsp90, Hsp70 and HSF during morphogenesis in the vetigastropod Haliotis asinina
    • Gunter H, Degnan B (2007) Developmental expression of Hsp90, Hsp70 and HSF during morphogenesis in the vetigastropod Haliotis asinina . Dev Genes Evol 217: 603-612.
    • (2007) Dev Genes Evol , vol.217 , pp. 603-612
    • Gunter, H.1    Degnan, B.2
  • 80
    • 77956314945 scopus 로고    scopus 로고
    • 2D gel-based multiplexed proteomic analysis during larval development and metamorphosis of the biofouling polychaete tubeworm Hydroides elegans
    • Zhang Y, Sun J, Xiao K, Arellano SM, Thiyagarajan V, et al. (2010) 2D gel-based multiplexed proteomic analysis during larval development and metamorphosis of the biofouling polychaete tubeworm Hydroides elegans. J Proteome Res 9: 4851-4860.
    • (2010) J Proteome Res , vol.9 , pp. 4851-4860
    • Zhang, Y.1    Sun, J.2    Xiao, K.3    Arellano, S.M.4    Thiyagarajan, V.5
  • 81
    • 84874630897 scopus 로고    scopus 로고
    • Transcriptome and quantitative proteome analysis reveals molecular processes associated with larval metamorphosis in the polychaete Pseudopolydora vexillosa
    • Chandramouli KH, Sun J, Mok FS, Liu L, Qiu J-W, et al. (2013) Transcriptome and quantitative proteome analysis reveals molecular processes associated with larval metamorphosis in the polychaete Pseudopolydora vexillosa. J Proteome Res 12: 1344-1358.
    • (2013) J Proteome Res , vol.12 , pp. 1344-1358
    • Chandramouli, K.H.1    Sun, J.2    Mok, F.S.3    Liu, L.4    Qiu, J.-W.5
  • 82
    • 80052215711 scopus 로고    scopus 로고
    • Differential expression of proteins and phosphoproteins during larval metamorphosis of the polychaete Capitella sp. I
    • Chandramouli KH, Soo L, Qian P-Y (2011) Differential expression of proteins and phosphoproteins during larval metamorphosis of the polychaete Capitella sp. I. Proteome Sci 9: 51.
    • (2011) Proteome Sci , vol.9 , pp. 51
    • Chandramouli, K.H.1    Soo, L.2    Qian, P.-Y.3
  • 83
    • 84972136607 scopus 로고
    • Attachment and metamorphosis of the cheilo-ctenostome bryozoan Bugula neritina (Linné)
    • Woollacott RM, Zimmer RL (1971) Attachment and metamorphosis of the cheilo-ctenostome bryozoan Bugula neritina (Linné). J Morphol 134: 351-382.
    • (1971) J Morphol , vol.134 , pp. 351-382
    • Woollacott, R.M.1    Zimmer, R.L.2


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