메뉴 건너뛰기




Volumn 14, Issue 1, 2013, Pages

Complex gene expression in the dragline silk producing glands of the Western black widow (Latrodectus hesperus)

Author keywords

Alternative polyadenylation; Major ampullate glands; MaSp1; Spider; Spidroin; Tag profiling

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; SILK;

EID: 84888620561     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-14-846     Document Type: Article
Times cited : (25)

References (79)
  • 1
    • 0004095514 scopus 로고    scopus 로고
    • New York: Oxford University Press, 3
    • Foelix RF. Biology of spiders 2011, New York: Oxford University Press, 3.
    • (2011) Biology of spiders
    • Foelix, R.F.1
  • 2
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • 10.1038/35069000, 11279484
    • Vollrath F, Knight DP. Liquid crystalline spinning of spider silk. Nature 2001, 410(6828):541-548. 10.1038/35069000, 11279484.
    • (2001) Nature , vol.410 , Issue.6828 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 3
    • 33747078717 scopus 로고    scopus 로고
    • Silken toolkits: biomechanics of silk fibers spun by the orb web spider Argiope argentata (Fabricius 1775)
    • 10.1242/jeb.02275, 16788028
    • Blackledge TA, Hayashi CY. Silken toolkits: biomechanics of silk fibers spun by the orb web spider Argiope argentata (Fabricius 1775). J Exp Biol 2006, 209(13):2452-2461. 10.1242/jeb.02275, 16788028.
    • (2006) J Exp Biol , vol.209 , Issue.13 , pp. 2452-2461
    • Blackledge, T.A.1    Hayashi, C.Y.2
  • 4
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: from fibroin sequence to mechanical function
    • Gosline JM, Guerette PA, Ortlepp CS, Savage KN. The mechanical design of spider silks: from fibroin sequence to mechanical function. J Exp Biol 1999, 202(23):3295-3303.
    • (1999) J Exp Biol , vol.202 , Issue.23 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Ortlepp, C.S.3    Savage, K.N.4
  • 6
    • 36649007685 scopus 로고    scopus 로고
    • Spider silk as a resource for future biotechnologies
    • Sponner A. Spider silk as a resource for future biotechnologies. Entomological Research 2007, 37(4):238-250.
    • (2007) Entomological Research , vol.37 , Issue.4 , pp. 238-250
    • Sponner, A.1
  • 7
    • 78651367978 scopus 로고    scopus 로고
    • Spider silk proteins: recent advances in recombinant production, structure-function relationships and biomedical applications
    • 10.1007/s00018-010-0462-z, 20668909
    • Rising A, Widhe M, Johansson J, Hedhammar M. Spider silk proteins: recent advances in recombinant production, structure-function relationships and biomedical applications. Cell Mol Life Sci 2011, 68(2):169-184. 10.1007/s00018-010-0462-z, 20668909.
    • (2011) Cell Mol Life Sci , vol.68 , Issue.2 , pp. 169-184
    • Rising, A.1    Widhe, M.2    Johansson, J.3    Hedhammar, M.4
  • 8
    • 0029925013 scopus 로고    scopus 로고
    • Silk properties determined by gland-specific expression of a spider fibroin gene family
    • 10.1126/science.272.5258.112, 8600519
    • Guerette PA, Ginzinger DG, Weber BHF, Gosline JM. Silk properties determined by gland-specific expression of a spider fibroin gene family. Science 1996, 272(5258):112-115. 10.1126/science.272.5258.112, 8600519.
    • (1996) Science , vol.272 , Issue.5258 , pp. 112-115
    • Guerette, P.A.1    Ginzinger, D.G.2    Weber, B.H.F.3    Gosline, J.M.4
  • 9
    • 0035970888 scopus 로고    scopus 로고
    • Extreme diversity, conservation, and convergence of spider silk fibroin sequences
    • 10.1126/science.1057561, 11283372
    • Gatesy J, Hayashi C, Motriuk D, Woods J, Lewis RV. Extreme diversity, conservation, and convergence of spider silk fibroin sequences. Science 2001, 291(5513):2603-2605. 10.1126/science.1057561, 11283372.
    • (2001) Science , vol.291 , Issue.5513 , pp. 2603-2605
    • Gatesy, J.1    Hayashi, C.2    Motriuk, D.3    Woods, J.4    Lewis, R.V.5
  • 10
    • 0025008260 scopus 로고
    • Structure of a protein superfiber: spider dragline silk
    • 10.1073/pnas.87.18.7120, 54695, 2402494
    • Xu M, Lewis RV. Structure of a protein superfiber: spider dragline silk. Proc Natl Acad Sci USA 1990, 87(18):7120-7124. 10.1073/pnas.87.18.7120, 54695, 2402494.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.18 , pp. 7120-7124
    • Xu, M.1    Lewis, R.V.2
  • 11
    • 0026657815 scopus 로고
    • Isolation of a clone encoding a second dragline silk fibroin: Nephila clavipes dragline silk is a two-protein fiber
    • Hinman MB, Lewis RV. Isolation of a clone encoding a second dragline silk fibroin: Nephila clavipes dragline silk is a two-protein fiber. J Biol Chem 1992, 267(27):19320-19324.
    • (1992) J Biol Chem , vol.267 , Issue.27 , pp. 19320-19324
    • Hinman, M.B.1    Lewis, R.V.2
  • 12
    • 23844471234 scopus 로고    scopus 로고
    • Modular evolution of egg case silk genes across orb-weaving spider superfamilies
    • 10.1073/pnas.0502473102, 1183556, 16061817
    • Garb JE, Hayashi CY. Modular evolution of egg case silk genes across orb-weaving spider superfamilies. Proc Natl Acad Sci USA 2005, 102(32):11379-11384. 10.1073/pnas.0502473102, 1183556, 16061817.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.32 , pp. 11379-11384
    • Garb, J.E.1    Hayashi, C.Y.2
  • 13
    • 20144362683 scopus 로고    scopus 로고
    • Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein
    • Tian M, Lewis RV. Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein. Biochemistry (NY) 2005, 44(22):8006-8012.
    • (2005) Biochemistry (NY) , vol.44 , Issue.22 , pp. 8006-8012
    • Tian, M.1    Lewis, R.V.2
  • 14
    • 30344447954 scopus 로고    scopus 로고
    • Unique molecular architecture of egg case silk protein in a spider: Nephila clavata
    • 10.1093/jb/mvi155, 16272571
    • Zhao A, Zhao T, SiMa Y, Zhang Y, Nakagaki K. Unique molecular architecture of egg case silk protein in a spider: Nephila clavata. J Biochem 2005, 138(5):593-604. 10.1093/jb/mvi155, 16272571.
    • (2005) J Biochem , vol.138 , Issue.5 , pp. 593-604
    • Zhao, A.1    Zhao, T.2    SiMa, Y.3    Zhang, Y.4    Nakagaki, K.5
  • 15
    • 0031932874 scopus 로고    scopus 로고
    • Spider minor ampullate silk proteins contain new repetitive sequences and highly conserved non-silk-like " spacer regions"
    • 10.1002/pro.5560070315, 2143960, 9541398
    • Colgin MA, Lewis RV. Spider minor ampullate silk proteins contain new repetitive sequences and highly conserved non-silk-like " spacer regions". Protein Sci 1998, 7(3):667-672. 10.1002/pro.5560070315, 2143960, 9541398.
    • (1998) Protein Sci , vol.7 , Issue.3 , pp. 667-672
    • Colgin, M.A.1    Lewis, R.V.2
  • 16
    • 4944247871 scopus 로고    scopus 로고
    • Molecular and mechanical characterization of aciniform silk: uniformity of iterated sequence modules in a novel member of the spider silk fibroin gene family
    • 10.1093/molbev/msh204, 15240839
    • Hayashi CY, Blackledge TA, Lewis RV. Molecular and mechanical characterization of aciniform silk: uniformity of iterated sequence modules in a novel member of the spider silk fibroin gene family. Mol Biol Evol 2004, 21(10):1950-1959. 10.1093/molbev/msh204, 15240839.
    • (2004) Mol Biol Evol , vol.21 , Issue.10 , pp. 1950-1959
    • Hayashi, C.Y.1    Blackledge, T.A.2    Lewis, R.V.3
  • 17
    • 0032488823 scopus 로고    scopus 로고
    • Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks
    • 10.1006/jmbi.1997.1478, 9480768
    • Hayashi CY, Lewis RV. Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks. J Mol Biol 1998, 275(5):773-784. 10.1006/jmbi.1997.1478, 9480768.
    • (1998) J Mol Biol , vol.275 , Issue.5 , pp. 773-784
    • Hayashi, C.Y.1    Lewis, R.V.2
  • 18
    • 70350418753 scopus 로고    scopus 로고
    • Pyriform spidroin 1, a novel member of the silk gene family that anchors dragline silk fibers in attachment discs of the black widow spider, Latrodectus hesperus
    • 10.1074/jbc.M109.021378, 2781455, 19666476
    • Blasingame E, Tuton-Blasingame T, Larkin L, Falick AM, Zhao L, Fong J, Vaidyanathan V, Visperas A, Geurts P, Hu X, La Mattina C, Vierra C. Pyriform spidroin 1, a novel member of the silk gene family that anchors dragline silk fibers in attachment discs of the black widow spider, Latrodectus hesperus. J Biol Chem 2009, 284(42):29097-29108. 10.1074/jbc.M109.021378, 2781455, 19666476.
    • (2009) J Biol Chem , vol.284 , Issue.42 , pp. 29097-29108
    • Blasingame, E.1    Tuton-Blasingame, T.2    Larkin, L.3    Falick, A.M.4    Zhao, L.5    Fong, J.6    Vaidyanathan, V.7    Visperas, A.8    Geurts, P.9    Hu, X.10    La Mattina, C.11    Vierra, C.12
  • 19
    • 0032963575 scopus 로고    scopus 로고
    • Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins
    • 10.1016/S0141-8130(98)00089-0, 10342774
    • Hayashi CY, Shipley NH, Lewis RV. Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins. Int J Biol Macromol 1999, 24(2-3):271-275. 10.1016/S0141-8130(98)00089-0, 10342774.
    • (1999) Int J Biol Macromol , vol.24 , Issue.2-3 , pp. 271-275
    • Hayashi, C.Y.1    Shipley, N.H.2    Lewis, R.V.3
  • 21
    • 36849026592 scopus 로고    scopus 로고
    • Aciniform spidroin, a constituent of egg case sacs and wrapping silk fibers from the black widow spider Latrodectus hesperus
    • 10.1074/jbc.M705791200, 17921147
    • Vasanthavada K, Hu X, Falick AM, La Mattina C, Moore AMF, Jones PR, Yee R, Reza R, Tuton T, Vierra C. Aciniform spidroin, a constituent of egg case sacs and wrapping silk fibers from the black widow spider Latrodectus hesperus. J Biol Chem 2007, 282(48):35088-35097. 10.1074/jbc.M705791200, 17921147.
    • (2007) J Biol Chem , vol.282 , Issue.48 , pp. 35088-35097
    • Vasanthavada, K.1    Hu, X.2    Falick, A.M.3    La Mattina, C.4    Moore, A.M.F.5    Jones, P.R.6    Yee, R.7    Reza, R.8    Tuton, T.9    Vierra, C.10
  • 22
    • 36649007963 scopus 로고    scopus 로고
    • Blueprint for a high-performance biomaterial: full-length spider dragline silk genes
    • 10.1371/journal.pone.0000514, 1885213, 17565367
    • Ayoub NA, Garb JE, Tinghitella RM, Collin MA, Hayashi CY. Blueprint for a high-performance biomaterial: full-length spider dragline silk genes. PLoS ONE 2007, 2(6):e514. 10.1371/journal.pone.0000514, 1885213, 17565367.
    • (2007) PLoS ONE , vol.2 , Issue.6
    • Ayoub, N.A.1    Garb, J.E.2    Tinghitella, R.M.3    Collin, M.A.4    Hayashi, C.Y.5
  • 24
    • 28844433042 scopus 로고    scopus 로고
    • Analysis of the conserved N-terminal domains in major ampullate spider silk proteins
    • 10.1021/bm050472b, 16283740
    • Motriuk-Smith D, Smith A, Hayashi CY, Lewis RV. Analysis of the conserved N-terminal domains in major ampullate spider silk proteins. Biomacromolecules 2005, 6(6):3152-3159. 10.1021/bm050472b, 16283740.
    • (2005) Biomacromolecules , vol.6 , Issue.6 , pp. 3152-3159
    • Motriuk-Smith, D.1    Smith, A.2    Hayashi, C.Y.3    Lewis, R.V.4
  • 25
    • 33846008063 scopus 로고    scopus 로고
    • N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins
    • 10.1021/bm060693x, 17096540
    • Rising A, Hjälm G, Engström W, Johansson J. N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins. Biomacromolecules 2006, 7(11):3120-3124. 10.1021/bm060693x, 17096540.
    • (2006) Biomacromolecules , vol.7 , Issue.11 , pp. 3120-3124
    • Rising, A.1    Hjälm, G.2    Engström, W.3    Johansson, J.4
  • 26
    • 77955292367 scopus 로고    scopus 로고
    • Untangling spider silk evolution with spidroin terminal domains
    • 10.1186/1471-2148-10-243, 2928236, 20696068
    • Garb JE, Ayoub NA, Hayashi CY. Untangling spider silk evolution with spidroin terminal domains. BMC Evol Biol 2010, 10(1):243. 10.1186/1471-2148-10-243, 2928236, 20696068.
    • (2010) BMC Evol Biol , vol.10 , Issue.1 , pp. 243
    • Garb, J.E.1    Ayoub, N.A.2    Hayashi, C.Y.3
  • 27
    • 77956296603 scopus 로고    scopus 로고
    • Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber
    • 10.1073/pnas.1003366107, 2922564, 20660779
    • Xia XX, Qian ZG, Ki CS, Park YH, Kaplan DL, Lee SY. Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber. Proc Natl Acad Sci USA 2010, 107(32):14059-14063. 10.1073/pnas.1003366107, 2922564, 20660779.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.32 , pp. 14059-14063
    • Xia, X.X.1    Qian, Z.G.2    Ki, C.S.3    Park, Y.H.4    Kaplan, D.L.5    Lee, S.Y.6
  • 28
    • 34249889559 scopus 로고    scopus 로고
    • Macroscopic fibers self-assembled from recombinant miniature spider silk proteins
    • 10.1021/bm070049y, 17402782
    • Stark M, Grip S, Rising A, Hedhammar M, Engström W, Hjälm G, Johansson J. Macroscopic fibers self-assembled from recombinant miniature spider silk proteins. Biomacromolecules 2007, 8(5):1695-1701. 10.1021/bm070049y, 17402782.
    • (2007) Biomacromolecules , vol.8 , Issue.5 , pp. 1695-1701
    • Stark, M.1    Grip, S.2    Rising, A.3    Hedhammar, M.4    Engström, W.5    Hjälm, G.6    Johansson, J.7
  • 29
    • 84856943369 scopus 로고    scopus 로고
    • Conserved C-terminal domain of spider tubuliform spidroin 1 contributes to extensibility in synthetic fibers
    • 10.1021/bm201262n, 22176138
    • Gnesa E, Hsia Y, Yarger JL, Weber W, Lin-Cereghino J, Lin-Cerghino G, Tang S, Agari K, Vierra CA. Conserved C-terminal domain of spider tubuliform spidroin 1 contributes to extensibility in synthetic fibers. Biomacromolecules 2012, 13(2):304-312. 10.1021/bm201262n, 22176138.
    • (2012) Biomacromolecules , vol.13 , Issue.2 , pp. 304-312
    • Gnesa, E.1    Hsia, Y.2    Yarger, J.L.3    Weber, W.4    Lin-Cereghino, J.5    Lin-Cerghino, G.6    Tang, S.7    Agari, K.8    Vierra, C.A.9
  • 30
    • 80052059803 scopus 로고    scopus 로고
    • Impact of initial solvent on thermal stability and mechanical properties of recombinant spider silk films
    • Spiess K, Ene R, Keenan CD, Senker J, Kremer F, Scheibel T. Impact of initial solvent on thermal stability and mechanical properties of recombinant spider silk films. J Mater Chem 2011, 21(35):13594-13604.
    • (2011) J Mater Chem , vol.21 , Issue.35 , pp. 13594-13604
    • Spiess, K.1    Ene, R.2    Keenan, C.D.3    Senker, J.4    Kremer, F.5    Scheibel, T.6
  • 31
    • 33846876976 scopus 로고    scopus 로고
    • Spider dragline silk: correlated and mosaic evolution in high-performance biological materials
    • Swanson BO, Blackledge TA, Summers AP, Hayashi CY. Spider dragline silk: correlated and mosaic evolution in high-performance biological materials. Evolution 2006, 60(12):2539-2551.
    • (2006) Evolution , vol.60 , Issue.12 , pp. 2539-2551
    • Swanson, B.O.1    Blackledge, T.A.2    Summers, A.P.3    Hayashi, C.Y.4
  • 32
    • 48449103887 scopus 로고    scopus 로고
    • Elasticity of spider silks
    • 10.1021/bm7014174, 18529075
    • Liu Y, Shao Z, Vollrath F. Elasticity of spider silks. Biomacromolecules 2008, 9(7):1782-1786. 10.1021/bm7014174, 18529075.
    • (2008) Biomacromolecules , vol.9 , Issue.7 , pp. 1782-1786
    • Liu, Y.1    Shao, Z.2    Vollrath, F.3
  • 33
    • 38949197123 scopus 로고    scopus 로고
    • Proline and processing of spider silks
    • 10.1021/bm700877g, 18052126
    • Liu Y, Sponner A, Porter D, Vollrath F. Proline and processing of spider silks. Biomacromolecules 2008, 9(1):116-121. 10.1021/bm700877g, 18052126.
    • (2008) Biomacromolecules , vol.9 , Issue.1 , pp. 116-121
    • Liu, Y.1    Sponner, A.2    Porter, D.3    Vollrath, F.4
  • 34
    • 0032956830 scopus 로고    scopus 로고
    • Protein and amino acid composition of silks from the cob weaver, Latrodectus hesperus (black widow)
    • 10.1016/S0141-8130(98)00078-6, 10342753
    • Casem ML, Turner D, Houchin K. Protein and amino acid composition of silks from the cob weaver, Latrodectus hesperus (black widow). Int J Biol Macromol 1999, 24(2-3):103-108. 10.1016/S0141-8130(98)00078-6, 10342753.
    • (1999) Int J Biol Macromol , vol.24 , Issue.2-3 , pp. 103-108
    • Casem, M.L.1    Turner, D.2    Houchin, K.3
  • 35
    • 38949105514 scopus 로고    scopus 로고
    • Multiple recombining loci encode MaSp1, the primary constituent of dragline silk, in widow spiders (Latrodectus: Theridiidae)
    • 10.1093/molbev/msm246, 18048404
    • Ayoub NA, Hayashi CY. Multiple recombining loci encode MaSp1, the primary constituent of dragline silk, in widow spiders (Latrodectus: Theridiidae). Mol Biol Evol 2008, 25(2):277-286. 10.1093/molbev/msm246, 18048404.
    • (2008) Mol Biol Evol , vol.25 , Issue.2 , pp. 277-286
    • Ayoub, N.A.1    Hayashi, C.Y.2
  • 36
    • 52049093924 scopus 로고    scopus 로고
    • Identification and characterization of multiple Spidroin 1 genes encoding major ampullate silk proteins in Nephila clavipes
    • 10.1111/j.1365-2583.2008.00828.x, 2831225, 18828837
    • Gaines WA, Marcotte WR. Identification and characterization of multiple Spidroin 1 genes encoding major ampullate silk proteins in Nephila clavipes. Insect Mol Biol 2008, 17(5):465-474. 10.1111/j.1365-2583.2008.00828.x, 2831225, 18828837.
    • (2008) Insect Mol Biol , vol.17 , Issue.5 , pp. 465-474
    • Gaines, W.A.1    Marcotte, W.R.2
  • 37
    • 33645221987 scopus 로고    scopus 로고
    • Spider egg case core fibers: trimeric complexes assembled from TuSp1, ECP-1, and ECP-2
    • Hu X, Kohler K, Falick AM, Moore AMF, Jones PR, Vierra C. Spider egg case core fibers: trimeric complexes assembled from TuSp1, ECP-1, and ECP-2. Biochemistry (N Y) 2006, 45(11):3506-3516.
    • (2006) Biochemistry (N Y) , vol.45 , Issue.11 , pp. 3506-3516
    • Hu, X.1    Kohler, K.2    Falick, A.M.3    Moore, A.M.F.4    Jones, P.R.5    Vierra, C.6
  • 38
    • 20544450200 scopus 로고    scopus 로고
    • Characterization of a novel class II bHLH transcription factor from the black widow spider, Latrodectus hesperus, with silk-gland restricted patterns of expression
    • 10.1089/dna.2005.24.371, 15941389
    • Kohler K, Thayer W, Le T, Sembhi A, Vasanthavada K, Moore AMF, Vierra CA. Characterization of a novel class II bHLH transcription factor from the black widow spider, Latrodectus hesperus, with silk-gland restricted patterns of expression. DNA Cell Biol 2005, 24(6):371-380. 10.1089/dna.2005.24.371, 15941389.
    • (2005) DNA Cell Biol , vol.24 , Issue.6 , pp. 371-380
    • Kohler, K.1    Thayer, W.2    Le, T.3    Sembhi, A.4    Vasanthavada, K.5    Moore, A.M.F.6    Vierra, C.A.7
  • 39
    • 52949096084 scopus 로고    scopus 로고
    • Next-generation DNA sequencing methods
    • Mardis ER. Next-generation DNA sequencing methods. Annu Rev of Genomics Hum Genet 2008, 9:387-402.
    • (2008) Annu Rev of Genomics Hum Genet , vol.9 , pp. 387-402
    • Mardis, E.R.1
  • 40
    • 39649117755 scopus 로고    scopus 로고
    • The impact of next-generation sequencing technology on genetics
    • 10.1016/j.tig.2007.12.007, 18262675
    • Mardis ER. The impact of next-generation sequencing technology on genetics. Trends Genet 2008, 24(3):133-141. 10.1016/j.tig.2007.12.007, 18262675.
    • (2008) Trends Genet , vol.24 , Issue.3 , pp. 133-141
    • Mardis, E.R.1
  • 41
    • 84859625932 scopus 로고    scopus 로고
    • Next-generation sequencing technologies for environmental DNA research
    • 10.1111/j.1365-294X.2012.05538.x, 22486820
    • Shokralla S, Spall JL, Gibson JF, Hajibabaei M. Next-generation sequencing technologies for environmental DNA research. Mol Ecol 2012, 21(8):1794-1805. 10.1111/j.1365-294X.2012.05538.x, 22486820.
    • (2012) Mol Ecol , vol.21 , Issue.8 , pp. 1794-1805
    • Shokralla, S.1    Spall, J.L.2    Gibson, J.F.3    Hajibabaei, M.4
  • 42
    • 79959634465 scopus 로고    scopus 로고
    • Spinning gland transcriptomics from two main clades of spiders (order: Araneae)-insights on their molecular, anatomical and behavioral evolution
    • 10.1371/journal.pone.0021634, 3126850, 21738742
    • Prosdocimi F, Bittencourt D, Da Silva FR, Kirst M, Motta PC, Rech EL. Spinning gland transcriptomics from two main clades of spiders (order: Araneae)-insights on their molecular, anatomical and behavioral evolution. PLoS ONE 2011, 6(6):e21634. 10.1371/journal.pone.0021634, 3126850, 21738742.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Prosdocimi, F.1    Bittencourt, D.2    Da Silva, F.R.3    Kirst, M.4    Motta, P.C.5    Rech, E.L.6
  • 43
    • 2542623618 scopus 로고    scopus 로고
    • Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus
    • 10.1021/bm0342640, 15132648
    • Lawrence BA, Vierra CA, Moore AMF. Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus. Biomacromolecules 2004, 5(3):689-695. 10.1021/bm0342640, 15132648.
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 689-695
    • Lawrence, B.A.1    Vierra, C.A.2    Moore, A.M.F.3
  • 44
    • 0032219928 scopus 로고    scopus 로고
    • Phylogeny of the orb-web building spiders (Araneae, Orbiculariae: Deinopoidea, Araneoidea)
    • Griswold CE, Coddington JA, Hormiga G, Scharff N. Phylogeny of the orb-web building spiders (Araneae, Orbiculariae: Deinopoidea, Araneoidea). Zool J Linn Soc 1998, 123(1):1-99.
    • (1998) Zool J Linn Soc , vol.123 , Issue.1 , pp. 1-99
    • Griswold, C.E.1    Coddington, J.A.2    Hormiga, G.3    Scharff, N.4
  • 45
    • 45349087762 scopus 로고    scopus 로고
    • Fine structureal analysis of secretory silk production in the black widow spider, Latrodectus mactans
    • Moon MJ, Townley MA, Tillinghast EK. Fine structureal analysis of secretory silk production in the black widow spider, Latrodectus mactans. Korean J Biol Sci 1998, 2:145-152.
    • (1998) Korean J Biol Sci , vol.2 , pp. 145-152
    • Moon, M.J.1    Townley, M.A.2    Tillinghast, E.K.3
  • 46
    • 0042430621 scopus 로고    scopus 로고
    • Genome sizes of spiders
    • 10.1093/jhered/esg070, 12920099
    • Gregory TR, Shorthouse DP. Genome sizes of spiders. J Hered 2003, 94(4):285-290. 10.1093/jhered/esg070, 12920099.
    • (2003) J Hered , vol.94 , Issue.4 , pp. 285-290
    • Gregory, T.R.1    Shorthouse, D.P.2
  • 47
    • 84873588081 scopus 로고    scopus 로고
    • Ancient properties of spider silks revealed by the complete gene sequence of the prey-wrapping silk protein (AcSp1)
    • 10.1093/molbev/mss254, 3563967, 23155003
    • Ayoub NA, Garb JE, Kuelbs A, Hayashi CY. Ancient properties of spider silks revealed by the complete gene sequence of the prey-wrapping silk protein (AcSp1). Mol Biol Evol 2013, 30(3):589-601. 10.1093/molbev/mss254, 3563967, 23155003.
    • (2013) Mol Biol Evol , vol.30 , Issue.3 , pp. 589-601
    • Ayoub, N.A.1    Garb, J.E.2    Kuelbs, A.3    Hayashi, C.Y.4
  • 48
    • 0033970022 scopus 로고    scopus 로고
    • Expectations from structural genomics
    • 2144435, 10739263
    • Brenner SE, Levitt M. Expectations from structural genomics. Protein Sci 2000, 9(1):197-200. 2144435, 10739263.
    • (2000) Protein Sci , vol.9 , Issue.1 , pp. 197-200
    • Brenner, S.E.1    Levitt, M.2
  • 49
    • 0033768266 scopus 로고    scopus 로고
    • Target selection for structural genomics
    • Brenner SE. Target selection for structural genomics. Nat Struct Biol 2000, 7(SUPPL):967-969.
    • (2000) Nat Struct Biol , vol.7 , Issue.SUPPL , pp. 967-969
    • Brenner, S.E.1
  • 50
    • 2942553957 scopus 로고    scopus 로고
    • The use of MPSS for whole-genome transcriptional analysis in Arabidopsis
    • 10.1101/gr.2275604, 509274, 15289482
    • Meyers BC, Tej SS, Vu TH, Haudenschild CD, Agrawal V, Edberg SB, Ghazal H, Decola S. The use of MPSS for whole-genome transcriptional analysis in Arabidopsis. Genome Res 2004, 14(8):1641-1653. 10.1101/gr.2275604, 509274, 15289482.
    • (2004) Genome Res , vol.14 , Issue.8 , pp. 1641-1653
    • Meyers, B.C.1    Tej, S.S.2    Vu, T.H.3    Haudenschild, C.D.4    Agrawal, V.5    Edberg, S.B.6    Ghazal, H.7    Decola, S.8
  • 51
    • 38049091067 scopus 로고    scopus 로고
    • Gene expression profiling by massively parallel sequencing
    • 2134766, 18032722
    • Torres TT, Metta M, Ottenwälder B, Schlötterer C. Gene expression profiling by massively parallel sequencing. Genome Res 2008, 18(1):172-177. 2134766, 18032722.
    • (2008) Genome Res , vol.18 , Issue.1 , pp. 172-177
    • Torres, T.T.1    Metta, M.2    Ottenwälder, B.3    Schlötterer, C.4
  • 53
    • 75249087100 scopus 로고    scopus 로고
    • EdgeR: a bioconductor package for differential expression analysis of digital gene expression data
    • 10.1093/bioinformatics/btp616, 2796818, 19910308
    • Robinson MD, McCarthy DJ, Smyth GK. edgeR: a bioconductor package for differential expression analysis of digital gene expression data. Bioinformatics 2010, 26(1):139-140. 10.1093/bioinformatics/btp616, 2796818, 19910308.
    • (2010) Bioinformatics , vol.26 , Issue.1 , pp. 139-140
    • Robinson, M.D.1    McCarthy, D.J.2    Smyth, G.K.3
  • 54
    • 58149528403 scopus 로고    scopus 로고
    • Antisense transcription: a critical look in both directions
    • 10.1007/s00018-008-8381-y, 18791843
    • Beiter T, Reich E, Williams RW, Simon P. Antisense transcription: a critical look in both directions. Cell Mol Life Sci 2009, 66(1):94-112. 10.1007/s00018-008-8381-y, 18791843.
    • (2009) Cell Mol Life Sci , vol.66 , Issue.1 , pp. 94-112
    • Beiter, T.1    Reich, E.2    Williams, R.W.3    Simon, P.4
  • 55
    • 26944454054 scopus 로고    scopus 로고
    • Evidence for a preferential targeting of 3′-UTRs by cis-encoded natural antisense transcripts
    • 10.1093/nar/gki852, 1243798, 16204454
    • Sun M, Hurst LD, Carmichael GG, Chen J. Evidence for a preferential targeting of 3′-UTRs by cis-encoded natural antisense transcripts. Nucleic Acids Res 2005, 33(17):5533-5543. 10.1093/nar/gki852, 1243798, 16204454.
    • (2005) Nucleic Acids Res , vol.33 , Issue.17 , pp. 5533-5543
    • Sun, M.1    Hurst, L.D.2    Carmichael, G.G.3    Chen, J.4
  • 57
    • 84872775027 scopus 로고    scopus 로고
    • Translational control by 3′-UTR-binding proteins
    • 10.1093/bfgp/els056, 3548161, 23196851
    • Szostak E, Gebauer F. Translational control by 3′-UTR-binding proteins. Brief Funct Genomics 2013, 12(1):58-65. 10.1093/bfgp/els056, 3548161, 23196851.
    • (2013) Brief Funct Genomics , vol.12 , Issue.1 , pp. 58-65
    • Szostak, E.1    Gebauer, F.2
  • 58
    • 13744260273 scopus 로고    scopus 로고
    • Gumfooted lines in black widow cobwebs and the mechanical properties of spider capture silk
    • 10.1016/j.zool.2004.11.001, 16351953
    • Blackledge TA, Summers AP, Hayashi CY. Gumfooted lines in black widow cobwebs and the mechanical properties of spider capture silk. Zoology 2005, 108(1):41-46. 10.1016/j.zool.2004.11.001, 16351953.
    • (2005) Zoology , vol.108 , Issue.1 , pp. 41-46
    • Blackledge, T.A.1    Summers, A.P.2    Hayashi, C.Y.3
  • 59
    • 84857422251 scopus 로고    scopus 로고
    • Variation in protein intake induces variation in spider silk expression
    • 10.1371/journal.pone.0031626, 3282770, 22363691
    • Blamires SJ, Wu CL, Tso IM. Variation in protein intake induces variation in spider silk expression. PLoS ONE 2012, 7(2):e31626. 10.1371/journal.pone.0031626, 3282770, 22363691.
    • (2012) PLoS ONE , vol.7 , Issue.2
    • Blamires, S.J.1    Wu, C.L.2    Tso, I.M.3
  • 60
    • 77949769815 scopus 로고    scopus 로고
    • Silk gene transcripts in the developing tubuliform glands of the Western black widow, Latrodectus hesperus
    • Casem ML, Collin MA, Ayoub NA, Hayashi CY. Silk gene transcripts in the developing tubuliform glands of the Western black widow, Latrodectus hesperus. J Arachnol 2010, 38(1):99-103.
    • (2010) J Arachnol , vol.38 , Issue.1 , pp. 99-103
    • Casem, M.L.1    Collin, M.A.2    Ayoub, N.A.3    Hayashi, C.Y.4
  • 61
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • 10.1038/nmeth.1701, 21959131
    • Petersen TN, Brunak S, Von Heijne G, Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 2011, 8(10):785-786. 10.1038/nmeth.1701, 21959131.
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 63
    • 80052979140 scopus 로고    scopus 로고
    • Mechanisms and consequences of alternative polyadenylation
    • 10.1016/j.molcel.2011.08.017, 3194005, 21925375
    • Giammartino D, Nishida K, Manley J. Mechanisms and consequences of alternative polyadenylation. Mol Cell 2011, 43:853-866. 10.1016/j.molcel.2011.08.017, 3194005, 21925375.
    • (2011) Mol Cell , vol.43 , pp. 853-866
    • Giammartino, D.1    Nishida, K.2    Manley, J.3
  • 64
    • 84869104652 scopus 로고    scopus 로고
    • Introns in UTRs: why we should stop ignoring them
    • 10.1002/bies.201200073, 23108796
    • Bicknell A, Cenik C, Chua H, Roth F, Moore M. Introns in UTRs: why we should stop ignoring them. Bioessays 2012, 34:1025-1034. 10.1002/bies.201200073, 23108796.
    • (2012) Bioessays , vol.34 , pp. 1025-1034
    • Bicknell, A.1    Cenik, C.2    Chua, H.3    Roth, F.4    Moore, M.5
  • 65
    • 0027518295 scopus 로고
    • Expression and structural studies of fasciclin I, an insect cell adhesion molecule
    • January 14
    • Wang W, Zinn K, Bjorkman PJ. Expression and structural studies of fasciclin I, an insect cell adhesion molecule. J Biol Chem 1993, 268(January 14):1448-1455.
    • (1993) J Biol Chem , vol.268 , pp. 1448-1455
    • Wang, W.1    Zinn, K.2    Bjorkman, P.J.3
  • 66
    • 84855902153 scopus 로고    scopus 로고
    • Adaptive evolution of a novel Drosophila lectin induced by parasitic wasp attack
    • 10.1093/molbev/msr191, 3258034, 21873297
    • Keebaugh ES, Schlenke TA. Adaptive evolution of a novel Drosophila lectin induced by parasitic wasp attack. Mol Biol Evol 2012, 29(2):565-577. 10.1093/molbev/msr191, 3258034, 21873297.
    • (2012) Mol Biol Evol , vol.29 , Issue.2 , pp. 565-577
    • Keebaugh, E.S.1    Schlenke, T.A.2
  • 67
    • 33846902097 scopus 로고    scopus 로고
    • Drosophila C-type lectins enhance cellular encapsulation
    • 10.1016/j.molimm.2006.12.024, 1876673, 17287021
    • Ao J, Ling E, Yu X. Drosophila C-type lectins enhance cellular encapsulation. Mol Immunol 2007, 44(10):2541-2548. 10.1016/j.molimm.2006.12.024, 1876673, 17287021.
    • (2007) Mol Immunol , vol.44 , Issue.10 , pp. 2541-2548
    • Ao, J.1    Ling, E.2    Yu, X.3
  • 68
    • 2542585370 scopus 로고    scopus 로고
    • Spider silk protein refolding is controlled by changing pH
    • 10.1021/bm034307c, 15132650
    • Dicko C, Vollrath F, Kenney JM. Spider silk protein refolding is controlled by changing pH. Biomacromolecules 2004, 5(3):704-710. 10.1021/bm034307c, 15132650.
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 704-710
    • Dicko, C.1    Vollrath, F.2    Kenney, J.M.3
  • 69
    • 0000008924 scopus 로고
    • The pathway and control of serine biosynthesis in Escherichia coli
    • Pizer L. The pathway and control of serine biosynthesis in Escherichia coli. J Biol Chem 1963, 238(12):3934-3944.
    • (1963) J Biol Chem , vol.238 , Issue.12 , pp. 3934-3944
    • Pizer, L.1
  • 70
    • 84867576301 scopus 로고    scopus 로고
    • γ-Glutamyltranspeptidases: sequence, structure, biochemical properties, and biotechnological applications
    • 10.1007/s00018-012-0988-3, 22527720
    • Castellano I, Merlino A. γ-Glutamyltranspeptidases: sequence, structure, biochemical properties, and biotechnological applications. Cell Mol Life Sci 2012, 69(20):3381-3394.71. 10.1007/s00018-012-0988-3, 22527720.
    • (2012) Cell Mol Life Sci , vol.69 , Issue.20
    • Castellano, I.1    Merlino, A.2
  • 71
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: A DNA sequence assembly program
    • 10.1101/gr.9.9.868, 310812, 10508846
    • Huang X, Madan A. CAP3: A DNA sequence assembly program. Genome Res 1999, 9(9):868-877. 10.1101/gr.9.9.868, 310812, 10508846.
    • (1999) Genome Res , vol.9 , Issue.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 75
    • 33644872577 scopus 로고    scopus 로고
    • Limma: linear models for microarray data
    • New York: Springer, Gentleman R, Carey VJ, Dudoit S, Irizarry R, Huber W
    • Smyth GK. Limma: linear models for microarray data. Bioinformatics and Computational Biology Solutions using R and Bioconductor 2005, 397-420. New York: Springer, Gentleman R, Carey VJ, Dudoit S, Irizarry R, Huber W.
    • (2005) Bioinformatics and Computational Biology Solutions using R and Bioconductor , pp. 397-420
    • Smyth, G.K.1
  • 76
    • 77953176036 scopus 로고    scopus 로고
    • A scaling normalization method for differential expression analysis of RNA-seq data
    • 10.1186/gb-2010-11-3-r25, 2864565, 20196867
    • Robinson MD, Oshlack A. A scaling normalization method for differential expression analysis of RNA-seq data. Genome Biol 2010, 11(3):R25. 10.1186/gb-2010-11-3-r25, 2864565, 20196867.
    • (2010) Genome Biol , vol.11 , Issue.3
    • Robinson, M.D.1    Oshlack, A.2
  • 77
    • 41149085992 scopus 로고    scopus 로고
    • Small-sample estimation of negative binomial dispersion, with applications to SAGE data
    • Robinson MD, Smyth GK. Small-sample estimation of negative binomial dispersion, with applications to SAGE data. Biostatistics 2008, 9(2):321-332.
    • (2008) Biostatistics , vol.9 , Issue.2 , pp. 321-332
    • Robinson, M.D.1    Smyth, G.K.2
  • 78
    • 36448981743 scopus 로고    scopus 로고
    • Moderated statistical tests for assessing differences in tag abundance
    • 10.1093/bioinformatics/btm453, 17881408
    • Robinson MD, Smyth GK. Moderated statistical tests for assessing differences in tag abundance. Bioinformatics 2007, 23(21):2881-2887. 10.1093/bioinformatics/btm453, 17881408.
    • (2007) Bioinformatics , vol.23 , Issue.21 , pp. 2881-2887
    • Robinson, M.D.1    Smyth, G.K.2
  • 79
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Series B
    • Benjamini Y, Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J R Stat Soc Series B Stat Methodol 1995, Series B(57):289-300.
    • (1995) J R Stat Soc Series B Stat Methodol , Issue.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.