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Volumn 17, Issue 2, 1998, Pages 93-106

The peculiar collagens of mussel byssus

Author keywords

Byssus; Collagen; Elastin like; Mussel; Silk like

Indexed keywords

COLLAGEN; COMPLEMENTARY DNA; PROCOLLAGEN; SIGNAL PEPTIDE; TROPOCOLLAGEN;

EID: 0031862042     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90023-3     Document Type: Short Survey
Times cited : (206)

References (69)
  • 1
    • 0003357084 scopus 로고
    • Molecular structure of the fibers of the collagen group
    • Astbury, W.T.: Molecular structure of the fibers of the collagen group. J. Int. Soc. Leather Trades Chem. 24: 69-92, 1940.
    • (1940) J. Int. Soc. Leather Trades Chem. , vol.24 , pp. 69-92
    • Astbury, W.T.1
  • 2
    • 0002438041 scopus 로고
    • The byssus of the mussel Mytilus from the molecules to the organ: Functional performance resides in the ultrastructural assemby
    • ed. by Lanzavecchia, G. and Valvassori, R., Mucchi, Modena
    • Bairati, A.: The byssus of the mussel Mytilus from the molecules to the organ: functional performance resides in the ultrastructural assemby. In: Form and Function in Zoology, ed. by Lanzavecchia, G. and Valvassori, R., Mucchi, Modena, 1991, pp. 163-177.
    • (1991) Form and Function in Zoology , pp. 163-177
    • Bairati, A.1
  • 3
    • 0008740864 scopus 로고
    • The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. Analysis of byssus by polarized light microscopy
    • Bairati, A. and Vitellaro Zuccarello, L.: The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. Analysis of byssus by polarized light microscopy. J. Submicr. Cytol. 6: 367-379, 1974.
    • (1974) J. Submicr. Cytol. , vol.6 , pp. 367-379
    • Bairati, A.1    Vitellaro Zuccarello, L.2
  • 4
    • 0017231408 scopus 로고
    • The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. Observations by transmission electron microscopy
    • Bairati, A. and Vitellaro Zuccarello, L.: The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. Observations by transmission electron microscopy. Cell Tiss. Res. 166: 219-234, 1976.
    • (1976) Cell Tiss. Res. , vol.166 , pp. 219-234
    • Bairati, A.1    Vitellaro Zuccarello, L.2
  • 5
    • 0000508581 scopus 로고    scopus 로고
    • Mechanical design of mussel byssus: Material yield enhances attachment strength
    • Bell, E.G. and Gosline, J.M.: Mechanical design of mussel byssus: Material yield enhances attachment strength. J. Exp. Biol. 199: 1005-1017, 1996.
    • (1996) J. Exp. Biol. , vol.199 , pp. 1005-1017
    • Bell, E.G.1    Gosline, J.M.2
  • 6
    • 0022762455 scopus 로고
    • Location and analysis of byssal structural proteins of Mytilus edulis
    • Benedict, C.V. and Waite, J.H.: Location and analysis of byssal structural proteins of Mytilus edulis. J. Morphol. 189: 171-181, 1986.
    • (1986) J. Morphol. , vol.189 , pp. 171-181
    • Benedict, C.V.1    Waite, J.H.2
  • 7
    • 0029051024 scopus 로고
    • Identification of an elastin cross-linking domain that joins three peptide chains
    • Brown-Augsburger, P., Tisdale, C., Broekelmann, T., Sloan, C. and Mecham, R.P.: Identification of an elastin cross-linking domain that joins three peptide chains. J. Biol. Chem. 270: 17778-17783, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17778-17783
    • Brown-Augsburger, P.1    Tisdale, C.2    Broekelmann, T.3    Sloan, C.4    Mecham, R.P.5
  • 8
    • 0031262876 scopus 로고    scopus 로고
    • Sequence of abductin, the molluscan "rubber" protein
    • Cao, Q., Wang, Y. and Bayley, H.: Sequence of abductin, the molluscan "rubber" protein. Curr. Biol. 7: R677-678, 1997.
    • (1997) Curr. Biol. , vol.7
    • Cao, Q.1    Wang, Y.2    Bayley, H.3
  • 9
    • 13144254590 scopus 로고
    • Étude roentgénographique des kératines sécrétées
    • Champctier, G. and Fauré-Fremiet, E.: Étude roentgénographique des kératines sécrétées. C. R. Acad. Sci., Paris 207: 1133-1134, 1938.
    • (1938) C. R. Acad. Sci., Paris , vol.207 , pp. 1133-1134
    • Champctier, G.1    Fauré-Fremiet, E.2
  • 10
    • 0022519320 scopus 로고
    • A gene encoding a novel glycine-rich structural protein of petunia
    • Condit, C.M. and Meagher, R.B.: A gene encoding a novel glycine-rich structural protein of petunia. Nature 323: 178-181, 1986.
    • (1986) Nature , vol.323 , pp. 178-181
    • Condit, C.M.1    Meagher, R.B.2
  • 11
    • 0019843104 scopus 로고
    • Mytilus byssal threads as an environmental marker for metals
    • Coombs, T.L. and Keller, P.J.: Mytilus byssal threads as an environmental marker for metals. Aquat. Toxicol. 1: 291-300, 1981.
    • (1981) Aquat. Toxicol. , vol.1 , pp. 291-300
    • Coombs, T.L.1    Keller, P.J.2
  • 12
    • 0030865952 scopus 로고    scopus 로고
    • Extensible collagen in mussel byssus: A natural block copolymer
    • Coyne, K.J., Qin, X.X. and Waite, J.H.: Extensible collagen in mussel byssus: A natural block copolymer. Science 277: 1830-1832, 1997.
    • (1997) Science , vol.277 , pp. 1830-1832
    • Coyne, K.J.1    Qin, X.X.2    Waite, J.H.3
  • 13
    • 0014028099 scopus 로고
    • Inter- and intramolecular cross-linking in tyrosinase-treated tropocollagen
    • Dabbous, M.K.: Inter- and intramolecular cross-linking in tyrosinase-treated tropocollagen. J. Biol. Chem. 241: 5307-5312, 1966.
    • (1966) J. Biol. Chem. , vol.241 , pp. 5307-5312
    • Dabbous, M.K.1
  • 14
    • 0027070905 scopus 로고
    • The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface
    • De La Cadena, R.A. and Colman, R.W.: The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface. Protein Sci. 1. 151-160, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 151-160
    • De La Cadena, R.A.1    Colman, R.W.2
  • 15
    • 0001263217 scopus 로고
    • The physical properties of spider's silk and their role in the design of orb webs
    • Denny, M.W. The physical properties of spider's silk and their role in the design of orb webs. J. Exp. Biol. 65: 483-505, 1976.
    • (1976) J. Exp. Biol. , vol.65 , pp. 483-505
    • Denny, M.W.1
  • 17
    • 0027952494 scopus 로고
    • Attachment and orientation of Mytilus edulis L. in flowing water
    • Dolmer, P. and Svane, I.: Attachment and orientation of Mytilus edulis L. in flowing water. Ophelia 40: 63-74, 1994.
    • (1994) Ophelia , vol.40 , pp. 63-74
    • Dolmer, P.1    Svane, I.2
  • 18
    • 0030865343 scopus 로고    scopus 로고
    • Versatile collagens in invertebrates
    • Engel, J.: Versatile collagens in invertebrates. Science 277: 1785-1786, 1997.
    • (1997) Science , vol.277 , pp. 1785-1786
    • Engel, J.1
  • 19
    • 0026636614 scopus 로고
    • Sea urchin collagen evolutionarily homologous to vertebrate pro-α2(I) collagen
    • Exposito, J.Y., D'Alessio, M., Solursh, M. and Ramirez, R.: Sea urchin collagen evolutionarily homologous to vertebrate pro-α2(I) collagen. J. Biol. Chem. 267: 15559-15564, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15559-15564
    • Exposito, J.Y.1    D'Alessio, M.2    Solursh, M.3    Ramirez, R.4
  • 20
    • 0025895543 scopus 로고
    • The stabilization of fibrillar collagen matrices with 3, 4-dihydroxyphenylalanine
    • Gade, J.N., Fellman, J.H. and Bentley, J.P.: The stabilization of fibrillar collagen matrices with 3, 4-dihydroxyphenylalanine. J. Biomed. Mat. Res. 25: 799-811, 1991.
    • (1991) J. Biomed. Mat. Res. , vol.25 , pp. 799-811
    • Gade, J.N.1    Fellman, J.H.2    Bentley, J.P.3
  • 21
    • 0002365096 scopus 로고
    • Light microscopic waveforms in collagenous tissues and their structural implications
    • ed. by Atkins, E.D.T. and Keller, A., Butterworths, London
    • Gathercole, L.J. and Keller, A.: Light microscopic waveforms in collagenous tissues and their structural implications. In: Structure of Fibrous Biopolymers, ed. by Atkins, E.D.T. and Keller, A., Butterworths, London, 1975, pp. 153-175.
    • (1975) Structure of Fibrous Biopolymers , pp. 153-175
    • Gathercole, L.J.1    Keller, A.2
  • 22
    • 33749443646 scopus 로고
    • The structure and properties of spider silk
    • Gosline, J.M., DeMont, M.E. and Denny, M.W.: The structure and properties of spider silk. Endeavour 10: 37-43, 1986.
    • (1986) Endeavour , vol.10 , pp. 37-43
    • Gosline, J.M.1    DeMont, M.E.2    Denny, M.W.3
  • 23
    • 0029925013 scopus 로고    scopus 로고
    • Silk properties determined by gland-specific expression of a spider fibroin gene family
    • Guerette, P.A., Ginzinger, D.G., Weber, B.H.F. and Gosline, J.M.: Silk properties determined by gland-specific expression of a spider fibroin gene family. Science 272: 112-115, 1996.
    • (1996) Science , vol.272 , pp. 112-115
    • Guerette, P.A.1    Ginzinger, D.G.2    Weber, B.H.F.3    Gosline, J.M.4
  • 25
  • 26
    • 0022395838 scopus 로고
    • Structural model of the collagen-like region of C1q comprising the kink region and the fiber-like packing of the six triple helices
    • Kilchherr, E., Hoffmann, H., Steigemann, W. and Engel, J.: Structural model of the collagen-like region of C1q comprising the kink region and the fiber-like packing of the six triple helices. J. Mol. Biol. 186: 403-415, 1985.
    • (1985) J. Mol. Biol. , vol.186 , pp. 403-415
    • Kilchherr, E.1    Hoffmann, H.2    Steigemann, W.3    Engel, J.4
  • 27
    • 0030249201 scopus 로고    scopus 로고
    • In situ analysis of peptidyl-Dopa in mussel byssus using rotationalecho double resonance NMR
    • Klug, C.A., Burzio, L.A., Waite, J.H. and Schaefer, J.: In situ analysis of peptidyl-Dopa in mussel byssus using rotationalecho double resonance NMR. Arch. Biochem. Biophys.333: 221-224, 1996.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 221-224
    • Klug, C.A.1    Burzio, L.A.2    Waite, J.H.3    Schaefer, J.4
  • 28
    • 0025782267 scopus 로고
    • Metal affinity precipitaion of proteins carrying genetically attached polyhistidine tails
    • Lilius, G., Persson, M., Bülow, L. and Mosbach, K.: Metal affinity precipitaion of proteins carrying genetically attached polyhistidine tails. Eur.J. Biochem. 198: 499-504, 1991.
    • (1991) Eur.J. Biochem. , vol.198 , pp. 499-504
    • Lilius, G.1    Persson, M.2    Bülow, L.3    Mosbach, K.4
  • 29
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzys mology
    • Lipscomb, W.N. and Sträter, N.: Recent advances in zinc enzys mology. Chem. Rev. 96: 2375-2433, 1996.
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2433
    • Lipscomb, W.N.1    Sträter, N.2
  • 30
    • 0041044205 scopus 로고
    • Etude de la pose et de l'activité de secrétion du byssus de Mytilus edulis L
    • Maheo, R.: Etude de la pose et de l'activité de secrétion du byssus de Mytilus edulis L. Cab. Biol. Mar. 11: 475-483, 1970.
    • (1970) Cab. Biol. Mar. , vol.11 , pp. 475-483
    • Maheo, R.1
  • 31
    • 9844230641 scopus 로고
    • Occurrence of collagen in the phylum Mollusca
    • Melnick, S.C.: Occurrence of collagen in the phylum Mollusca. Nature 181: 1483-1484, 1958.
    • (1958) Nature , vol.181 , pp. 1483-1484
    • Melnick, S.C.1
  • 32
    • 84970581841 scopus 로고
    • Observations on the molecular structure of byssus fibres
    • Mercer, E.H.: Observations on the molecular structure of byssus fibres. Austral. Mar. Freshwater Res. 3: 199-204, 1952.
    • (1952) Austral. Mar. Freshwater Res. , vol.3 , pp. 199-204
    • Mercer, E.H.1
  • 33
    • 0022423906 scopus 로고
    • The histidine-rich glycoprotein of serum has a domain rich in histidine, proline and glycine that binds heme and metals
    • Morgan, W.T: The histidine-rich glycoprotein of serum has a domain rich in histidine, proline and glycine that binds heme and metals. Biochem. 24: 1496-1501, 1985.
    • (1985) Biochem. , vol.24 , pp. 1496-1501
    • Morgan, W.T.1
  • 34
    • 0029166187 scopus 로고
    • Hydroxyarginine containing polyphenolic proteins in the adhesive plaques of marine mussel
    • Papov, V.V., Diamond, T.V., Biemann, K. and Waite, J.H.: Hydroxyarginine containing polyphenolic proteins in the adhesive plaques of marine mussel Mytilus edulis. J. Biol. Chem. 270: 20183-20192, 1995.
    • (1995) Mytilus Edulis. J. Biol. Chem. , vol.270 , pp. 20183-20192
    • Papov, V.V.1    Diamond, T.V.2    Biemann, K.3    Waite, J.H.4
  • 35
    • 0019992204 scopus 로고
    • Structure and assembly of the native collagen fibril
    • Piez, K.A.: Structure and assembly of the native collagen fibril. Connect. Tiss. Res. 10: 25-36, 1982.
    • (1982) Connect. Tiss. Res. , vol.10 , pp. 25-36
    • Piez, K.A.1
  • 37
    • 0030875449 scopus 로고    scopus 로고
    • Self assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
    • Pins, G.D., Christiansen, D.L., Patel, R. and Silver, F.H.: Self assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophys. J. 73: 2164-2172, 1997.
    • (1997) Biophys. J. , vol.73 , pp. 2164-2172
    • Pins, G.D.1    Christiansen, D.L.2    Patel, R.3    Silver, F.H.4
  • 38
    • 84985427955 scopus 로고
    • Byssus thread strength in the mussel, Mytilus edulis
    • Price, H.A.: Byssus thread strength in the mussel, Mytilus edulis. J. Zool. Lond. 194: 245-255, 1981.
    • (1981) J. Zool. Lond. , vol.194 , pp. 245-255
    • Price, H.A.1
  • 39
    • 0007249243 scopus 로고
    • Le complex byssogene des mollusques bivalves: Histochimie comparée des secrétions chez Mytilus edulis et Pinna nobilis
    • Pujol, P.J.: Le complex byssogene des mollusques bivalves: Histochimie comparée des secrétions chez Mytilus edulis et Pinna nobilis. Bull. Soc. Linn. Normandie 10: 308-332, 1967.
    • (1967) Bull. Soc. Linn. Normandie , vol.10 , pp. 308-332
    • Pujol, P.J.1
  • 40
    • 0031437429 scopus 로고    scopus 로고
    • Tough tendons: Mussel byssus has collagen with silk like domains
    • Qin, X.X., Coyne, K.J. and Waite, J.H.: Tough tendons: Mussel byssus has collagen with silk like domains. J. Biol. Chem. 272: 32623-32627, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32623-32627
    • Qin, X.X.1    Coyne, K.J.2    Waite, J.H.3
  • 41
    • 0029267044 scopus 로고
    • Exotic collagen gradients in the byssus of the mussel Mytilus edulis
    • Qin, X.X. and Waite, J.H.: Exotic collagen gradients in the byssus of the mussel Mytilus edulis. J. Exp. Biol. 198: 633-644, 1995.
    • (1995) J. Exp. Biol. , vol.198 , pp. 633-644
    • Qin, X.X.1    Waite, J.H.2
  • 42
    • 85030337233 scopus 로고    scopus 로고
    • A collagenous precursor that may mediate block copolymer gradients in mussel byssal threads
    • Qin, X.X. and Waite, J.H.: A collagenous precursor that may mediate block copolymer gradients in mussel byssal threads. Proc. Nat. Acad. Sci. USA, in revision.
    • Proc. Nat. Acad. Sci. USA, in Revision
    • Qin, X.X.1    Waite, J.H.2
  • 43
    • 0023664380 scopus 로고
    • Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones
    • Raju, K. and Anwar, A.: Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones. J. Biol. Chem. 262: 5755-5762, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5755-5762
    • Raju, K.1    Anwar, A.2
  • 44
    • 12644291491 scopus 로고
    • Ricerche sul bisso e sulla sua secrezione
    • Ravera, O.: Ricerche sul bisso e sulla sua secrezione. Pubbl. Staz. Zool. Napoli 22: 95-105, 1950.
    • (1950) Pubbl. Staz. Zool. Napoli , vol.22 , pp. 95-105
    • Ravera, O.1
  • 45
    • 0027422979 scopus 로고
    • Extracellular matrix: The elastic fiber
    • Rosenbloom, J., Abrams, W.R. and Mecham, R.: Extracellular matrix: The elastic fiber. FASEB J. 7: 1208-1218, 1993.
    • (1993) FASEB J. , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 46
    • 0002904636 scopus 로고
    • The distribution of collagen and chitin
    • Rudall, K.M. The distribution of collagen and chitin. Symp. Soc. Exp. Biol. 9: 49-71, 1955.
    • (1955) Symp. Soc. Exp. Biol. , vol.9 , pp. 49-71
    • Rudall, K.M.1
  • 48
    • 0031008422 scopus 로고    scopus 로고
    • Gly-Gly-containing triplets of low stability adjacent to a type II collagen epitope
    • Shah, N.K., Sharma, M., Kirkpatrick, A., Ramshaw, J.A.M. and Brodsky, B.: Gly-Gly-containing triplets of low stability adjacent to a type II collagen epitope. Biochem. 36: 5878-5883, 1997.
    • (1997) Biochem. , vol.36 , pp. 5878-5883
    • Shah, N.K.1    Sharma, M.2    Kirkpatrick, A.3    Ramshaw, J.A.M.4    Brodsky, B.5
  • 49
    • 0030970733 scopus 로고    scopus 로고
    • Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagens
    • Sicot, F.X., Exposito, J.Y., Masselot, M., Garrone, R., Deutsch, J. and Gaill, F.: Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagens. Eur. J. Biochem. 246: 50-58, 1997.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 50-58
    • Sicot, F.X.1    Exposito, J.Y.2    Masselot, M.3    Garrone, R.4    Deutsch, J.5    Gaill, F.6
  • 50
    • 0030569727 scopus 로고    scopus 로고
    • Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk
    • Simmons, A.H., Michal, C.A. and Jelinski, L.W: Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk. Science 271: 84-87, 1996.
    • (1996) Science , vol.271 , pp. 84-87
    • Simmons, A.H.1    Michal, C.A.2    Jelinski, L.W.3
  • 51
    • 0001315611 scopus 로고
    • Mechanical properties of mussel byssus threads
    • Smeathers, J.E. , and Vincent, J.F.V.: Mechanical properties of mussel byssus threads. J. Molluscan Stud. 49: 219-230, 1979.
    • (1979) J. Molluscan Stud. , vol.49 , pp. 219-230
    • Smeathers, J.E.1    Vincent, J.F.V.2
  • 52
    • 0001704314 scopus 로고
    • A technique for the histochemical demostration of phenoloxidase and its application to egg-shell formation in helminths and byssus formation in Mytilus
    • Smyth, J.D.: A technique for the histochemical demostration of phenoloxidase and its application to egg-shell formation in helminths and byssus formation in Mytilus. Q. J. Microsc. Sci. 95: 139-152, 1954.
    • (1954) Q. J. Microsc. Sci. , vol.95 , pp. 139-152
    • Smyth, J.D.1
  • 54
    • 0001206814 scopus 로고    scopus 로고
    • Formation of protein-bound 3, 4-dihydroxyphenylalanine and 5-S-cysteinyl-3, 4-dihydroxyphenylalanine as new cross-linkers in gluten
    • Takasaki, S. and Kawakishi, S.: Formation of protein-bound 3, 4-dihydroxyphenylalanine and 5-S-cysteinyl-3, 4-dihydroxyphenylalanine as new cross-linkers in gluten. J. Agric. Food Chem. 45: 3472-3475, 1997.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3472-3475
    • Takasaki, S.1    Kawakishi, S.2
  • 55
    • 0015383685 scopus 로고
    • An ultrastructural study of the byssal thread forming system in Mytilus
    • Tamarin, A. and Keller, P.J.: An ultrastructural study of the byssal thread forming system in Mytilus. J. Ultrastruct. Res. 40: 401-416, 1972.
    • (1972) J. Ultrastruct. Res. , vol.40 , pp. 401-416
    • Tamarin, A.1    Keller, P.J.2
  • 56
    • 0025944530 scopus 로고
    • Polypeptide models of elastin: CD and NMR studies on synthetic poly (X-Gly-Gly)
    • Tamburro, A.M., Guantieri, V., Scopa, A. and Drabble, J.M.: Polypeptide models of elastin: CD and NMR studies on synthetic poly (X-Gly-Gly). Chirality 3: 318-323, 1991.
    • (1991) Chirality , vol.3 , pp. 318-323
    • Tamburro, A.M.1    Guantieri, V.2    Scopa, A.3    Drabble, J.M.4
  • 57
    • 2542545206 scopus 로고    scopus 로고
    • Ferric ion complexes of a DOPA-containing adhesive protein from Mytilus edulis
    • Taylor, S.W., Chase, D.B., Emptage, M.H., Nelson, M.J. and Waite, J.H.: Ferric ion complexes of a DOPA-containing adhesive protein from Mytilus edulis. Inorg. Chem. 35: 7572-7577; 1996.
    • (1996) Inorg. Chem. , vol.35 , pp. 7572-7577
    • Taylor, S.W.1    Chase, D.B.2    Emptage, M.H.3    Nelson, M.J.4    Waite, J.H.5
  • 58
    • 0001516577 scopus 로고
    • Polarographic and spectrophotometric investigation of iron (III) complexation to 3, 4-dihydroxyphenylalanine-containing peptides and proteins from Mytilus edulis
    • Taylor, S.W., Luther, G.W. and Waite, J.H.: Polarographic and spectrophotometric investigation of iron (III) complexation to 3, 4-dihydroxyphenylalanine-containing peptides and proteins from Mytilus edulis. Inorg. Chem. 33: 5819-5824, 1994.
    • (1994) Inorg. Chem. , vol.33 , pp. 5819-5824
    • Taylor, S.W.1    Luther, G.W.2    Waite, J.H.3
  • 59
    • 0031172364 scopus 로고    scopus 로고
    • Non-periodic lattice crystals in the hierarchical microstructure of spider (major ampullate) silk
    • Thiel, B.L., Guess, K.B. and Viney, C.: Non-periodic lattice crystals in the hierarchical microstructure of spider (major ampullate) silk. Biopolymers 41: 703-719, 1997.
    • (1997) Biopolymers , vol.41 , pp. 703-719
    • Thiel, B.L.1    Guess, K.B.2    Viney, C.3
  • 60
    • 0024990763 scopus 로고
    • Collagens as multidomain proteins
    • van der Rest, M. and Garrone, R.: Collagens as multidomain proteins. Biochimie 72: 473-484, 1990.
    • (1990) Biochimie , vol.72 , pp. 473-484
    • Van Der Rest, M.1    Garrone, R.2
  • 61
    • 0024199795 scopus 로고
    • Collagen cross-linking: Distribution of hydroxypyridinium cross-links among invertebrate phyla and tissues
    • van Ness, K.P. , Koob, T.J. and Eyre, D.R.: Collagen cross-linking: distribution of hydroxypyridinium cross-links among invertebrate phyla and tissues. Comp. Biochem. Physiol. 91B: 531-534, 1988.
    • (1988) Comp. Biochem. Physiol. , vol.91 B , pp. 531-534
    • Van Ness, K.P.1    Koob, T.J.2    Eyre, D.R.3
  • 63
    • 84971151388 scopus 로고
    • Catechol oxidase in the byssus of the common mussel Mytilus edulis
    • Waite, J.H.: Catechol oxidase in the byssus of the common mussel Mytilus edulis. J. Mar. Biol. Assoc. U.K. 65: 359-371, 1985.
    • (1985) J. Mar. Biol. Assoc. U.K. , vol.65 , pp. 359-371
    • Waite, J.H.1
  • 64
    • 0025160176 scopus 로고
    • The phylogeny and chemical diversity of quinone tanned glues and varnishes
    • Waite, J.H.: The phylogeny and chemical diversity of quinone tanned glues and varnishes. Comp. Biochem. Physiol. 97B: 19-29, 1990.
    • (1990) Comp. Biochem. Physiol. , vol.97 B , pp. 19-29
    • Waite, J.H.1
  • 65
    • 0027031130 scopus 로고
    • The formation of mussel byssus: Anatomy of a natural manufacturing process
    • Waite, J.H.: The formation of mussel byssus: Anatomy of a natural manufacturing process. Results Problems Cell Differentiation 19: 27-54, 1992.
    • (1992) Results Problems Cell Differentiation , vol.19 , pp. 27-54
    • Waite, J.H.1
  • 67
    • 0001673036 scopus 로고
    • Comparative studies of fibroins. II. The crystal structures of various fibroins
    • Warwicker, J.O.: Comparative studies of fibroins. II. The crystal structures of various fibroins. J. Mol. Biol. 2: 350-362, 1960.
    • (1960) J. Mol. Biol. , vol.2 , pp. 350-362
    • Warwicker, J.O.1
  • 68
    • 9144257407 scopus 로고    scopus 로고
    • Antifreeze proteins: Structures and mechanisms
    • Yeh, Y. and Feeney, R.E.: Antifreeze proteins: Structures and mechanisms. Chem. Rev. 96: 601-617, 1996.
    • (1996) Chem. Rev. , vol.96 , pp. 601-617
    • Yeh, Y.1    Feeney, R.E.2
  • 69
    • 0000572635 scopus 로고
    • On the significance of the byssus in the bivalvia and its effects in evolution
    • Yonge, M.: On the significance of the byssus in the bivalvia and its effects in evolution. J. Mar. Biol. Ass. U.K. 42: 113-125, 1962.
    • (1962) J. Mar. Biol. Ass. U.K. , vol.42 , pp. 113-125
    • Yonge, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.