메뉴 건너뛰기




Volumn 5, Issue 1, 2014, Pages 1-19

Experimental strategies for the identification and characterization of adhesive proteins in animals: A review

Author keywords

Biological adhesion; Metazoans; Protein characterization

Indexed keywords


EID: 84919391352     PISSN: 20428898     EISSN: 20428901     Source Type: Journal    
DOI: 10.1098/rsfs.2014.0064     Document Type: Article
Times cited : (62)

References (161)
  • 1
    • 41249103077 scopus 로고    scopus 로고
    • Biological attachment devices: Exploring nature's diversity for biomimetics
    • Gorb S. 2008 Biological attachment devices: exploring nature's diversity for biomimetics. Phil. Trans. R. Soc. A 366, 1557–1574. (doi:10.1098/rsta.2007.2172)
    • (2008) Phil. Trans. R. Soc. A , vol.366 , pp. 1557-1574
    • Gorb, S.1
  • 3
    • 0003139123 scopus 로고
    • Adhesion in byssally attached bivalves
    • Waite JH. 1983 Adhesion in byssally attached bivalves. Biol. Rev. 58, 209–231. (doi:10.1111/j.1469-185X.1983.tb00387.x)
    • (1983) Biol. Rev , vol.58 , pp. 209-231
    • Waite, J.H.1
  • 7
    • 84885626440 scopus 로고    scopus 로고
    • Accelerating the design of biomimetic materials by integrating RNA-seq with proteomics and materials science
    • Guerette PA et al. 2013 Accelerating the design of biomimetic materials by integrating RNA-seq with proteomics and materials science. Nat. Biotechnol. 31, 908–915. (doi:10.1038/nbt.2671)
    • (2013) Nat. Biotechnol , vol.31 , pp. 908-915
    • Guerette, P.A.1
  • 9
    • 0035947715 scopus 로고    scopus 로고
    • Molecular cloning and characterization of spiggin. An androgen-regulated extraorganismal adhesive with structural similarities to von Willebrand factor-related proteins
    • Jones I, Lindberg C, Jakobsson S, Hellqvist A, Hellman U, Borg B, Olsson PE. 2001 Molecular cloning and characterization of spiggin. An androgen-regulated extraorganismal adhesive with structural similarities to von Willebrand factor-related proteins. J. Biol. Chem. 276, 17857–17863. (doi:10.1074/jbc.M101142200)
    • (2001) J. Biol. Chem , vol.276 , pp. 17857-17863
    • Jones, I.1    Lindberg, C.2    Jakobsson, S.3    Hellqvist, A.4    Hellman, U.5    Borg, B.6    Olsson, B.7
  • 10
    • 77958122939 scopus 로고    scopus 로고
    • Harnessing disorder: Onychophorans use highly unstructured proteins, not silks, for prey capture
    • Haritos VS, Niranjane A, Weisman S, Trueman HE, Sriskantha A, Sutherland TD. 2010 Harnessing disorder: onychophorans use highly unstructured proteins, not silks, for prey capture. Proc. R. Soc. B 277, 3255–3263. (doi:10.1098/rspb.2010.0604)
    • (2010) Proc. R. Soc. B , vol.277 , pp. 3255-3263
    • Haritos, V.S.1    Niranjane, A.2    Weisman, S.3    Trueman, H.E.4    Sriskantha, A.5    Sutherland, T.D.6
  • 11
    • 34547774153 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel barnacle cement protein
    • Urushida Y, Nakano M, Matsuda S, Inoue N, Kanai S, Kitamura N, Nishino T, Kamino K. 2007 Identification and functional characterization of a novel barnacle cement protein. FEBS J. 274, 4336–4346. (doi:10.1111/j.1742-4658.2007.05965.x)
    • (2007) FEBS J , vol.274 , pp. 4336-4346
    • Urushida, Y.1    Nakano, M.2    Matsuda, S.3    Inoue, N.4    Kanai, S.5    Kitamura, N.6    Nishino, T.7    Kamino, K.8
  • 12
    • 0035366508 scopus 로고    scopus 로고
    • Novel barnacle underwater adhesive protein is a charged amino acid-rich protein constituted by a Cys-rich repetitive sequence
    • Kamino K. 2001 Novel barnacle underwater adhesive protein is a charged amino acid-rich protein constituted by a Cys-rich repetitive sequence. Biochem. J. 356, 503–507. (doi:10.1042/0264-6021:3560503)
    • (2001) Biochem. J , vol.356 , pp. 503-507
    • Kamino, K.1
  • 13
    • 84860344578 scopus 로고    scopus 로고
    • Significance of the conformation of building blocks in curing of barnacle underwater adhesive
    • Kamino K, Nakano M, Kanai S. 2012 Significance of the conformation of building blocks in curing of barnacle underwater adhesive. FEBS J. 279, 1750–1760. (doi:10.1111/j.1742-4658.2012.08552.x)
    • (2012) FEBS J , vol.279 , pp. 1750-1760
    • Kamino, K.1    Nakano, M.2    Kanai, S.3
  • 14
    • 0034282718 scopus 로고    scopus 로고
    • Barnacle cement proteins. Importance of disulfide bonds in their insolubility
    • Kamino K, Inoue K, Murayama T, Takamatsu N, Harayama S, Shizuri Y. 2000 Barnacle cement proteins. Importance of disulfide bonds in their insolubility. J. Biol. Chem. 275, 27360–27365. (doi:10.1074/jbc.M910363199)
    • (2000) J. Biol. Chem , vol.275 , pp. 27360-27365
    • Kamino, K.1    Inoue, K.2    Murayama, T.3    Takamatsu, N.4    Harayama, S.5    Shizuri, Y.6
  • 15
    • 36749013620 scopus 로고    scopus 로고
    • Calcite-specific coupling protein in barnacle underwater cement
    • Mori Y, Urushida Y, Nakano M, Uchiyama S, Kamino K. 2007 Calcite-specific coupling protein in barnacle underwater cement. FEBS J. 274, 6436–6446. (doi:10.1111/j.1742-4658.2007.06161.x)
    • (2007) FEBS J , vol.274 , pp. 6436-6446
    • Mori, Y.1    Urushida, Y.2    Nakano, M.3    Uchiyama, S.4    Kamino, K.5
  • 16
    • 70350063816 scopus 로고    scopus 로고
    • Spider web glue. Two proteins expressed from opposite strands of the same DNA sequence
    • Choresh 0, Bayarmagnai B, Lewis RV. 2009 Spider web glue. Two proteins expressed from opposite strands of the same DNA sequence. Biomacromolecules 10, 2852–2856. (doi:10.1021/bm900681w)
    • (2009) Biomacromolecules , vol.10 , pp. 2852-2856
    • Choresh 0, B.B.1    Bayarmagnai, B.2    Lewis, R.V.3
  • 17
    • 78650292103 scopus 로고    scopus 로고
    • Synthetic spider silk fibers spun from pyriform spidroin 2, a glue silk protein discovered in orb-weaving spider attachment discs
    • Geurts P et al. 2010 Synthetic spider silk fibers spun from pyriform spidroin 2, a glue silk protein discovered in orb-weaving spider attachment discs. Biomacromolecules 11, 3495–3503. (doi:10.1021/bm101002w)
    • (2010) Biomacromolecules , vol.11 , pp. 3495-3503
    • Geurts, P.1
  • 18
    • 84867824150 scopus 로고    scopus 로고
    • Spider glue proteins have distinct architectures compared with traditional spidroin family members
    • Vasanthavada K et al. 2012 Spider glue proteins have distinct architectures compared with traditional spidroin family members. J. Biol. Chem. 287, 35986–35999. (doi:10.1074/jbc.M112.399816)
    • (2012) J. Biol. Chem , vol.287 , pp. 35986-35999
    • Vasanthavada, K.1
  • 19
    • 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
    • Blasingame E et al. 2009 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. 284, 29097–29108. (doi:10.1074/jbc.M109.021378)
    • (2009) J. Biol. Chem , vol.284 , pp. 29097-29108
    • Blasingame, E.1
  • 20
    • 0036275989 scopus 로고    scopus 로고
    • A cement protein of the tick Rhipicephalus appendiculatus, located in the secretory e-granules of the type III salivary gland acini, induces strong antibody responses in cattle
    • Bishop R, Lambson B, Wells C, Pandit P, Osaso J, Nkonge C, Morzaria S, Musoke A, Nene V. 2002 A cement protein of the tick Rhipicephalus appendiculatus, located in the secretory e-granules of the type III salivary gland acini, induces strong antibody responses in cattle. Int. J. Parasitol. 32, 833–842. (doi:10.1016/S0020-7519(02)00027-9)
    • (2002) Int. J. Parasitol , vol.32 , pp. 833-842
    • Bishop, R.1    Lambson, B.2    Wells, C.3    Pandit, P.4    Osaso, J.5    Nkonge, C.6    Morzaria, S.7    Musoke, A.8    Nene, V.9
  • 21
    • 0037019903 scopus 로고    scopus 로고
    • Dual action ectoparasite vaccine targeting ‘exposed’ and ‘concealed’ antigens
    • Trimnell AR, Hails RS, Nuttall PA. 2002 Dual action ectoparasite vaccine targeting ‘exposed’ and ‘concealed’ antigens. Vaccine 20, 3560–3568. (doi:10.1016/S0264-410X(02)00334-1)
    • (2002) Vaccine , vol.20 , pp. 3560-3568
    • Trimnell, A.R.1    Hails, R.S.2    Nuttall, P.A.3
  • 22
    • 33751225103 scopus 로고    scopus 로고
    • Identification of a glycine-rich protein from the tick Rhipicephalus haemaphysaloides and evaluation of its vaccine potential against tick feeding
    • Zhou J, Gong H, Zhou Y, Xuan X, Fujisaki K. 2006 Identification of a glycine-rich protein from the tick Rhipicephalus haemaphysaloides and evaluation of its vaccine potential against tick feeding. Parasitol. Res. 100, 77–84. (doi:10.1007/s00436-006-0243-7)
    • (2006) Parasitol. Res , vol.100 , pp. 77-84
    • Zhou, J.1    Gong, H.2    Zhou, Y.3    Xuan, X.4    Fujisaki, K.5
  • 23
    • 0032051872 scopus 로고    scopus 로고
    • A Major protein precursor of zebra mussel (Dreissena polymorpha) byssus: Deduced sequence and significance
    • Anderson K, Waite JH. 1998 A Major protein precursor of zebra mussel (Dreissena polymorpha) byssus: deduced sequence and significance. Biol. Bull. 194, 150–160. (doi:10.2307/1543045)
    • (1998) Biol. Bull , vol.194 , pp. 150-160
    • Anderson, K.1    Waite, J.H.2
  • 24
  • 25
    • 33744954494 scopus 로고    scopus 로고
    • Probing the adhesive footprints of Mytilus californianus byssus
    • Zhao H, Robertson NB, Jewhurst SA, Waite JH. 2006 Probing the adhesive footprints of Mytilus californianus byssus. J. Biol. Chem. 281, 11090–11096. (doi:10.1074/jbc.M510792200)
    • (2006) J. Biol. Chem , vol.281 , pp. 11090-11096
    • Zhao, H.1    Robertson, N.B.2    Jewhurst, S.A.3    Waite, J.H.4
  • 26
    • 33748743983 scopus 로고    scopus 로고
    • Linking adhesive and structural proteins in the attachment plaque of Mytilus californianus
    • Zhao H, Waite JH. 2006 Linking adhesive and structural proteins in the attachment plaque of Mytilus californianus. J. Biol. Chem. 281, 26150–26158. (doi:10.1074/jbc.M604357200)
    • (2006) J. Biol. Chem , vol.281 , pp. 26150-26158
    • Zhao, H.1    Waite, J.H.2
  • 27
    • 36749099994 scopus 로고    scopus 로고
    • Understanding marine mussel adhesion
    • Silverman HG, Roberto FF. 2007 Understanding marine mussel adhesion. Mar. Biotechnol. 9, 661–681. (doi:10.1007/s10126-007-9053-x)
    • (2007) Mar. Biotechnol , vol.9 , pp. 661-681
    • Silverman, H.G.1    Roberto, F.F.2
  • 28
    • 0032850312 scopus 로고    scopus 로고
    • Expression of multiple forms of an adhesive plaque protein in an individual mussel
    • Warner SC, Waite JH. 1999 Expression of multiple forms of an adhesive plaque protein in an individual mussel, Mytilus edulis. Mar. Biol. 134, 729–734. (doi:10.1007/s002270050589)
    • (1999) Mytilus Edulis. Mar. Biol , vol.134 , pp. 729-734
    • Warner, S.C.1    Waite, J.H.2
  • 29
    • 0035814883 scopus 로고    scopus 로고
    • Polyphosphoprotein from the adhesive pads of Mytilus edulis
    • Waite JH, Qin X. 2001 Polyphosphoprotein from the adhesive pads of Mytilus edulis. Biochemistry 40, 2887–2893. (doi:10.1021/bi002718x)
    • (2001) Biochemistry , vol.40 , pp. 2887-2893
    • Waite, J.H.1    Qin, X.2
  • 30
    • 0028445988 scopus 로고
    • The adhesive protein cDNA of Mytilus galloprovincialis encodes decapeptide repeats but no hexapeptide motif
    • Inoue K, Odo S. 1994 The adhesive protein cDNA of Mytilus galloprovincialis encodes decapeptide repeats but no hexapeptide motif. Biol. Bull. 186, 349–355. (doi:10.2307/1542281)
    • (1994) Biol. Bull , vol.186 , pp. 349-355
    • Inoue, K.1    Odo, S.2
  • 31
    • 2942532196 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli
    • Hwang DS, Yoo HJ, Jun JH, Moon WK, Cha HJ. 2004 Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli. Appl. Environ. Microbiol. 70, 3352–3359. (doi:10.1128/AEM.70.6.3352-3359.2004)
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 3352-3359
    • Hwang, D.S.1    Yoo, H.J.2    Jun, J.H.3    Moon, W.K.4    Cha, H.J.5
  • 32
    • 69949149109 scopus 로고    scopus 로고
    • Glycosylated hydroxytryptophan in a mussel adhesive protein from Perna viridis
    • Zhao H, Sagert J, Hwang DS, Waite JH. 2009 Glycosylated hydroxytryptophan in a mussel adhesive protein from Perna viridis. J. Biol. Chem. 284, 23344–23352. (doi:10.1074/jbc.M109.022517)
    • (2009) J. Biol. Chem , vol.284 , pp. 23344-23352
    • Zhao, H.1    Sagert, J.2    Hwang, D.S.3    Waite, J.H.4
  • 33
    • 35448949632 scopus 로고    scopus 로고
    • Epidermal secretions of terrestrial flatworms and slugs: Lehmannia valentiana mucus contains matrilin-like proteins
    • Li D, Graham L. 2007 Epidermal secretions of terrestrial flatworms and slugs: Lehmannia valentiana mucus contains matrilin-like proteins. Comp. Biochem. Phys. B 148, 231–244. (doi:10.1016/j.cbpb.2007.06.001)
    • (2007) Comp. Biochem. Phys. B , vol.148 , pp. 231-244
    • Li, D.1    Graham, L.2
  • 34
    • 30044452034 scopus 로고    scopus 로고
    • Cement proteins of the tube-building polychaete Phragmatopoma californica
    • Zhao H, Sun C, Stewart RJ, Waite JH. 2005 Cement proteins of the tube-building polychaete Phragmatopoma californica. J. Biol. Chem. 280, 42938–42944. (doi:10.1074/jbc.M508457200)
    • (2005) J. Biol. Chem , vol.280 , pp. 42938-42944
    • Zhao, H.1    Sun, C.2    Stewart, R.J.3    Waite, J.H.4
  • 35
    • 69349091497 scopus 로고    scopus 로고
    • Glueomics: An expression survey of the adhesive gland of the sandcastle worm
    • Endrizzi BJ, Stewart RJ. 2009 Glueomics: an expression survey of the adhesive gland of the sandcastle worm. J. Adhesion 85, 546–559. (doi:10.1080/00218460902996457)
    • (2009) J. Adhesion , vol.85 , pp. 546-559
    • Endrizzi, B.J.1    Stewart, R.J.2
  • 36
    • 84869072983 scopus 로고    scopus 로고
    • Identification, characterization, and expression levels of putative adhesive proteins from the tube-dwelling polychaete Sabellaria alveolata
    • Becker PT, Lambert A, Lejeune A, Lanterbecq D, Flammang P. 2012 Identification, characterization, and expression levels of putative adhesive proteins from the tube-dwelling polychaete Sabellaria alveolata. Biol. Bull. 223, 217–225. (doi:10.2307/41759008)
    • (2012) Biol. Bull , vol.223 , pp. 217-225
    • Becker, P.T.1    Lambert, A.2    Lejeune, A.3    Lanterbecq, D.4    Flammang, P.5
  • 37
    • 33751183224 scopus 로고    scopus 로고
    • Adhesive secretions in echinoderms: An overview
    • (eds AM Smith, JA Callow, Berlin, Germany: Springer
    • Flammang P. 2006 Adhesive secretions in echinoderms: an overview. In Biological adhesives (eds AM Smith, JA Callow), pp. 183–206. Berlin, Germany: Springer.
    • (2006) Biological Adhesives , pp. 183-206
    • Flammang, P.1
  • 38
    • 0001812635 scopus 로고    scopus 로고
    • Adhesion in echinoderms
    • (eds M Jangoux, JM Lawrence, Rotterdam, The Netherlands: Balkema
    • Flammang P. 1996 Adhesion in echinoderms. In Echinoderm studies (eds M Jangoux, JM Lawrence), pp. 1–60. Rotterdam, The Netherlands: Balkema.
    • (1996) Echinoderm Studies , pp. 1-60
    • Flammang, P.1
  • 39
    • 0031691654 scopus 로고    scopus 로고
    • A study of the temporary adhesion of the podia in the sea star Asterias rubens (Echinodermata, Asteroidea) through their footprints
    • Flammang P, Michel A, Van Cauwenberge A, Alexandre H, Jangoux M. 1998 A study of the temporary adhesion of the podia in the sea star Asterias rubens (Echinodermata, Asteroidea) through their footprints. J. Exp. Biol. 201, 2383–2395.
    • (1998) J. Exp. Biol , vol.201 , pp. 2383-2395
    • Flammang, P.1    Michel, A.2    Van Cauwenberge, A.3    Alexandre, H.4    Jangoux, M.5
  • 40
    • 51749098978 scopus 로고    scopus 로고
    • Micro- and nanostructure of the adhesive material secreted by the tube feet of the sea starAsterias rubens
    • Hennebert E, Viville P, Lazzaroni R, Flammang P. 2008 Micro- and nanostructure of the adhesive material secreted by the tube feet of the sea star Asterias rubens. J. Struct. Biol. 164, 108–118. (doi:10.1016/j.jsb.2008.06.007)
    • (2008) J. Struct. Biol , vol.164 , pp. 108-118
    • Hennebert, E.1    Viville, P.2    Lazzaroni, R.3    Flammang, P.4
  • 41
    • 70449517481 scopus 로고    scopus 로고
    • First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata)
    • Santos R, da Costa G, Franco C, Gomes-Alves P, Flammang P, Coelho AV. 2009 First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata). Mar. Biotechnol. 11, 686–698. (doi:10.1007/s10126-009-9182-5)
    • (2009) Mar. Biotechnol , vol.11 , pp. 686-698
    • Santos, R.1    Da Costa, G.2    Franco, C.3    Gomes-Alves, P.4    Flammang, P.5    Coelho, A.V.6
  • 42
    • 84859499654 scopus 로고    scopus 로고
    • Characterization of the protein fraction of the temporary adhesive secreted by the tube feet of the sea star
    • Hennebert E, Wattiez R, Waite JH, Flammang P. 2012 Characterization of the protein fraction of the temporary adhesive secreted by the tube feet of the sea star Asterias rubens. Biofouling. 28, 289–303. (doi:10.1080/08927014.2012.672645)
    • (2012) Asterias Rubens. Biofouling , vol.28 , pp. 289-303
    • Hennebert, E.1    Wattiez, R.2    Waite, J.H.3    Flammang, P.4
  • 43
    • 0002032995 scopus 로고
    • The adhesion of barnacles
    • Walker G. 1981 The adhesion of barnacles. J. Adhesion 12, 51–58. (doi:10.1080/00218468108071188)
    • (1981) J. Adhesion , vol.12 , pp. 51-58
    • Walker, G.1
  • 44
    • 40449140938 scopus 로고    scopus 로고
    • Underwater adhesive of marine organisms as the vital link between biological science and material science
    • Kamino K. 2008 Underwater adhesive of marine organisms as the vital link between biological science and material science. Mar. Biotechnol. 10, 111–121. (doi:10.1007/s10126-007-9076-3)
    • (2008) Mar. Biotechnol , vol.10 , pp. 111-121
    • Kamino, K.1
  • 45
    • 0001647553 scopus 로고
    • A comparative study of the cement glands in some balanid barnacles (Cirripedia, Balanidae)
    • Lacombre D. 1970 A comparative study of the cement glands in some balanid barnacles (Cirripedia, Balanidae). Biol. Bull. 139, 164–179. (doi:10.2307/1540134)
    • (1970) Biol. Bull , vol.139 , pp. 164-179
    • Lacombre, D.1
  • 47
    • 84869088121 scopus 로고    scopus 로고
    • Unusual adhesive production system in the barnacle Lepas anatifera: An ultrastructural and histochemical investigation
    • Jonker JL, von Byern J, Flammang P, Klepal W, Power AM. 2012 Unusual adhesive production system in the barnacle Lepas anatifera: an ultrastructural and histochemical investigation. J. Morphol. 273, 1377–1391. (doi:10.1002/jmor.20067)
    • (2012) J. Morphol , vol.273 , pp. 1377-1391
    • Jonker, J.L.1    Von Byern, J.2    Flammang, P.3    Klepal, W.4    Power, A.M.5
  • 48
    • 84971925589 scopus 로고
    • The biochemical composition of the cement of two barnacle species, Balanus hameri and Balanus crenatus
    • Walker G. 1972 The biochemical composition of the cement of two barnacle species, Balanus hameri and Balanus crenatus. J. Mar. Biol. Assoc. UK 52, 429–435. (doi:10.1017/S0025315400018786)
    • (1972) J. Mar. Biol. Assoc. UK , vol.52 , pp. 429-435
    • Walker, G.1
  • 49
    • 34347357100 scopus 로고    scopus 로고
    • Barnacle underwater attachment
    • (eds AM Smith, JA Callow, Berlin, Germany: Springer
    • Kamino K. 2006 Barnacle underwater attachment. In Biological adhesives (eds AM Smith, JA Callow), pp. 145–166. Berlin, Germany: Springer.
    • (2006) Biological Adhesives , pp. 145-166
    • Kamino, K.1
  • 50
    • 76649134410 scopus 로고    scopus 로고
    • Molecular design of barnacle cement in comparison with those of mussel and tubeworm
    • Kamino K. 2010 Molecular design of barnacle cement in comparison with those of mussel and tubeworm. J. Adhesion 86, 96–110. (doi:10.1080/00218460903418139)
    • (2010) J. Adhesion , vol.86 , pp. 96-110
    • Kamino, K.1
  • 51
    • 0003872735 scopus 로고    scopus 로고
    • Oxford, UK: Oxford University Press
    • Rouse G, Pleijel F. 2001 Polychaetes. Oxford, UK: Oxford University Press.
    • (2001) Polychaetes
    • Rouse, G.1    Pleijel, F.2
  • 52
    • 0002670306 scopus 로고
    • The tube of Sabellaria alveolata
    • Vovelle J. 1965 The tube of Sabellaria alveolata. Arch. Zool. Exp. Gen. 106, 1–187.
    • (1965) Arch. Zool. Exp. Gen , vol.106 , pp. 1-187
    • Vovelle, J.1
  • 53
    • 13144282764 scopus 로고    scopus 로고
    • The tube cement of Phragmatopoma californica: A solid foam
    • Stewart RJ, Weaver JC, Morse DE, Waite JH. 2004 The tube cement of Phragmatopoma californica: a solid foam. J. Exp. Biol. 207, 4727–4734. (doi:10.1242/jeb.01330)
    • (2004) J. Exp. Biol , vol.207 , pp. 4727-4734
    • Stewart, R.J.1    Weaver, J.C.2    Morse, D.E.3    Waite, J.H.4
  • 54
    • 34248362688 scopus 로고    scopus 로고
    • Multiscale structure of the underwater adhesive of Phragmatopoma californica: A nanostructured latex with a steep microporosity gradient
    • Stevens MJ, Steren RE, Vlamidir H, Stewart RJ. 2007 Multiscale structure of the underwater adhesive of Phragmatopoma californica: a nanostructured latex with a steep microporosity gradient. Langmuir 20, 5045–5049. (doi:10.1021/la063765e)
    • (2007) Langmuir , vol.20 , pp. 5045-5049
    • Stevens, M.J.1    Steren, R.E.2    Vlamidir, H.3    Stewart, R.J.4
  • 55
    • 84877738939 scopus 로고    scopus 로고
    • Multipart copolyelectrolyte adhesive of the sandcastle worm, Phragmatopoma californica (Fewkes): Catechol oxidase catalyzed curing through peptidyl-DOPA
    • Wang CS, Stewart RJ. 2013 Multipart copolyelectrolyte adhesive of the sandcastle worm, Phragmatopoma californica (Fewkes): catechol oxidase catalyzed curing through peptidyl-DOPA. Biomacromolecules 14, 1607–1617. (doi:10.1021/bm400251k)
    • (2013) Biomacromolecules , vol.14 , pp. 1607-1617
    • Wang, C.S.1    Stewart, R.J.2
  • 56
    • 84863015690 scopus 로고    scopus 로고
    • Localization of the bioadhesive precursors of the sandcastle worm, Phragmatopoma
    • Wang CS, Stewart RJ. 2012 Localization of the bioadhesive precursors of the sandcastle worm, Phragmatopoma. J. Exp. Biol. 215, 351–361. (doi:10.1242/jeb.065011)
    • (2012) J. Exp. Biol , vol.215 , pp. 351-361
    • Wang, C.S.1    Stewart, R.J.2
  • 57
    • 0026650709 scopus 로고
    • Cement precursor proteins of the reef-building polychaete Phragmatopoma californica (Fewkes)
    • Waite JH, Jensen RA, Morse DE. 1992 Cement precursor proteins of the reef-building polychaete Phragmatopoma californica (Fewkes). Biochemistry 31, 5733–5738. (doi:10.1021/bi00140a007)
    • (1992) Biochemistry , vol.31 , pp. 5733-5738
    • Waite, J.H.1    Jensen, R.A.2    Morse, D.E.3
  • 60
    • 0017161826 scopus 로고
    • The structure and formation of the byssus attachment plaque in Mytilus
    • Tamarin A, Lewis P, Askey J. 1976 The structure and formation of the byssus attachment plaque in Mytilus. J. Morph. 149, 199–222. (doi:10.1002/jmor.1051490205)
    • (1976) J. Morph , vol.149 , pp. 199-222
    • Tamarin, A.1    Lewis, P.2    Askey, J.3
  • 61
    • 0022772912 scopus 로고
    • Composition and ultrastructureof the byssus of Mytilus edulis
    • Benedict CV, Waite JH. 1986 Composition and ultrastructure of the byssus of Mytilus edulis. J. Morphol. 189, 261–270. (doi:10.1002/jmor.1051890305)
    • (1986) J. Morphol , vol.189 , pp. 261-270
    • Benedict, C.V.1    Waite, J.H.2
  • 62
    • 0038067927 scopus 로고    scopus 로고
    • Adhesion à la moule
    • Waite JH. 2002 Adhesion à la moule. Integr. Comp. Biol. 42, 1172–1180. (doi:10.1093/icb/42.6.1172)
    • (2002) Integr. Comp. Biol , vol.42 , pp. 1172-1180
    • Waite, J.H.1
  • 63
    • 21044451304 scopus 로고    scopus 로고
    • Mussel adhesion: Finding the tricks worth mimicking
    • Waite JH, Andersen NH, Jewhurst S, Sun C. 2005 Mussel adhesion: finding the tricks worth mimicking. J. Adhesion 81, 297–317. (doi:10.1080/00218460590944602)
    • (2005) J. Adhesion , vol.81 , pp. 297-317
    • Waite, J.H.1    Ersen, N.H.2    Jewhurst, S.3    Sun, C.4
  • 64
    • 84858280813 scopus 로고    scopus 로고
    • Zebra mussel adhesion: Structure of the byssal adhesive apparatus in the freshwater mussel, Dreissena polymorpha
    • Farsad N, Sone ED. 2012 Zebra mussel adhesion: structure of the byssal adhesive apparatus in the freshwater mussel, Dreissena polymorpha. J. Struct. Biol. 177, 613–620. (doi:10.1016/j.jsb.2012.01.011)
    • (2012) J. Struct. Biol , vol.177 , pp. 613-620
    • Farsad, N.1    Sone, E.D.2
  • 65
    • 0027679768 scopus 로고
    • The byssus of the zebra mussel, Dreissena polymorpha. II. Structure and polymorphism of byssal polyphenolic protein families
    • Rzepecki LM, Waite JH. 1993 The byssus of the zebra mussel, Dreissena polymorpha. II. Structure and polymorphism of byssal polyphenolic protein families. Mol. Mar. Biol. Biotechnol. 2, 267–279.
    • (1993) Mol. Mar. Biol. Biotechnol , vol.2 , pp. 267-279
    • Rzepecki, L.M.1    Waite, J.H.2
  • 66
    • 84894289965 scopus 로고    scopus 로고
    • Novel proteins identified in the insoluble byssal matrix of the freshwater zebra mussel
    • Gantayet A, Ohana L, Sone ED. 2014 Novel proteins identified in the insoluble byssal matrix of the freshwater zebra mussel. Mar. Biotechnol. 16, 144–155. (doi:10.1007/s10126-013-9537-9)
    • (2014) Mar. Biotechnol , vol.16 , pp. 144-155
    • Gantayet, A.1    Ohana, L.2    Sone, E.D.3
  • 67
    • 79953329204 scopus 로고    scopus 로고
    • From ‘trash fish’ to supermodel: The rise and rise of the three-spined stickleback in evolution and ecology
    • Barber I, Nettleship S. 2010 From 'trash fish' to supermodel: the rise and rise of the three-spined stickleback in evolution and ecology. Biologist 57, 15–21.
    • (2010) Biologist , vol.57 , pp. 15-21
    • Barber, I.1    Nettleship, S.2
  • 68
    • 0002556272 scopus 로고    scopus 로고
    • An 11-ketotestosterone induced kidney-secreted protein: The nest building glue from male three-spined stickleback, Gasterosteus aculeatus
    • Jakobsson S, Borg B, Haux C, Hyllner SJ. 1999 An 11-ketotestosterone induced kidney-secreted protein: the nest building glue from male three-spined stickleback, Gasterosteus aculeatus. Fish Physiol. Biochem. 20, 79–85. (doi:10.1023/A:1007776016610)
    • (1999) Fish Physiol. Biochem , vol.20 , pp. 79-85
    • Jakobsson, S.1    Borg, B.2    Haux, C.3    Hyllner, S.J.4
  • 69
    • 33646268410 scopus 로고    scopus 로고
    • Multiple occurrences of spiggin genes in sticklebacks
    • Kawahara R, Nishida M. 2006 Multiple occurrences of spiggin genes in sticklebacks. Gene 373, 58–66. (doi:10.1016/j.gene.2006.01.008)
    • (2006) Gene , vol.373 , pp. 58-66
    • Kawahara, R.1    Nishida, M.2
  • 70
    • 84898959601 scopus 로고    scopus 로고
    • Flow-mediated plasticity in the expression of stickleback nesting glue genes
    • Seear PJ, Head ML, Tilley CA, Rosato E, Barber I. 2014 Flow-mediated plasticity in the expression of stickleback nesting glue genes. Ecol. Evol. 4, 1233–1242. (doi:10.1002/ece3.1016)
    • (2014) Ecol. Evol , vol.4 , pp. 1233-1242
    • Seear, P.J.1    Head, M.L.2    Tilley, C.A.3    Rosato, E.4    Barber, I.5
  • 71
    • 0000325458 scopus 로고
    • Marine organisms and their adhesion
    • (ed. WC Wake, Chichester, UK: John Wiley & Sons
    • Walker G. 1987 Marine organisms and their adhesion. In Synthetic adhesives and sealants (ed. WC Wake), pp. 112–135. Chichester, UK: John Wiley & Sons.
    • (1987) Synthetic Adhesives and Sealants , pp. 112-135
    • Walker, G.1
  • 72
    • 33751167773 scopus 로고    scopus 로고
    • The biochemistry and mechanics of gastropod adhesive gels
    • (eds AM Smith, JA Callow), Berlin, Germany: Springer
    • Smith AM. 2006 The biochemistry and mechanics of gastropod adhesive gels. In Biological adhesives (eds AM Smith, JA Callow), pp. 167–182. Berlin, Germany: Springer.
    • (2006) Biological Adhesives , pp. 167-182
    • Smith, A.M.1
  • 73
    • 0040926591 scopus 로고
    • Feeding behavior and prey choice in Macroperipatus torquatus (Onychophora)
    • Read VMJ, Hughes RN. 1987 Feeding behavior and prey choice in Macroperipatus torquatus (Onychophora). Proc. R. Soc. Lond. B 230, 483–506. (doi:10.1098/rspb.1987.0030)
    • (1987) Proc. R. Soc. Lond. B , vol.230 , pp. 483-506
    • Read, V.1    Hughes, R.N.2
  • 74
    • 84866161071 scopus 로고    scopus 로고
    • Comparative anatomy of slime glands in onychophora (velvet worms)
    • Baer A, Mayer G. 2012 Comparative anatomy of slime glands in onychophora (velvet worms). J. Morphol. 273, 1079–1088. (doi:10.1002/jmor.20044)
    • (2012) J. Morphol , vol.273 , pp. 1079-1088
    • Baer, A.1    Mayer, G.2
  • 75
    • 0032702118 scopus 로고    scopus 로고
    • Characterisation of the slime gland secretion from the peripatus, Euperipatoides kanangrensis (Onychophora: Peripatopsidae)
    • Benkendorff K, Beardmore K, Gooley AA, Packer NH, Tait NN. 1999 Characterisation of the slime gland secretion from the peripatus, Euperipatoides kanangrensis (Onychophora: Peripatopsidae). Comp. Biochem. Physiol. B 124, 457–465. (doi:10.1016/S0305-0491(99)00145-5)
    • (1999) Comp. Biochem. Physiol. B , vol.124 , pp. 457-465
    • Benkendorff, K.1    Beardmore, K.2    Gooley, A.A.3    Packer, N.H.4    Tait, N.N.5
  • 76
    • 78650717443 scopus 로고    scopus 로고
    • A new giant species of placented worm and the mechanism by which onychophorans weave their nets (Onychophora: Peripatidae)
    • Morera-Brenes B, Monge-Najera J. 2010 A new giant species of placented worm and the mechanism by which onychophorans weave their nets (Onychophora: Peripatidae). Rev. Biol. Trop. 58, 1127–1142. (doi:10.15517/rbt.V58i4.5398)
    • (2010) Rev. Biol. Trop , vol.58 , pp. 1127-1142
    • Morera-Brenes, B.1    Monge-Najera, J.2
  • 78
    • 84860109547 scopus 로고    scopus 로고
    • Changes in the adhesive properties of spider aggregate glue during the evolution of cobwebs
    • Sahni V, Blackledge AT, Dhinojwala A. 2011 Changes in the adhesive properties of spider aggregate glue during the evolution of cobwebs. Sci. Rep. 1, 41. (doi:10.1038/srep00041).
    • (2011) Sci. Rep , vol.1 , pp. 41
    • Sahni, V.1    Blackledge, A.T.2    Dhinojwala, A.3
  • 79
    • 84898623950 scopus 로고    scopus 로고
    • Direct solvation of glycoproteins by salts in spider silk glues enhances adhesion and helps to explain the evolution of modern spider orb webs
    • Sahni V, Miyoshi T, Chen K, Jain D, Blamires SJ, Blackledge TA, Dhinojwala A. 2014 Direct solvation of glycoproteins by salts in spider silk glues enhances adhesion and helps to explain the evolution of modern spider orb webs. Biomacromolecules 15, 1225–1232. (doi:10.1021/bm401800y)
    • (2014) Biomacromolecules , vol.15 , pp. 1225-1232
    • Sahni, V.1    Miyoshi, T.2    Chen, K.3    Jain, D.4    Blamires, S.J.5    Blackledge, T.A.6    Dhinojwala, A.7
  • 80
    • 77953124242 scopus 로고    scopus 로고
    • The expression of genes coding for distinct types of glycine-rich proteins varies according to the biology of three metastriate ticks, Rhipicephalus (Boophilus) microplus, Rhipicephalus sanguineus and Amblyomma cajennense
    • Maruyama SR et al. 2010 The expression of genes coding for distinct types of glycine-rich proteins varies according to the biology of three metastriate ticks, Rhipicephalus (Boophilus) microplus, Rhipicephalus sanguineus and Amblyomma cajennense. BMC Genomics 11, 363. (doi:10.1186/1471-2164-11-363)
    • (2010) BMC Genomics , vol.11 , pp. 363
    • Maruyama, S.R.1
  • 81
    • 33846185926 scopus 로고    scopus 로고
    • Characterization of Haemaphysalis longicornis recombinant cement-like antigens and preliminary study of their vaccination effects
    • Harnnoi T, Watchabunsook S, Sakaguchi T, Xuan X, Fujisaki K. 2006 Characterization of Haemaphysalis longicornis recombinant cement-like antigens and preliminary study of their vaccination effects. J. Vet. Med. Sci. 68, 1289–1295. (doi:10.1292/jvms.68.1289)
    • (2006) J. Vet. Med. Sci , vol.68 , pp. 1289-1295
    • Harnnoi, T.1    Watchabunsook, S.2    Sakaguchi, T.3    Xuan, X.4    Fujisaki, K.5
  • 82
    • 77954783755 scopus 로고    scopus 로고
    • An insight into the sialotranscriptome of the brown dog tick, Rhipicephalus sanguineus
    • Anatriello I et al. 2010 An insight into the sialotranscriptome of the brown dog tick, Rhipicephalus sanguineus. BMC Genomics 11, 450. (doi:10.1186/1471-2164-11-450)
    • (2010) BMC Genomics , vol.11 , pp. 450
    • Anatriello, I.1
  • 84
    • 80052427057 scopus 로고    scopus 로고
    • Complex coacervates as a foundation for synthetic underwater adhesives
    • Stewart RJ, Wang CS, Shao H. 2011 Complex coacervates as a foundation for synthetic underwater adhesives. Adv. Colloid Interface Sci. 167, 85–93. (doi:10.1016/j.cis.2010.10.009)
    • (2011) Adv. Colloid Interface Sci , vol.167 , pp. 85-93
    • Stewart, R.J.1    Wang, C.S.2    Shao, H.3
  • 85
    • 84872114658 scopus 로고    scopus 로고
    • Hydrophobic enhancement of Dopa-mediated adhesion in a mussel foot protein
    • Wei JY, Broomell C, Israelachvili JN, Waite JH. 2013 Hydrophobic enhancement of Dopa-mediated adhesion in a mussel foot protein. J. Am. Chem. Soc. 135, 377–383. (doi:10.1021/ja309590f)
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 377-383
    • Wei, J.Y.1    Broomell, C.2    Israelachvili, J.N.3    Waite, J.H.4
  • 87
    • 33751571086 scopus 로고    scopus 로고
    • Chemical subtleties of mussel and polychaete holdfasts
    • (eds AM Smith, JA Callow), Berlin, Germany: Springer
    • Sagert J, Sun C, Waite H. 2006 Chemical subtleties of mussel and polychaete holdfasts. In Biological adhesives (eds AM Smith, JA Callow), pp. 125–143. Berlin, Germany: Springer.
    • (2006) Biological Adhesives , pp. 125-143
    • Sagert, J.1    Sun, C.2    Waite, H.3
  • 88
    • 0034641671 scopus 로고    scopus 로고
    • Cross-linking in adhesive quinoproteins: Studies with model decapeptides
    • Burzio LA, Waite JH. 2000 Cross-linking in adhesive quinoproteins: studies with model decapeptides. Biochemistry 39, 11147–11153. (doi:10.1021/bi0002434)
    • (2000) Biochemistry , vol.39 , pp. 11147-11153
    • Burzio, L.A.1    Waite, J.H.2
  • 89
    • 84971151388 scopus 로고
    • Catechol oxidase in the byssus of the common mussel, Mytilus edulis L
    • Waite JH. 1985 Catechol oxidase in the byssus of the common mussel, Mytilus edulis L. J. Mar. Biol. Assoc. UK 65, 359–371. (doi:10.1017/S0025315400050487)
    • (1985) J. Mar. Biol. Assoc. UK , vol.65 , pp. 359-371
    • Waite, J.H.1
  • 91
    • 0029166187 scopus 로고
    • Hydroxyarginine containing polyphenolic proteins in the adhesive plaques of the marine mussel Mytilus edulis
    • Papov VV, Diamond TV, Biemann K, Waite JH. 1995 Hydroxyarginine containing polyphenolic proteins in the adhesive plaques of the marine mussel Mytilus edulis. J. Biol. Chem. 270, 20183–20192. (doi:10.1074/jbc.270.34.20183)
    • (1995) J. Biol. Chem , vol.270 , pp. 20183-20192
    • Papov, V.V.1    Diamond, T.V.2    Biemann, K.3    Waite, J.H.4
  • 92
    • 0025879424 scopus 로고
    • Complementary DNA sequencing: Expressed sequence tags and human genome project
    • Adams MD et al. 1991 Complementary DNA sequencing: expressed sequence tags and human genome project. Science 252, 1651–1656. (doi:10.1126/science.2047873)
    • (1991) Science , vol.252 , pp. 1651-1656
    • Adams, M.D.1
  • 93
    • 84858608318 scopus 로고    scopus 로고
    • Designing a transcriptomenext-generation sequencing project for a nonmodel plant species
    • Strickler SR, Bombarely A, Mueller LA. 2012 Designing a transcriptome next-generation sequencing project for a nonmodel plant species. Am. J. Bot. 99, 257–266. (doi:10.3732/ajb.1200020)
    • (2012) Am. J. Bot , vol.99 , pp. 257-266
    • Strickler, S.R.1    Bombarely, A.2    Mueller, L.A.3
  • 94
    • 84893242996 scopus 로고    scopus 로고
    • RNA-seq differential expression studies: More sequence, or more replication?
    • Liu Y, Zhou J, White KP. 2013 RNA-seq differential expression studies: more sequence, or more replication? Bioinformatics 14, 797. (doi:10.1093/bioinformatics/btt688)
    • (2013) Bioinformatics , vol.14 , pp. 797
    • Liu, Y.1    Zhou, J.2    White, K.P.3
  • 95
    • 69349088501 scopus 로고    scopus 로고
    • Functional role of 64P, the candidate transmission-blocking caccine antigen from the tick, Rhipicephalus appendiculatus
    • Havlikova S, Roller L, Koci J, Trimnell AR, Kazimirova M, Klempa B, Nuttall PA. 2009 Functional role of 64P, the candidate transmission-blocking caccine antigen from the tick, Rhipicephalus appendiculatus. Int. J. Parasitoi 39, 1485–1494. (doi:10.1016/j.ijpara.2009.05.005)
    • (2009) Int. J. Parasitoi , vol.39 , pp. 1485-1494
    • Havlikova, S.1    Roller, L.2    Koci, J.3    Trimnell, A.R.4    Kazimirova, M.5    Klempa, B.6    Nuttall, P.A.7
  • 96
    • 78650539308 scopus 로고    scopus 로고
    • From RNA-seq reads to differential expression results
    • Oshlack A, Robinson MD, Young MD. 2010 From RNA-seq reads to differential expression results. Genome Biol. 11, 220. (doi:10.1186/gb-2010-11-12-220)
    • (2010) Genome Biol , vol.11 , pp. 220
    • Oshlack, A.1    Robinson, M.D.2    Young, M.D.3
  • 97
    • 84874677498 scopus 로고    scopus 로고
    • A comparison of methods for differential expression analysis of RNA-seq data
    • Soneson C, Delorenzi M. 2013 A comparison of methods for differential expression analysis of RNA-seq data. BMC Bioinf. 14, 91. (doi:10.1186/1471-2105-14-91)
    • (2013) BMC Bioinf , vol.14 , pp. 91
    • Soneson, C.1    Delorenzi, M.2
  • 98
  • 101
    • 84899119779 scopus 로고    scopus 로고
    • Biological adhesion of the flatworm Macrostomum lignano relies on a duo-gland system and is mediated by a cell type-specific intermediate filament protein
    • Lengerer B et al. 2014 Biological adhesion of the flatworm Macrostomum lignano relies on a duo-gland system and is mediated by a cell type-specific intermediate filament protein. Front. Zool. 11, 12. (doi:10.1186/1742-9994-11-12)
    • (2014) Front. Zool , vol.11 , pp. 12
    • Lengerer, B.1
  • 102
    • 84892986118 scopus 로고    scopus 로고
    • First study on gene expression of cement proteins and potential adhesion-related genes of a membranous-based barnacle as revealed from next-generation sequencing technology
    • Lin HC, Wong YH, Tsang LM, Chu KH, Qian PY, Chan BK. 2014 First study on gene expression of cement proteins and potential adhesion-related genes of a membranous-based barnacle as revealed from next-generation sequencing technology. Biofouling 30, 169–181. (doi:10.1080/08927014.2013.853051)
    • (2014) Biofouling , vol.30 , pp. 169-181
    • Lin, H.C.1    Wong, Y.H.2    Tsang, L.M.3    Chu, K.H.4    Qian, K.5    Chan, B.K.6
  • 103
    • 84864434718 scopus 로고    scopus 로고
    • ExPASy: SIB bioinformatics resource portal
    • Artimo P et al. 2012 ExPASy: SIB bioinformatics resource portal. Nucleic Acids Res. 40, W597–W603. (doi:10.1093/bioinformatics/bts133)
    • (2012) Nucleic Acids Res , vol.40 , pp. W597-W603
    • Artimo, P.1
  • 104
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Nordahl Petersen T, Brunak S, von Heijne G, Nielsen H. 2011 SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8, 785–786. (doi:10.1038/nmeth.1701)
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Nordahl Petersen, T.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 106
    • 0034333196 scopus 로고    scopus 로고
    • Rapid automatic detection and alignment of repeats in protein sequences
    • Heger A, Holm L. 2000 Rapid automatic detection and alignment of repeats in protein sequences. Proteins 41, 224–237. (doi:10.1002/1097-0134 (20001101)41:23.0.CO;2-Z)
    • (2000) Proteins , vol.41 , pp. 224-237
    • Heger, A.1    Holm, L.2
  • 107
    • 78651285748 scopus 로고    scopus 로고
    • CDD: A conserved domain database for the functional annotation of proteins
    • Marchler-Bauer A et al. 2011 CDD: a conserved domain database for the functional annotation of proteins. Nucleic Acids Res. 39, D225–D229. (doi:10.1093/nar/gkq1189)
    • (2011) Nucleic Acids Res , vol.39 , pp. D225-D229
    • Marchler-Bauer, A.1
  • 108
    • 0024840711 scopus 로고
    • The glue protein of ribbed mussels (Geukensia demissa): A natural adhesive with some features of collagen
    • Waite JH, Hansen DC, Little KT. 1989 The glue protein of ribbed mussels (Geukensia demissa): a natural adhesive with some features of collagen. J. Comp. Physiol. B 159, 517–525. (doi:10.1007/BF00694376)
    • (1989) J. Comp. Physiol. B , vol.159 , pp. 517-525
    • Waite, J.H.1    Hansen, D.C.2    Little, K.T.3
  • 109
    • 84872199761 scopus 로고    scopus 로고
    • Mapping sea urchins tube feet proteome—a unique hydraulic mechano-sensory adhesive organ
    • Santos R, Barreto A, Franco C, Coelho AV. 2013 Mapping sea urchins tube feet proteome—a unique hydraulic mechano-sensory adhesive organ. J. Proteomics 79, 100–113. (doi:10.1016/j.jprot.2012.12.004)
    • (2013) J. Proteomics , vol.79 , pp. 100-113
    • Santos, R.1    Barreto, A.2    Franco, C.3    Coelho, A.V.4
  • 110
    • 84908022649 scopus 로고    scopus 로고
    • Biochemical analyses of the cement float of the goose barnacle Dosima fascicularis—a preliminary study
    • Zheden V, Klepal W, von Byern J, Bogner FR, Thiel K, Kowalik T, Grunwald I. 2014 Biochemical analyses of the cement float of the goose barnacle Dosima fascicularis—a preliminary study. Biofouling 30, 949–963. (doi:10.1080/08927014.2014.954557)
    • (2014) Biofouling , vol.30 , pp. 949-963
    • Zheden, V.1    Klepal, W.2    Von Byern, J.3    Bogner, F.R.4    Thiel, K.5    Kowalik, T.6    Grunwald, I.7
  • 111
    • 0001336813 scopus 로고
    • Characterization of a cystine-rich polyphenolic protein family from the blue mussel Mytilus edulis L
    • Rzepecki LM, Hansen KM, Waite JH. 1992 Characterization of a cystine-rich polyphenolic protein family from the blue mussel Mytilus edulis L. Biol. Bull. 183, 123–137. (doi:10.2307/1542413)
    • (1992) Biol. Bull , vol.183 , pp. 123-137
    • Rzepecki, L.M.1    Hansen, K.M.2    Waite, J.H.3
  • 112
    • 0036080661 scopus 로고    scopus 로고
    • Biochemical characterization of a byssal protein from Dreissena bugensis (Andrusov)
    • Anderson KE, Waite JH. 2002 Biochemical characterization of a byssal protein from Dreissena bugensis (Andrusov). Biofouling 18, 37–45. (doi:10.1080/08927010290017716)
    • (2002) Biofouling , vol.18 , pp. 37-45
    • Anderson, K.E.1    Waite, J.H.2
  • 113
    • 4444335470 scopus 로고    scopus 로고
    • The abc's (and xyz's) of peptide sequencing
    • Steen H, Mann M. 2004 The abc's (and xyz's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 5, 699–711. (doi:10.1038/nrm1468)
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 114
    • 33749189517 scopus 로고    scopus 로고
    • Top-down versus bottom-up approaches in proteomics
    • Wehr T. 2006 Top-down versus bottom-up approaches in proteomics. LC-GC North Am. 24, 1004.
    • (2006) LC-GC North Am , vol.24 , pp. 1004
    • Wehr, T.1
  • 115
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. 2006 Mass spectrometry and protein analysis. Science 312, 212–217. (doi:10.1126/science.1124619)
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 116
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walter TC, Mann M. 2010 Mass spectrometry-based proteomics in cell biology. J. Cell Biol. 190, 491–500. (doi:10.1083/jcb.201004052)
    • (2010) J. Cell Biol , vol.190 , pp. 491-500
    • Walter, T.C.1    Mann, M.2
  • 117
    • 77951603487 scopus 로고    scopus 로고
    • Highlights on the capacities of ‘gel-based’ proteomics
    • Chevalier F. 2010 Highlights on the capacities of 'gel-based' proteomics. Proteome Sci. 8, 23. (doi:10.1186/1477-5956-8-23)
    • (2010) Proteome Sci , vol.8 , pp. 23
    • Chevalier, F.1
  • 118
    • 84891804649 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology Information
    • NCBI Resource Coordinators. 2014 Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 42, D7–D17. (doi:10.1093/nar/gkt1146)
    • (2014) Nucleic Acids Res , vol.42 , pp. DD7-D17
    • Resource Coordinators, N.1
  • 119
    • 84890231620 scopus 로고    scopus 로고
    • Quantitative and qualitative proteome characteristics extracted from in-depth integrated genomics and proteomics analysis
    • Low TY et al. 2013 Quantitative and qualitative proteome characteristics extracted from in-depth integrated genomics and proteomics analysis. Cell Rep. 5, 1469–1478. (doi:10.1016/j.celrep.2013.10.041)
    • (2013) Cell Rep , vol.5 , pp. 1469-1478
    • Low, T.Y.1
  • 120
    • 69349096579 scopus 로고    scopus 로고
    • Polyphosphoprotein-containing marine adhesives
    • Flammang P, Lambert A, Bailly P, Hennebert E. 2009 Polyphosphoprotein-containing marine adhesives. J. Adhesion 85, 447–464. (doi:10.1080/00218460902996358)
    • (2009) J. Adhesion , vol.85 , pp. 447-464
    • Flammang, P.1    Lambert, A.2    Bailly, P.3    Hennebert, E.4
  • 121
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG. 2002 Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12, 43R–56R. (doi:10.1093/glycob/12.4.43R)
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 122
    • 84884187149 scopus 로고    scopus 로고
    • Identification and quantification of protein glycosylation
    • Roth Z, Yehezkel G, Khalaila I. 2012 Identification and quantification of protein glycosylation. Int. J. Carbohydr. Chem. 2012, 640923. (doi:10.1155/2012/640923)
    • (2012) Int. J. Carbohydr. Chem , vol.2012
    • Roth, Z.1    Yehezkel, G.2    Khalaila, I.3
  • 123
    • 3142780053 scopus 로고    scopus 로고
    • A glycosylated byssal precursor protein from the green mussel Perna viridis with modified dopa side-chains
    • Ohkawa K, Nishida A, Yamamoto H, Waite JH. 2004 A glycosylated byssal precursor protein from the green mussel Perna viridis with modified dopa side-chains. Biofouling 20, 101–115. (doi:10.1080/08927010410001681246)
    • (2004) Biofouling , vol.20 , pp. 101-115
    • Ohkawa, K.1    Nishida, A.2    Yamamoto, H.3    Waite, J.H.4
  • 124
    • 79957985249 scopus 로고    scopus 로고
    • Characterisation of the carbohydrate fraction of the temporary adhesive secreted by the tube feet of the sea star
    • Hennebert E, Wattiez R, Flammang P. 2011 Characterisation of the carbohydrate fraction of the temporary adhesive secreted by the tube feet of the sea star Asterias rubens. Mar. Biotechnol. 13, 484–495. (doi:10.1007/s10126-010-9319-6)
    • (2011) Asterias Rubens. Mar. Biotechnol , vol.13 , pp. 484-495
    • Hennebert, E.1    Wattiez, R.2    Flammang, P.3
  • 125
    • 84858674835 scopus 로고    scopus 로고
    • Structural characterisation of the N-glycan moiety of the barnacle settlement-inducing protein complex (SIPC)
    • Pagett HE et al. 2012 Structural characterisation of the N-glycan moiety of the barnacle settlement-inducing protein complex (SIPC). J. Exp. Biol. 215, 1192–1198. (doi:10.1242/jeb.063503)
    • (2012) J. Exp. Biol , vol.215 , pp. 1192-1198
    • Pagett, H.E.1
  • 126
    • 22244440847 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression
    • Kaelin WG. 2005 Proline hydroxylation and gene expression. Annu. Rev. Biochem. 74, 115–128. (doi:10.1146/annurev.biochem.74.082803.133142)
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 115-128
    • Kaelin, W.G.1
  • 127
    • 0020346292 scopus 로고
    • Conformational implications of enzymatic proline hydroxylation in collagen
    • Chopra RK, Ananthanarayanan VS. 1982 Conformational implications of enzymatic proline hydroxylation in collagen. Proc. Natl Acad. Sci. USA 79, 7180–7184. (doi:10.1073/pnas.79.23.7180)
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 7180-7184
    • Chopra, R.K.1    Ananthanarayanan, V.S.2
  • 129
    • 0028171667 scopus 로고    scopus 로고
    • 1994 trans-2,3-cis-3,4-Dihydroxyproline, a new naturally occurring amino acid, is the sixth residue in the tandemly repeated consensus decapeptides of an adhesive protein from Mytilus edulis
    • Taylor SW, Waite JH. 1994 trans-2,3-cis-3,4-Dihydroxyproline, a new naturally occurring amino acid, is the sixth residue in the tandemly repeated consensus decapeptides of an adhesive protein from Mytilus edulis. J. Am. Chem. Soc. 116, 10803–10804. (doi:10.1021/ja00102a063)
    • J. Am. Chem. Soc , vol.116 , pp. 10803-10804
    • Taylor, S.W.1    Waite, J.H.2
  • 131
    • 0034567281 scopus 로고    scopus 로고
    • Amino acid analysis, using postcolumn ninhydrin detection, in a biotechnology laboratory
    • (eds C Cooper, N Packer, K Williams), Totwa, NJ: Humana Press Inc
    • Macchi FD, Shen FJ, Keck RG, Harris RJ. 2000 Amino acid analysis, using postcolumn ninhydrin detection, in a biotechnology laboratory. In Methods in molecular biology, vol. 159: amino acid analysis protocols (eds C Cooper, N Packer, K Williams), pp. 9–30. Totwa, NJ: Humana Press Inc.
    • (2000) Methods in Molecular Biology, Vol. 159: Amino Acid Analysis Protocols , pp. 9-30
    • Macchi, F.D.1    Shen, F.J.2    Keck, R.G.3    Harris, R.J.4
  • 132
    • 0019499337 scopus 로고
    • Polyphenolic substance of Mytilus edulis: Novel adhesive containing L-dopa and hydroxyproline
    • Waite JH, Tanzer M. 1981 Polyphenolic substance of Mytilus edulis: novel adhesive containing L-dopa and hydroxyproline. Science 212, 1038–1040. (doi:10.1126/science.212.4498.1038)
    • (1981) Science , vol.212 , pp. 1038-1040
    • Waite, J.H.1    Tanzer, M.2
  • 133
    • 0000435509 scopus 로고
    • Colorimetric determination of components of 3,4-dihydroxyphenyl-L-alanine/ tyrosine mixtures
    • Arnow LE. 1937 Colorimetric determination of components of 3,4-dihydroxyphenyl-L-alanine/ tyrosine mixtures. J. Biol. Chem. 118, 531–537.
    • (1937) J. Biol. Chem , vol.118 , pp. 531-537
    • Arnow, L.E.1
  • 135
    • 0021494574 scopus 로고
    • Determination of (catecholato)-borate complex using difference spectrometry
    • Waite JH. 1984 Determination of (catecholato)-borate complex using difference spectrometry. Anal. Chem. 56, 1935–1939. (doi:10.1021/ac00275a040)
    • (1984) Anal. Chem , vol.56 , pp. 1935-1939
    • Waite, J.H.1
  • 136
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders J, Sickmann A. 2005 State-of-the-art in phosphoproteomics. Proteomics 5, 4052–4061. (doi:10.1002/pmic.200401289)
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 137
    • 84904351636 scopus 로고    scopus 로고
    • Phosphoproteomics: Detection, identification and importance of protein phosphorylation
    • (eds HCE Leung, TK Man, RJ Flores). Rijeka, Croatia: In Tech
    • Jia M, Lin KW, Souchelnytskyi S. 2012 Phosphoproteomics: detection, identification and importance of protein phosphorylation. In Integrative proteomics (eds HCE Leung, TK Man, RJ Flores). Rijeka, Croatia: In Tech. (doi:10.5772/31305)
    • (2012) Integrative Proteomics
    • Jia, M.1    Lin, K.W.2    Souchelnytskyi, S.3
  • 138
    • 1542290379 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding mussel adhesive protein from Mytilus sp JHX-2002
    • Wang YJ, Zheng X, Zhang LH, Ohta Y. 2004 Cloning and sequencing of the gene encoding mussel adhesive protein from Mytilus sp JHX-2002. Process Biochem. 39, 659–664. (doi:10.1016/S0032-9592(03)00165-1)
    • (2004) Process Biochem , vol.39 , pp. 659-664
    • Wang, Y.J.1    Zheng, X.2    Zhang, L.H.3    Ohta, Y.4
  • 139
    • 34248581215 scopus 로고    scopus 로고
    • The role of calcium and magnesium in the concrete tubes of the sandcastle worm
    • Sun C, Fantner GE, Adams J, Hansma PK, Waite JH. 2007 The role of calcium and magnesium in the concrete tubes of the sandcastle worm. J. Exp. Biol. 210, 1481–1488. (doi:10.1242/jeb.02759)
    • (2007) J. Exp. Biol , vol.210 , pp. 1481-1488
    • Sun, C.1    Fantner, G.E.2    Adams, J.3    Hansma, P.K.4    Waite, J.H.5
  • 140
    • 34547408364 scopus 로고    scopus 로고
    • Histidinoalanine: A crosslinking amino acid
    • Taylor CM, Wang W. 2007 Histidinoalanine: a crosslinking amino acid. Tetrahedron 63, 9033–9047. (doi:10.1016/j.tet.2007.05.114)
    • (2007) Tetrahedron , vol.63 , pp. 9033-9047
    • Taylor, C.M.1    Wang, W.2
  • 141
    • 84904284898 scopus 로고    scopus 로고
    • Synergistic roles for lipids and proteins in the permanent adhesive of barnacle larvae
    • Gohad NV et al. 2014 Synergistic roles for lipids and proteins in the permanent adhesive of barnacle larvae. Nat. Commun. 5, 4414. (doi:10.1038/ncomms5414)
    • (2014) Nat. Commun , vol.5 , pp. 4414
    • Gohad, N.V.1
  • 142
    • 21044451453 scopus 로고    scopus 로고
    • Introduction: Laboratory animals and immunization procedures: Challenges and opportunities
    • Hendriksen CF. 2005 Introduction: laboratory animals and immunization procedures: challenges and opportunities. ILAR J. NLMID 46, 227–229. (doi:10.1093/ilar.46.3.227)
    • (2005) ILAR J. NLMID , vol.46 , pp. 227-229
    • Hendriksen, C.F.1
  • 143
    • 21044456771 scopus 로고    scopus 로고
    • Critical steps in the production of polyclonal and monoclonal antibodies: Evaluation and recommendations
    • Leenaars M, Hendriksen CF. 2005 Critical steps in the production of polyclonal and monoclonal antibodies: evaluation and recommendations. ILAR J. NLMID 46, 269–279. (doi:10.1093/ilar.46.3.269)
    • (2005) ILAR J. NLMID , vol.46 , pp. 269-279
    • Leenaars, M.1    Hendriksen, C.F.2
  • 144
    • 0033742794 scopus 로고    scopus 로고
    • Immunolocalization of Dpfp1, a byssal protein of the zebra mussel Dreissena polymorpha
    • Anderson KE, Waite JH. 2000 Immunolocalization of Dpfp1, a byssal protein of the zebra mussel Dreissena polymorpha. J. Exp. Biol. 203, 3065–3076.
    • (2000) J. Exp. Biol , vol.203 , pp. 3065-3076
    • Anderson, K.E.1    Waite, J.H.2
  • 145
    • 0027452358 scopus 로고
    • Fundamental principles of in situ hybridization
    • Wilcox JN. 1993 Fundamental principles of in situ hybridization. J. Histochem. Cytochem. 41, 1725–1733. (doi:10.1177/41.12)
    • (1993) J. Histochem. Cytochem , vol.41 , pp. 1725-1733
    • Wilcox, J.N.1
  • 146
    • 0029899565 scopus 로고    scopus 로고
    • Cloning, sequencing and sites of expression of genes for the hydroxyarginine-containing adhesive-plaque protein of the mussel Mytilus galloprovincialis
    • Inoue K, Takeuchi Y, Miki D, Odo S, Harayama S, Waite JH. 1996 Cloning, sequencing and sites of expression of genes for the hydroxyarginine-containing adhesive-plaque protein of the mussel Mytilus galloprovincialis. Eur. J. Biochem. 239, 172–176. (doi:10.1111/j.1432-1033.1996.0172u.x)
    • (1996) Eur. J. Biochem , vol.239 , pp. 172-176
    • Inoue, K.1    Takeuchi, Y.2    Miki, D.3    Odo, S.4    Harayama, S.5    Waite, J.H.6
  • 147
    • 0030117334 scopus 로고    scopus 로고
    • Expression sites of two byssal protein genes of Mytilus galloprovincialis
    • Miki D, Takeuchi Y, Inoue K, Odo S. 1996 Expression sites of two byssal protein genes of Mytilus galloprovincialis. Biol. Bull. 190, 213–217. (doi:10.2307/1542541)
    • (1996) Biol. Bull , vol.190 , pp. 213-217
    • Miki, D.1    Takeuchi, Y.2    Inoue, K.3    Odo, S.4
  • 148
    • 77952693245 scopus 로고    scopus 로고
    • Factorial microarray analysis of zebra mussel (Dreissena polymorpha: Dreissenidae, Bivalvia) adhesion
    • Xu W, Faisal M. 2010 Factorial microarray analysis of zebra mussel (Dreissena polymorpha: Dreissenidae, Bivalvia) adhesion. BMC genomics 11, 341. (doi:10.1186/1471-2164-11-341)
    • (2010) BMC Genomics , vol.11 , pp. 341
    • Xu, W.1    Faisal, M.2
  • 149
    • 77949892175 scopus 로고    scopus 로고
    • Gene expression profiling during the byssogenesis of zebra mussel (Dreissena polymorpha)
    • Xu W, Faisal M. 2010 Gene expression profiling during the byssogenesis of zebra mussel (Dreissena polymorpha). Mol. Genet. Genomics 283, 327–339. (doi:10.1007/s00438-010-0517-8)
    • (2010) Mol. Genet. Genomics , vol.283 , pp. 327-339
    • Xu, W.1    Faisal, M.2
  • 151
    • 84877766936 scopus 로고    scopus 로고
    • Molecular mechanisms of RNA interference
    • (10.1146/annurev-biophys-083012-130404)
    • Wilson RC, Doudna JA. 2013 Molecular mechanisms of RNA interference. Ann. Rev. Biophys. 42, 217–239. (10.1146/annurev-biophys-083012-130404)
    • (2013) Ann. Rev. Biophys , vol.42 , pp. 217-239
    • Wilson, R.C.1    Doudna, J.A.2
  • 152
    • 20144366711 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein type 3A in
    • Hwang DS, Gim Y, Cha HJ. 2005 Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli. Biotechnol. Prog. 21, 965–970. (doi:10.1021/bp050014e)
    • (2005) Escherichia Coli. Biotechnol. Prog , vol.21 , pp. 965-970
    • Hwang, D.S.1    Gim, Y.2    Cha, H.J.3
  • 153
    • 60549084746 scopus 로고    scopus 로고
    • Bulk adhesive strength of recombinant hybrid mussel adhesive protein
    • Cha HJ, Hwang DS, Lim S, White JD, Matos-Perez CR, Wilker JJ. 2009 Bulk adhesive strength of recombinant hybrid mussel adhesive protein. Biofouling 25, 99–107. (doi:10.1080/ 08927010802563108)
    • (2009) Biofouling , vol.25 , pp. 99-107
    • Cha, H.J.1    Hwang, D.S.2    Lim, S.3    White, J.D.4    Matos-Perez, C.R.5    Wilker, J.J.6
  • 154
    • 24044457367 scopus 로고    scopus 로고
    • Use of surface-sensitive methods for the study of adsorption and cross-linking of marine bioadhesives
    • Berglin M, Hedlund J, Fant C, Elwing H. 2005 Use of surface-sensitive methods for the study of adsorption and cross-linking of marine bioadhesives. J. Adhesion 81, 805–822. (doi:10.1080/00218460500189059)
    • (2005) J. Adhesion , vol.81 , pp. 805-822
    • Berglin, M.1    Hedlund, J.2    Fant, C.3    Elwing, H.4
  • 155
    • 84881546449 scopus 로고    scopus 로고
    • Molecular surface chemistry in marine bioadhesion
    • Petrone L. 2013 Molecular surface chemistry in marine bioadhesion. Adv. Colloid Interface Sci. 195–196, 1–18. (doi:10.1016/j.cis.2013.03.006)
    • (2013) Adv. Colloid Interface Sci , vol.195-196 , pp. 1-18
    • Petrone, L.1
  • 157
    • 0027312161 scopus 로고
    • Cloning, expression, and characterization of a synthetic analog to the bioadhesive precursor protein of the sea mussel Mytilus edulis
    • Salerno AJ, Goldberg I. 1993 Cloning, expression, and characterization of a synthetic analog to the bioadhesive precursor protein of the sea mussel Mytilus edulis. Appl. Microbiol. Biotechnol. 39, 221–226. (doi:10.1007/BF00228610)
    • (1993) Appl. Microbiol. Biotechnol , vol.39 , pp. 221-226
    • Salerno, A.J.1    Goldberg, I.2
  • 158
    • 53449089869 scopus 로고    scopus 로고
    • A novel expression system for recombinant marine mussel adhesive protein Mefp1 using a truncated 0mpA signal peptide
    • Lee SJ, Han YH, Nam BH, Kim Y0, Reeves P. 2008 A novel expression system for recombinant marine mussel adhesive protein Mefp1 using a truncated 0mpA signal peptide. Mol. Cells 26, 34–40.
    • (2008) Mol. Cells , vol.26 , pp. 34-40
    • Lee, S.J.1    Han, Y.H.2    Nam, B.H.3    Y0, K.4    Reeves, P.5
  • 159
    • 44949138865 scopus 로고    scopus 로고
    • Development of bioadhesives from marine mussels
    • Cha HJ, Hwang DS, Lim S. 2008 Development of bioadhesives from marine mussels. Biotechnol. J. 3, 631–638. (doi:10.1002/biot.200700258)
    • (2008) Biotechnol. J , vol.3 , pp. 631-638
    • Cha, H.J.1    Hwang, D.S.2    Lim, S.3
  • 160
    • 78651068270 scopus 로고    scopus 로고
    • Protein-based underwater adhesives and the prospects for their biotechnological production
    • Stewart RJ. 2011 Protein-based underwater adhesives and the prospects for their biotechnological production. Appl. Microbiol. Biotechnol. 89, 27–33. (doi:10.1007/s00253-010-2913-8)
    • (2011) Appl. Microbiol. Biotechnol , vol.89 , pp. 27-33
    • Stewart, R.J.1
  • 161
    • 0025160176 scopus 로고
    • The phylogeny and chemical diversity of quinone-tanned glues and varnishes
    • Waite JH. 1990 The phylogeny and chemical diversity of quinone-tanned glues and varnishes. Comp. Physiol. Biochem. B 97, 19–29. (doi:10.1016/0305-0491(90)90172-P)
    • (1990) Comp. Physiol. Biochem. B , vol.97 , pp. 19-29
    • Waite, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.