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Volumn 39, Issue 8, 2014, Pages 1564-1583

Nature as a blueprint for polymer material concepts: Protein fiber-reinforced composites as holdfasts of mussels

Author keywords

Biomimetics; Collagen structure; Gradient materials; Mussel byssus; preCols; PTMP1

Indexed keywords

BIOMIMETICS; FIBER REINFORCED PLASTICS; PROTEINS;

EID: 84905668631     PISSN: 00796700     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.progpolymsci.2014.02.007     Document Type: Review
Times cited : (58)

References (178)
  • 1
    • 80054894161 scopus 로고    scopus 로고
    • The conflicts between strength and toughness
    • R.O. Ritchie The conflicts between strength and toughness Nat Mater 10 2011 817 822
    • (2011) Nat Mater , vol.10 , pp. 817-822
    • Ritchie, R.O.1
  • 3
    • 0035968012 scopus 로고    scopus 로고
    • Graded materials for resistance to contact deformation and damage
    • DOI 10.1126/science.1059716
    • S. Suresh Graded materials for resistance to contact deformation and damage Science 292 2001 2447 2451 (Pubitemid 32601650)
    • (2001) Science , vol.292 , Issue.5526 , pp. 2447-2451
    • Suresh, S.1
  • 5
    • 0036963494 scopus 로고    scopus 로고
    • Rigid biological composite materials: Structural examples for biomimetic design
    • DOI 10.1177/001448502321548229
    • G. Mayer, and M. Sarikaya Rigid biological composite materials: structural examples for biomimetic design Exp Mech 42 2002 395 403 (Pubitemid 36108672)
    • (2002) Experimental Mechanics , vol.42 , Issue.4 , pp. 395-403
    • Mayer, G.1    Sarikaya, M.2
  • 6
    • 35548930317 scopus 로고    scopus 로고
    • Biological materials: Structure and mechanical properties
    • DOI 10.1016/j.pmatsci.2007.05.002, PII S0079642507000254
    • M.A. Meyers, P.Y. Chen, A.Y.M. Lin, and Y. Seki Biological materials: structure and mechanical properties Prog Mater Sci 53 2008 1 206 (Pubitemid 350017839)
    • (2008) Progress in Materials Science , vol.53 , Issue.1 , pp. 1-206
    • Meyers, M.A.1    Chen, P.-Y.2    Lin, A.Y.-M.3    Seki, Y.4
  • 7
    • 23844484603 scopus 로고    scopus 로고
    • The crustacean exoskeleton as an example of a structurally and mechanically graded biological nanocomposite material
    • DOI 10.1016/j.actamat.2005.05.027, PII S1359645405003265
    • D. Raabe, C. Sachs, and P. Romano The crustacean exoskeleton as an example of a structurally and mechanically graded biological nanocomposite material Acta Mater 53 2005 4281 4292 (Pubitemid 41164420)
    • (2005) Acta Materialia , vol.53 , Issue.15 , pp. 4281-4292
    • Raabe, D.1    Sachs, C.2    Romano, P.3
  • 9
    • 41349096674 scopus 로고    scopus 로고
    • The transition from stiff to compliant materials in squid beaks
    • DOI 10.1126/science.1154117
    • A. Miserez, T. Schneberk, C. Sun, F.W. Zok, and J.H. Waite The transition from stiff to compliant materials in squid beaks Science 319 2008 1816 1819 (Pubitemid 351451587)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1816-1819
    • Miserez, A.1    Schneberk, T.2    Sun, C.3    Zok, F.W.4    Waite, J.H.5
  • 10
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • DOI 10.1016/S0021-9290(03)00135-0
    • F.H. Silver, J.W. Freeman, and G.P. Seehra Collagen self-assembly and the development of tendon mechanical properties J Biomech 36 2003 1529 1553 (Pubitemid 37117360)
    • (2003) Journal of Biomechanics , vol.36 , Issue.10 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 11
    • 2942707997 scopus 로고    scopus 로고
    • Exploring molecular and mechanical gradients in structural bioscaffolds
    • DOI 10.1021/bi049380h
    • J.H. Waite, H.C. Lichtenegger, G.D. Stucky, and P. Hansma Exploring molecular and mechanical gradients in structural bioscaffolds Biochemistry 43 2004 7653 7662 (Pubitemid 38787672)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7653-7662
    • Waite, J.H.1    Lichtenegger, H.C.2    Stucky, G.D.3    Hansma, P.4
  • 12
    • 84858673085 scopus 로고    scopus 로고
    • Changing environments and structure-property relationships in marine biomaterials
    • J.H. Waite, and C.C. Broomell Changing environments and structure-property relationships in marine biomaterials J Exp Biol 215 2012 873 883
    • (2012) J Exp Biol , vol.215 , pp. 873-883
    • Waite, J.H.1    Broomell, C.C.2
  • 13
    • 67349224411 scopus 로고    scopus 로고
    • Short order tendons: Liquid crystal mesophases, metal-complexation and protein gradients in the externalized collagens of mussel byssal threads
    • T. Scheibel, Landes Bioscience Austin
    • M.J. Harrington, and J.H. Waite Short order tendons: liquid crystal mesophases, metal-complexation and protein gradients in the externalized collagens of mussel byssal threads T. Scheibel, Fibrous proteins 2008 Landes Bioscience Austin 1 16
    • (2008) Fibrous Proteins , pp. 1-16
    • Harrington, M.J.1    Waite, J.H.2
  • 15
    • 0005688915 scopus 로고
    • Structure and formation of the Byssus complex in Mytilus (Mollusca Bivalvia)
    • H.A. Price Structure and formation of the Byssus complex in Mytilus (Mollusca Bivalvia) J Molluscan Stud 49 1983 9 17
    • (1983) J Molluscan Stud , vol.49 , pp. 9-17
    • Price, H.A.1
  • 16
    • 0017231408 scopus 로고
    • The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. IV. Observations by transmission electron microscopy
    • A. Bairati, and L. Vitellaro Zuccarello The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. IV. Observations by transmission electron microscopy Cell Tissue Res 166 1976 219 234
    • (1976) Cell Tissue Res , vol.166 , pp. 219-234
    • Bairati, A.1    Vitellaro Zuccarello, L.2
  • 17
    • 52049098695 scopus 로고    scopus 로고
    • Mussel-designed protective coatings for compliant substrates
    • N. Holten-Andersen, and J.H. Waite Mussel-designed protective coatings for compliant substrates J Dent Res 87 2008 701 709
    • (2008) J Dent Res , vol.87 , pp. 701-709
    • Holten-Andersen, N.1    Waite, J.H.2
  • 18
    • 28244477374 scopus 로고    scopus 로고
    • Mapping chemical gradients within and along a fibrous structural tissue, mussel byssal threads
    • DOI 10.1074/jbc.M508674200
    • C. Sun, and J.H. Waite Mapping chemical gradients within and along a fibrous structural tissue, mussel byssal threads J Biol Chem 280 2005 39332 39336 (Pubitemid 41713889)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39332-39336
    • Sun, C.1    Waite, J.H.2
  • 19
    • 0020650782 scopus 로고
    • The ultrastructure of the byssal apparatus of a mussel. V. Localization of collagenic and elastic components in the threads
    • L. Vitellaro-Zuccarello, S. De Biasi, and A. Bairati The ultrastructure of the byssal apparatus of a mussel. V. Localization of collagenic and elastic components in the threads Tissue Cell 15 1983 547 554
    • (1983) Tissue Cell , vol.15 , pp. 547-554
    • Vitellaro-Zuccarello, L.1    De Biasi, S.2    Bairati, A.3
  • 20
    • 0000508581 scopus 로고    scopus 로고
    • Mechanical design of mussel byssus: Material yield enhances attachment strength
    • E. Bell, and J. Gosline Mechanical design of mussel byssus: material yield enhances attachment strength J Exp Biol 199 1996 1005 1017 (Pubitemid 126603739)
    • (1996) Journal of Experimental Biology , vol.199 , Issue.4 , pp. 1005-1017
    • Bell, E.C.1    Gosline, J.M.2
  • 21
    • 79960925340 scopus 로고    scopus 로고
    • Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads
    • A. Hagenau, P. Papadopoulos, F. Kremer, and T. Scheibel Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads J Struct Biol 175 2011 339 347
    • (2011) J Struct Biol , vol.175 , pp. 339-347
    • Hagenau, A.1    Papadopoulos, P.2    Kremer, F.3    Scheibel, T.4
  • 22
    • 0036022290 scopus 로고    scopus 로고
    • A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis
    • J.M. Lucas, E. Vaccaro, and J.H. Waite A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis J Exp Biol 205 2002 1807 1817 (Pubitemid 34853753)
    • (2002) Journal of Experimental Biology , vol.205 , Issue.12 , pp. 1807-1817
    • Lucas, J.M.1    Vaccaro, E.2    Waite, J.H.3
  • 23
    • 0034821348 scopus 로고    scopus 로고
    • Yield and post-yield behavior of mussel byssal thread: A self-healing biomolecular material
    • DOI 10.1021/bm0100514
    • E. Vaccaro, and J.H. Waite Yield and post-yield behavior of mussel byssal thread: a self-healing biomolecular material Biomacromolecules 2 2001 906 911 (Pubitemid 32894649)
    • (2001) Biomacromolecules , vol.2 , Issue.3 , pp. 906-911
    • Vaccaro, E.1    Waite, J.H.2
  • 24
    • 33845966768 scopus 로고    scopus 로고
    • Interspecific comparison of the mechanical properties of mussel byssus
    • S.L. Brazee, and E. Carrington Interspecific comparison of the mechanical properties of mussel byssus Biol Bull 211 2006 263 274 (Pubitemid 46047752)
    • (2006) Biological Bulletin , vol.211 , Issue.3 , pp. 263-274
    • Brazee, S.L.1    Carrington, E.2
  • 25
    • 0001315611 scopus 로고
    • Mechanical properties of mussel byssal threads
    • J.E. Smeathers, and F.F.V. Vincent Mechanical properties of mussel byssal threads J Molluscan Stud 45 1979 219 230
    • (1979) J Molluscan Stud , vol.45 , pp. 219-230
    • Smeathers, J.E.1    Vincent, F.F.V.2
  • 26
    • 37349057043 scopus 로고    scopus 로고
    • Tensile and dynamic mechanical analysis of the distal portion of mussel (Mytilus edulis) byssal threads
    • DOI 10.1098/rsif.2007.1026, PII J34633515J0J2831
    • N. Aldred, T. Wills, D.N. Williams, and A.S. Clare Tensile and dynamic mechanical analysis of the distal portion of mussel (Mytilus edulis) byssal threads J R Soc Interface 4 2007 1159 1167 (Pubitemid 350303868)
    • (2007) Journal of the Royal Society Interface , vol.4 , Issue.17 , pp. 1159-1167
    • Aldred, N.1    Wills, T.2    Williams, D.N.3    Clare, A.S.4
  • 27
    • 33745662632 scopus 로고    scopus 로고
    • Seasonal variation in mussel byssal thread mechanics
    • DOI 10.1242/jeb.02234
    • G.M. Moeser, and E. Carrington Seasonal variation in mussel byssal thread mechanics J Exp Biol 209 2006 1996 2003 (Pubitemid 43965873)
    • (2006) Journal of Experimental Biology , vol.209 , Issue.10 , pp. 1996-2003
    • Moeser, G.M.1    Carrington, E.2
  • 28
    • 70349783566 scopus 로고    scopus 로고
    • Spider silk: From soluble protein to extraordinary fiber
    • M. Heim, D. Keerl, and T. Scheibel Spider silk: from soluble protein to extraordinary fiber Angew Chem Int Ed Engl 48 2009 3584 3596
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 3584-3596
    • Heim, M.1    Keerl, D.2    Scheibel, T.3
  • 29
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: From fibroin sequence to mechanical function
    • J.M. Gosline, P.A. Guerette, C.S. Ortlepp, and K.N. Savage The mechanical design of spider silks: from fibroin sequence to mechanical function J Exp Biol 202 1999 3295 3303 (Pubitemid 30018435)
    • (1999) Journal of Experimental Biology , vol.202 , Issue.23 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Ortlepp, C.S.3    Savage, K.N.4
  • 30
    • 59249098159 scopus 로고    scopus 로고
    • How nature modulates a fiber's mechanical properties: Mechanically distinct fibers drawn from natural mesogenic block copolymer variants
    • M.J. Harrington, and J.H. Waite How nature modulates a fiber's mechanical properties: mechanically distinct fibers drawn from natural mesogenic block copolymer variants Adv Mater 21 2009 440 444
    • (2009) Adv Mater , vol.21 , pp. 440-444
    • Harrington, M.J.1    Waite, J.H.2
  • 31
    • 34548428806 scopus 로고    scopus 로고
    • Mechanics of the hysteretic large strain behavior of mussel byssus threads
    • DOI 10.1007/s10853-007-1649-z, Nano- and micromechanica I prperties of hieracrhal biological materials: Linking mechanics, chemistry and biology
    • K. Bertoldi, and M.C. Boyce Mechanics of the hysteretic large strain behavior of mussel byssus threads J Mater Sci 42 2007 8943 8956 (Pubitemid 47353317)
    • (2007) Journal of Materials Science , vol.42 , Issue.21 , pp. 8943-8956
    • Bertoldi, K.1    Boyce, M.C.2
  • 32
    • 67349119545 scopus 로고    scopus 로고
    • Collagen insulated from tensile damage by domains that unfold reversibly: In situ X-ray investigation of mechanical yield and damage repair in the mussel byssus
    • M.J. Harrington, H.S. Gupta, P. Fratzl, and J.H. Waite Collagen insulated from tensile damage by domains that unfold reversibly: in situ X-ray investigation of mechanical yield and damage repair in the mussel byssus J Struct Biol 167 2009 47 54
    • (2009) J Struct Biol , vol.167 , pp. 47-54
    • Harrington, M.J.1    Gupta, H.S.2    Fratzl, P.3    Waite, J.H.4
  • 33
    • 38149114767 scopus 로고    scopus 로고
    • Holdfast heroics: Comparing the molecular and mechanical properties of Mytilus californianus byssal threads
    • M.J. Harrington, and J.H. Waite Holdfast heroics: comparing the molecular and mechanical properties of Mytilus californianus byssal threads J Exp Biol 210 2007 4307 4318
    • (2007) J Exp Biol , vol.210 , pp. 4307-4318
    • Harrington, M.J.1    Waite, J.H.2
  • 34
    • 84877751226 scopus 로고    scopus 로고
    • Self-repair of a biological fiber guided by an ordered elastic framework
    • S. Krauss, T.H. Metzger, P. Fratzl, and M.J. Harrington Self-repair of a biological fiber guided by an ordered elastic framework Biomacromolecules 14 2013 1520 1528
    • (2013) Biomacromolecules , vol.14 , pp. 1520-1528
    • Krauss, S.1    Metzger, T.H.2    Fratzl, P.3    Harrington, M.J.4
  • 35
    • 0035193168 scopus 로고    scopus 로고
    • Oxidative stress and the mechanical properties of naturally occurring chimeric collagen-containing fibers
    • C. Sun, E. Vaccaro, and J.H. Waite Oxidative stress and the mechanical properties of naturally occurring chimeric collagen-containing fibers Biophys J 81 2001 3590 3595 (Pubitemid 33111502)
    • (2001) Biophysical Journal , vol.81 , Issue.6 , pp. 3590-3595
    • Sun, C.1    Vaccaro, E.2    Waite, J.H.3
  • 36
    • 0000138947 scopus 로고
    • Observations on the rate of production and mechanical properties of the byssus threads of Mytilus edulis
    • J.A. Allen, M. Cook, D.J. Jackson, S. Preston, and E.M. Worth Observations on the rate of production and mechanical properties of the byssus threads of Mytilus edulis J Molluscan Stud 42 1976 279 289
    • (1976) J Molluscan Stud , vol.42 , pp. 279-289
    • Allen, J.A.1    Cook, M.2    Jackson, D.J.3    Preston, S.4    Worth, E.M.5
  • 38
    • 0017161826 scopus 로고
    • Structure and formation of byssus attachment plaque in mytilus
    • A. Tamarin, P. Lewis, and J. Askey Structure and formation of byssus attachment plaque in mytilus J Morphol 149 1976 199 221
    • (1976) J Morphol , vol.149 , pp. 199-221
    • Tamarin, A.1    Lewis, P.2    Askey, J.3
  • 41
    • 0036707217 scopus 로고    scopus 로고
    • The ecomechanics of mussel attachment: From molecules to ecosystems
    • E. Carrington The ecomechanics of mussel attachment: from molecules to ecosystems Integr Comp Biol 42 2002 846 852 (Pubitemid 36224948)
    • (2002) Integrative and Comparative Biology , vol.42 , Issue.4 , pp. 846-852
    • Carrington, E.1
  • 42
    • 0019278313 scopus 로고
    • The collagen gland of Mytilus galloprovincialis: An ultrastructural and cytochemical study on secretory granules
    • DOI 10.1016/S0022-5320(80)90119-7
    • L.V. Zuccarello The collagen gland of Mytilus galloprovincialis - an ultrastractural and cytochemical study on secretory granules J Ultra Struct R 73 1980 135 147 (Pubitemid 11122286)
    • (1980) Journal of Ultrastructure Research , vol.73 , Issue.2 , pp. 135-147
    • Zuccarello, L.V.1
  • 43
    • 84883790545 scopus 로고
    • Le collagène du byssus de Mytilus edulis L.I. Ultrastructure descellules sécrétrices
    • M.M. Pujol, G. Houvenagel, and J. Boullion Le collagène du byssus de Mytilus edulis L.I. Ultrastructure descellules sécrétrices Arch Zool Exp Gen 113 1972 251 264
    • (1972) Arch Zool Exp Gen , vol.113 , pp. 251-264
    • Pujol, M.M.1    Houvenagel, G.2    Boullion, J.3
  • 44
    • 4143101515 scopus 로고    scopus 로고
    • Giant bent-core mesogens in the thread forming process of marine mussels
    • DOI 10.1021/bm049899t
    • T. Hassenkam, T. Gutsmann, P. Hansma, J. Sagert, and J.H. Waite Giant bent-core mesogens in the thread forming process of marine mussels Biomacromolecules 5 2004 1351 1355 (Pubitemid 39089735)
    • (2004) Biomacromolecules , vol.5 , Issue.4 , pp. 1351-1355
    • Hassenkam, T.1    Gutsmann, T.2    Hansma, P.3    Sagert, J.4    Waite, J.H.5
  • 45
    • 0015383685 scopus 로고
    • An ultrastructural study of the byssal thread forming system in Mytilus
    • A. Tamarin, and P.J. Keller An ultrastructural study of the byssal thread forming system in Mytilus J Ultra Struct R 40 1972 401 416
    • (1972) J Ultra Struct R , vol.40 , pp. 401-416
    • Tamarin, A.1    Keller, P.J.2
  • 46
    • 0015962457 scopus 로고
    • Specialized cilia of byssus attachment - Plaque forming region in Mytilus californianus
    • A. Tamarin, P. Lewis, and J. Askey Specialized cilia of byssus attachment - plaque forming region in Mytilus californianus J Morphol 142 1974 321 327
    • (1974) J Morphol , vol.142 , pp. 321-327
    • Tamarin, A.1    Lewis, P.2    Askey, J.3
  • 49
    • 84970581841 scopus 로고
    • Observations of the molecular structure of byssus fibres
    • E. Mercer Observations of the molecular structure of byssus fibres Mar Freshwater Res 3 1952 199 204
    • (1952) Mar Freshwater Res , vol.3 , pp. 199-204
    • Mercer, E.1
  • 50
    • 0002904636 scopus 로고
    • The distribution of collagen and chitin
    • R. Brown, J.F. Danielli, Soc Exp Biol Cambridge University Press Cambridge
    • K.M. Rudall The distribution of collagen and chitin R. Brown, J.F. Danielli, Fibrous proteins and their biological significance Soc Exp Biol vol. 9 1955 Cambridge University Press Cambridge 49 71
    • (1955) Fibrous Proteins and Their Biological Significance , vol.9 VOL. , pp. 49-71
    • Rudall, K.M.1
  • 51
    • 66149108464 scopus 로고    scopus 로고
    • Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis
    • A. Hagenau, H.A. Scheidt, L. Serpell, D. Huster, and T. Scheibel Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis Macromol Biosci 9 2009 162 168
    • (2009) Macromol Biosci , vol.9 , pp. 162-168
    • Hagenau, A.1    Scheidt, H.A.2    Serpell, L.3    Huster, D.4    Scheibel, T.5
  • 52
    • 77950838795 scopus 로고    scopus 로고
    • Iron-clad fibers: A metal-based biological strategy for hard flexible coatings
    • M.J. Harrington, A. Masic, N. Holten-Andersen, J.H. Waite, and P. Fratzl Iron-clad fibers: a metal-based biological strategy for hard flexible coatings Science 328 2010 216 220
    • (2010) Science , vol.328 , pp. 216-220
    • Harrington, M.J.1    Masic, A.2    Holten-Andersen, N.3    Waite, J.H.4    Fratzl, P.5
  • 53
    • 0036856907 scopus 로고    scopus 로고
    • Collagen-binding matrix proteins from elastomeric extraorganismic byssal fibers
    • DOI 10.1021/bm0255903
    • C. Sun, J.M. Lucas, and J.H. Waite Collagen-binding matrix proteins from elastomeric extraorganismic byssal fibers Biomacromolecules 3 2002 1240 1248 (Pubitemid 35428774)
    • (2002) Biomacromolecules , vol.3 , Issue.6 , pp. 1240-1248
    • Sun, C.1    Lucas, J.M.2    Waite, J.H.3
  • 54
    • 33744954494 scopus 로고    scopus 로고
    • Probing the adhesive footprints of Mytilus californianus byssus
    • DOI 10.1074/jbc.M510792200
    • H. Zhao, N.B. Robertson, S.A. Jewhurst, and J.H. Waite Probing the adhesive footprints of Mytilus californianus byssus J Biol Chem 281 2006 11090 11096 (Pubitemid 43855533)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.16 , pp. 11090-11096
    • Zhao, H.1    Robertson, N.B.2    Jewhurst, S.A.3    Waite, J.H.4
  • 55
    • 0012909341 scopus 로고
    • Identification of collagen from byssus threads produced by the sea mussel, Mytilus edulis
    • D.P. Devore, G.H. Engebretson, C.F. Schachtele, and J.J. Sauk Identification of collagen from byssus threads produced by the sea mussel, Mytilus edulis Comp Biochem Physiol B 77 1984 529 531
    • (1984) Comp Biochem Physiol B , vol.77 , pp. 529-531
    • Devore, D.P.1    Engebretson, G.H.2    Schachtele, C.F.3    Sauk, J.J.4
  • 56
    • 84971151388 scopus 로고
    • Catechol oxidase in the byssus of the common mussel, Mytilus edulis-L
    • J.H. Waite Catechol oxidase in the byssus of the common mussel, Mytilus edulis-L J Mar Biol Assoc UK 65 1985 359 371
    • (1985) J Mar Biol Assoc UK , vol.65 , pp. 359-371
    • Waite, J.H.1
  • 57
    • 0029166187 scopus 로고
    • Hydroxyarginine-containing polyphenolic proteins in the adhesive plaques of the marine mussel Mytilus edulis
    • V.V. Papov, T.V. Diamond, K. Biemann, and J.H. Waite Hydroxyarginine- containing polyphenolic proteins in the adhesive plaques of the marine mussel Mytilus edulis J Biol Chem 270 1995 20183 20192
    • (1995) J Biol Chem , vol.270 , pp. 20183-20192
    • Papov, V.V.1    Diamond, T.V.2    Biemann, K.3    Waite, J.H.4
  • 58
    • 0029267044 scopus 로고
    • Exotic collagen gradients in the byssus of the mussel Mytilus edulis
    • X. Qin, and J.H. Waite Exotic collagen gradients in the byssus of the mussel Mytilus edulis J Exp Biol 198 1995 633 644
    • (1995) J Exp Biol , vol.198 , pp. 633-644
    • Qin, X.1    Waite, J.H.2
  • 59
    • 0022762455 scopus 로고
    • Location and analysis of byssal structural proteins of Mytilus edulis
    • C.V. Benedict, and J.H. Waite Location and analysis of byssal structural proteins of Mytilus edulis J Morphol 189 1986 171 181
    • (1986) J Morphol , vol.189 , pp. 171-181
    • Benedict, C.V.1    Waite, J.H.2
  • 60
    • 0023463931 scopus 로고
    • Prolyl 4-hydroxylase in the foot of the marine mussel Mytilus edulis L.: Purification and characterization
    • K. Marumo, and J.H. Waite Prolyl 4-hydroxylase in the foot of the marine mussel Mytilus edulis L.: purification and characterization J Exp Zool 244 1987 365 374
    • (1987) J Exp Zool , vol.244 , pp. 365-374
    • Marumo, K.1    Waite, J.H.2
  • 61
    • 0001336813 scopus 로고
    • Characterization of a cystine-rich polyphenolic protein family from the blue mussel Mytilus edulis-L
    • L.M. Rzepecki, K.M. Hansen, and J.H. Waite Characterization of a cystine-rich polyphenolic protein family from the blue mussel Mytilus edulis-L Biol Bull 183 1992 123 137
    • (1992) Biol Bull , vol.183 , pp. 123-137
    • Rzepecki, L.M.1    Hansen, K.M.2    Waite, J.H.3
  • 62
    • 44449158136 scopus 로고    scopus 로고
    • PH-dependent locking of giant mesogens in fibers drawn from mussel byssal collagens
    • DOI 10.1021/bm8000827
    • M.J. Harrington, and J.H. Waite pH-dependent locking of giant mesogens in fibers drawn from mussel byssal collagens Biomacromolecules 9 2008 1480 1486 (Pubitemid 351757128)
    • (2008) Biomacromolecules , vol.9 , Issue.5 , pp. 1480-1486
    • Harrington, M.J.1    Waite, J.H.2
  • 63
    • 0017126523 scopus 로고
    • Isolation of collagen granules from foot of sea mussel, Mytilus californianus
    • A. Bdolah, and P.J. Keller Isolation of collagen granules from foot of sea mussel, Mytilus californianus Comp Biochem Physiol B 55 1976 171 174
    • (1976) Comp Biochem Physiol B , vol.55 , pp. 171-174
    • Bdolah, A.1    Keller, P.J.2
  • 64
    • 0021099316 scopus 로고
    • Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L
    • J.H. Waite Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L J Biol Chem 258 1983 2911 2915
    • (1983) J Biol Chem , vol.258 , pp. 2911-2915
    • Waite, J.H.1
  • 65
    • 0019336856 scopus 로고
    • The bioadhesive of Mytilus byssus: A protein containing l-dopa
    • J.H. Waite, and M.L. Tanzer The bioadhesive of Mytilus byssus: a protein containing l-dopa Biochem Biophys Res Commun 96 1980 1554 1561
    • (1980) Biochem Biophys Res Commun , vol.96 , pp. 1554-1561
    • Waite, J.H.1    Tanzer, M.L.2
  • 66
    • 0019499337 scopus 로고
    • Polyphenolic substance of Mytilus edulis: Novel adhesive containing L-dopa and hydroxyproline
    • J.H. Waite, and M.L. Tanzer Polyphenolic substance of Mytilus edulis: novel adhesive containing l-dopa and hydroxyproline Science 212 1981 1038 1040 (Pubitemid 11078017)
    • (1981) Science , vol.212 , Issue.4498 , pp. 1038-1040
    • Waite, J.H.1    Tanzer, M.L.2
  • 68
    • 67650046983 scopus 로고    scopus 로고
    • Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis
    • J. Sagert, and J.H. Waite Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis J Exp Biol 212 2009 2224 2236
    • (2009) J Exp Biol , vol.212 , pp. 2224-2236
    • Sagert, J.1    Waite, J.H.2
  • 71
    • 0034086247 scopus 로고    scopus 로고
    • In search of molecular dovetails in mussel byssus: From the threads to the stem
    • K.J. Coyne, and J.H. Waite In search of molecular dovetails in mussel byssus: from the threads to the stem J Exp Biol 203 2000 1425 1431 (Pubitemid 30351513)
    • (2000) Journal of Experimental Biology , vol.203 , Issue.9 , pp. 1425-1431
    • Coyne, K.J.1    Waite, J.H.2
  • 72
    • 0030865952 scopus 로고    scopus 로고
    • Extensible collagen in mussel byssus: A natural block copolymer
    • DOI 10.1126/science.277.5333.1830
    • K.J. Coyne, X.X. Qin, and J.H. Waite Extensible collagen in mussel byssus: a natural block copolymer Science 277 1997 1830 1832 (Pubitemid 27449196)
    • (1997) Science , vol.277 , Issue.5333 , pp. 1830-1832
    • Coyne, K.J.1    Qin, X.-X.2    Waite, J.H.3
  • 73
    • 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
    • K. Inoue, Y. Takeuchi, D. Miki, S. Odo, S. Harayama, and J.H. Waite Cloning, sequencing and sites of expression of genes for the hydroxyarginine-containing adhesive-plaque protein of the mussel Mytilus galloprovincialis Eur J Biochem 239 1996 172 176 (Pubitemid 26228156)
    • (1996) European Journal of Biochemistry , vol.239 , Issue.1 , pp. 172-176
    • Inoue, K.1    Takeuchi, Y.2    Miki, D.3    Odo, S.4    Harayama, S.5    Waite, J.H.6
  • 74
    • 0035814883 scopus 로고    scopus 로고
    • Polyphosphoprotein from the adhesive pads of Mytilus edulis
    • DOI 10.1021/bi002718x
    • J.H. Waite, and X. Qin Polyphosphoprotein from the adhesive pads of Mytilus edulis Biochemistry 40 2001 2887 2893 (Pubitemid 32198291)
    • (2001) Biochemistry , vol.40 , Issue.9 , pp. 2887-2893
    • Waite, J.H.1    Qin, X.2
  • 75
    • 33751575809 scopus 로고    scopus 로고
    • Proteins in load-bearing junctions: The Histidine-rich metal-binding protein of mussel byssus
    • DOI 10.1021/bi061677n
    • H. Zhao, and J.H. Waite Proteins in load-bearing junctions: the histidine-rich metal-binding protein of mussel byssus Biochemistry 45 2006 14223 14231 (Pubitemid 44846211)
    • (2006) Biochemistry , vol.45 , Issue.47 , pp. 14223-14231
    • Zhao, H.1    Waite, J.H.2
  • 77
    • 0028445988 scopus 로고
    • The adhesive protein cDNA of Mytilus galloprovincialis encodes decapeptide repeats but no hexapeptide motif
    • K. Inoue, and S. Odo The adhesive protein cDNA of Mytilus galloprovincialis encodes decapeptide repeats but no hexapeptide motif Biol Bull 186 1994 349 355 (Pubitemid 2108749)
    • (1994) Biological Bulletin , vol.186 , Issue.3 , pp. 349-355
    • Inoue, K.1    Odo, S.2
  • 78
    • 0028939986 scopus 로고
    • Mussel adhesive plaque protein gene is a novel member of epidermal growth factor-like gene family
    • K. Inoue, Y. Takeuchi, D. Miki, and S. Odo Mussel adhesive plaque protein gene is a novel member of epidermal growth factor-like gene family J Biol Chem 270 1995 6698 6701
    • (1995) J Biol Chem , vol.270 , pp. 6698-6701
    • Inoue, K.1    Takeuchi, Y.2    Miki, D.3    Odo, S.4
  • 79
    • 33748743983 scopus 로고    scopus 로고
    • Linking adhesive and structural proteins in the attachment plaque of Mytilus californianus
    • DOI 10.1074/jbc.M604357200
    • H. Zhao, and J.H. Waite Linking adhesive and structural proteins in the attachment plaque of Mytilus californianus J Biol Chem 281 2006 26150 26158 (Pubitemid 44401822)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26150-26158
    • Zhao, H.1    Waite, J.H.2
  • 80
    • 0031437429 scopus 로고    scopus 로고
    • Tough tendons. Mussel byssus has collagen with silk-like domains
    • DOI 10.1074/jbc.272.51.32623
    • X.X. Qin, K.J. Coyne, and J.H. Waite Tough tendons. Mussel byssus has collagen with silk-like domains J Biol Chem 272 1997 32623 32627 (Pubitemid 28011952)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32623-32627
    • Qin, X.-X.1    Coyne, K.J.2    Waite, J.H.3
  • 81
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • DOI 10.1038/nprot.2007.131, PII NPROT.2007.131
    • O. Emanuelsson, S. Brunak, G. von Heijne, and H. Nielsen Locating proteins in the cell using TargetP. SignalP and related tools Nat Protoc 2 2007 953 971 (Pubitemid 46745592)
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 83
    • 0034858667 scopus 로고    scopus 로고
    • Spider flagelliform silk: Lessons in protein design, gene structure, and molecular evolution
    • DOI 10.1002/bies.1105
    • C.Y. Hayashi, and R.V. Lewis Spider flagelliform silk: lessons in protein design, gene structure and molecular evolution Bioessays 23 2001 750 756 (Pubitemid 32792520)
    • (2001) BioEssays , vol.23 , Issue.8 , pp. 750-756
    • Hayashi, C.Y.1    Lewis, R.V.2
  • 84
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • DOI 10.1046/j.1432-1327.1998.2580001.x
    • B. Vrhovski, and A.S. Weiss Biochemistry of tropoelastin Eur J Biochem 258 1998 1 18 (Pubitemid 28538302)
    • (1998) European Journal of Biochemistry , vol.258 , Issue.1 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 85
    • 0003664714 scopus 로고
    • Conformation in fibrous proteins and related synthetic polypeptides
    • Academic Press New York [chapter 12]
    • R.D.B. Fraser, and T.P. MacRae Conformation in fibrous proteins and related synthetic polypeptides The influence of composition on conformation 1973 Academic Press New York 276 290 [chapter 12]
    • (1973) The Influence of Composition on Conformation , pp. 276-290
    • Fraser, R.D.B.1    Macrae, T.P.2
  • 87
    • 0031862042 scopus 로고    scopus 로고
    • The peculiar collagens of mussel byssus
    • DOI 10.1016/S0945-053X(98)90023-3
    • J.H. Waite, X.X. Qin, and K.J. Coyne The peculiar collagens of mussel byssus Matrix Biol 17 1998 93 106 (Pubitemid 28310244)
    • (1998) Matrix Biology , vol.17 , Issue.2 , pp. 93-106
    • Waite, J.H.1    Qin, X.-X.2    Coyne, K.J.3
  • 88
    • 0022519320 scopus 로고
    • A gene encoding a novel glycine-rich structural protein of petunia
    • C.M. Condit, and R.B. Meagher A gene encoding a novel glycine-rich structural protein of petunia Nature 323 1986 178 181 (Pubitemid 16024970)
    • (1986) Nature , vol.322 , Issue.6084 , pp. 178-181
    • Condit, C.M.1    Meagher, R.B.2
  • 89
    • 0023737318 scopus 로고
    • Small gene family encoding an eggshell (chorion) protein of the human parasite Schistosoma-Mansoni
    • L.A. Bobek, D.M. Rekosh, and P.T. Loverde Small gene family encoding an eggshell (chorion) protein of the human parasite Schistosoma-Mansoni Mol Cell Biol 8 1988 3008 3016
    • (1988) Mol Cell Biol , vol.8 , pp. 3008-3016
    • Bobek, L.A.1    Rekosh, D.M.2    Loverde, P.T.3
  • 90
    • 0003664714 scopus 로고
    • Conformation in fibrous proteins and related synthetic polypeptides
    • Academic Press New York [chapter 9]
    • R.D.B. Fraser, and T.P. MacRae Conformation in fibrous proteins and related synthetic polypeptides The alpha helix 1973 Academic Press New York 179 217 [chapter 9]
    • (1973) The Alpha Helix , pp. 179-217
    • Fraser, R.D.B.1    Macrae, T.P.2
  • 91
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • C.N. Pace, and J.M. Scholtz A helix propensity scale based on experimental studies of peptides and proteins Biophys J 75 1998 422 427 (Pubitemid 28311831)
    • (1998) Biophysical Journal , vol.75 , Issue.1 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 92
    • 0034643851 scopus 로고    scopus 로고
    • Beta transition and stress-induced phase separation in the spinning of spider dragline silk
    • DOI 10.1016/S0141-8130(00)00124-0, PII S0141813000001240
    • D.P. Knight, M.M. Knight, and F. Vollrath Beta transition and stress-induced phase separation in the spinning of spider dragline silk Int J Biol Macromol 27 2000 205 210 (Pubitemid 30316291)
    • (2000) International Journal of Biological Macromolecules , vol.27 , Issue.3 , pp. 205-210
    • Knight, D.P.1    Knight, M.M.2    Vollrath, F.3
  • 93
    • 0036678028 scopus 로고    scopus 로고
    • The molecular structure of spider dragline silk: Folding and orientation of the protein backbone
    • J.D. van Beek, S. Hess, F. Vollrath, and B.H. Meier The molecular structure of spider dragline silk: folding and orientation of the protein backbone Proc Natl Acad Sci USA 99 2002 10266 10271
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10266-10271
    • Van Beek, J.D.1    Hess, S.2    Vollrath, F.3    Meier, B.H.4
  • 94
    • 0003664714 scopus 로고
    • Conformation in fibrous proteins and related synthetic polypeptides
    • Academic Press New York [chapter 14]
    • R.D.B. Fraser, and T.P. MacRae Conformation in fibrous proteins and related synthetic polypeptides Collagens 1973 Academic Press New York 344 402 [chapter 14]
    • (1973) Collagens , pp. 344-402
    • Fraser, R.D.B.1    Macrae, T.P.2
  • 95
    • 84898597786 scopus 로고    scopus 로고
    • Structural diversity of a collagen-binding matrix protein from the byssus of blue mussels upon refolding
    • 10.1016/j.jsb.2014.02.013
    • M.H. Suhre, and T. Scheibel Structural diversity of a collagen-binding matrix protein from the byssus of blue mussels upon refolding J Struct Biol 2014 10.1016/j.jsb.2014.02.013
    • (2014) J Struct Biol
    • Suhre, M.H.1    Scheibel, T.2
  • 96
    • 84905506446 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of Proximal Thread Matrix Protein 1 (PTMP1) from Mytilus galloprovincialis
    • [submitted for publication]
    • M.H. Suhre, T. Scheibel, C. Steegborn, and M. Gertz Crystallization and preliminary X-ray diffraction analysis of Proximal Thread Matrix Protein 1 (PTMP1) from Mytilus galloprovincialis Acta Crystallogr Sect F 2014 [submitted for publication]
    • (2014) Acta Crystallogr Sect F
    • Suhre, M.H.1    Scheibel, T.2    Steegborn, C.3    Gertz, M.4
  • 97
    • 84905506858 scopus 로고    scopus 로고
    • Structural and functional features of a collagen binding matrix protein from the mussel byssus
    • 10.1038/ncomms4392
    • M.H. Suhre, M. Gertz, C. Steegborn, and T. Scheibel Structural and functional features of a collagen binding matrix protein from the mussel byssus Nat Commun 2014 10.1038/ncomms4392
    • (2014) Nat Commun
    • Suhre, M.H.1    Gertz, M.2    Steegborn, C.3    Scheibel, T.4
  • 98
    • 33751571086 scopus 로고    scopus 로고
    • Chemical subtleties of mussel and polychaete holdfasts
    • A.M. Smith, J.A. Callow, Springer-Verlag Berlin
    • J. Sagert, C. Sun, and J.H. Waite Chemical subtleties of mussel and polychaete holdfasts A.M. Smith, J.A. Callow, Biological adhesives 2006 Springer-Verlag Berlin 125 143
    • (2006) Biological Adhesives , pp. 125-143
    • Sagert, J.1    Sun, C.2    Waite, J.H.3
  • 101
    • 77955478320 scopus 로고    scopus 로고
    • Protein- and metal-dependent interactions of a prominent protein in mussel adhesive plaques
    • D.S. Hwang, H. Zeng, A. Masic, M.J. Harrington, J.N. Israelachvili, and J.H. Waite Protein- and metal-dependent interactions of a prominent protein in mussel adhesive plaques J Biol Chem 285 2010 25850 25858
    • (2010) J Biol Chem , vol.285 , pp. 25850-25858
    • Hwang, D.S.1    Zeng, H.2    Masic, A.3    Harrington, M.J.4    Israelachvili, J.N.5    Waite, J.H.6
  • 102
  • 103
  • 104
    • 0028171667 scopus 로고
    • Trans-2,3-Cis-3,4-dihydroxyproline, a new naturally-occurring amino-acid is the 6th residue in the tandemly repeated consensus decapeptides of an adhesive protein from Mytilus edulis
    • S.W. Taylor, J.H. Waite, M.M. Ross, J. Shabanowitz, and D.F. Hunt Trans-2,3-Cis-3,4-dihydroxyproline, a new naturally-occurring amino-acid is the 6th residue in the tandemly repeated consensus decapeptides of an adhesive protein from Mytilus edulis J Am Chem Soc 116 1994 10803 10804
    • (1994) J Am Chem Soc , vol.116 , pp. 10803-10804
    • Taylor, S.W.1    Waite, J.H.2    Ross, M.M.3    Shabanowitz, J.4    Hunt, D.F.5
  • 105
    • 69949149109 scopus 로고    scopus 로고
    • Glycosylated hydroxytryptophan in a mussel adhesive protein from perna viridis
    • H. Zhao, J. Sagert, D.S. Hwang, and J.H. Waite Glycosylated hydroxytryptophan in a mussel adhesive protein from perna viridis J Biol Chem 284 2009 23344 23352
    • (2009) J Biol Chem , vol.284 , pp. 23344-23352
    • Zhao, H.1    Sagert, J.2    Hwang, D.S.3    Waite, J.H.4
  • 106
    • 0034489585 scopus 로고    scopus 로고
    • Phenoloxidase (E.C. 1.14.18.1) from the byssus gland of Mytilus edulis: Purification, partial characterization and application for screening products with potential antifouling activities
    • C. Hellio, N. Bourgougnon, and Y. Le Gal Phenoloxidase (EC 1.14.18.1) from the byssus gland of Mytilus edulis: purification, partial characterization and application for screening products with potential antifouling activities Biofouling 16 2000 235 244 (Pubitemid 32106227)
    • (2000) Biofouling , vol.16 , Issue.2-4 , pp. 235-244
    • Hellio, C.1    Bourgougnon, N.2    Le Gal, Y.3
  • 109
    • 0001704314 scopus 로고
    • A technique for the histochemical demonstration of polyphenol oxidase and its application to egg-shell formation in helminths and Byssus formation in Mytillus
    • J.D. Smyth A technique for the histochemical demonstration of polyphenol oxidase and its application to egg-shell formation in helminths and Byssus formation in Mytillus Q J Microsc Sci 95 1954 139 152
    • (1954) Q J Microsc Sci , vol.95 , pp. 139-152
    • Smyth, J.D.1
  • 111
    • 56349098272 scopus 로고    scopus 로고
    • Revisiting the molecular structure of collagen
    • K. Okuyama Revisiting the molecular structure of collagen Connect Tissue Res 49 2008 299 310
    • (2008) Connect Tissue Res , vol.49 , pp. 299-310
    • Okuyama, K.1
  • 112
  • 113
    • 32844463093 scopus 로고
    • Structure of collagen
    • A. Rich, and F.H.C. Crick Structure of collagen Nature 176 1955 915 916
    • (1955) Nature , vol.176 , pp. 915-916
    • Rich, A.1    Crick, F.H.C.2
  • 114
    • 0033034104 scopus 로고    scopus 로고
    • Structure analysis of a collagen-model peptide with a (Pro-Hyp-Gly) sequence repeat
    • V. Nagarajan, S. Kamitori, and K. Okuyama Structure analysis of a collagen-model peptide with a (Pro-Hyp-Gly) sequence repeat J Biochem 125 1999 310 318 (Pubitemid 29112296)
    • (1999) Journal of Biochemistry , vol.125 , Issue.2 , pp. 310-318
    • Nagarajan, V.1    Kamitori, S.2    Okuyama, K.3
  • 115
    • 0033077144 scopus 로고    scopus 로고
    • 7/2-Helical model for collagen - Evidence from model peptides
    • K. Okuyama, V. Nagarajan, and S. Kamitori 7/2-Helical model for collagen - evidence from model peptides Proc Indian Natl Sci Acad 111 1999 19 34
    • (1999) Proc Indian Natl Sci Acad , vol.111 , pp. 19-34
    • Okuyama, K.1    Nagarajan, V.2    Kamitori, S.3
  • 117
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides
    • DOI 10.1006/jsbi.1998.3977
    • J.A.M. Ramshaw, N.K. Shah, and B. Brodsky Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides J Struct Biol 122 1998 86 91 (Pubitemid 28411187)
    • (1998) Journal of Structural Biology , vol.122 , Issue.1-2 , pp. 86-91
    • Ramshaw, J.A.M.1    Shah, N.K.2    Brodsky, B.3
  • 118
    • 0036007873 scopus 로고    scopus 로고
    • Insights on the conformational stability of collagen
    • DOI 10.1039/a903001h
    • C.L. Jenkins, and R.T. Raines Insights on the conformational stability of collagen Nat Prod Rep 19 2002 49 59 (Pubitemid 34140332)
    • (2002) Natural Product Reports , vol.19 , Issue.1 , pp. 49-59
    • Jenkins, C.L.1    Raines, R.T.2
  • 119
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution
    • J. Bella, M. Eaton, B. Brodsky, and H.M. Berman Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution Science 266 1994 75 81
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 120
    • 33747789133 scopus 로고    scopus 로고
    • Conformational Effects of Gly-X-Gly Interruptions in the Collagen Triple Helix
    • DOI 10.1016/j.jmb.2006.07.014, PII S0022283606008801
    • J. Bella, J. Liu, R. Kramer, B. Brodsky, and H.M. Berman Conformational effects of Gly-X-Gly interruptions in the collagen triple helix J Mol Biol 362 2006 298 311 (Pubitemid 44278853)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.2 , pp. 298-311
    • Bella, J.1    Liu, J.2    Kramer, R.3    Brodsky, B.4    Berman, H.M.5
  • 121
    • 38649105499 scopus 로고    scopus 로고
    • Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: Sequence analysis and structural studies on triple-helix peptide models
    • G. Thiagarajan, Y. Li, A. Mohs, C. Strafaci, M. Popiel, J. Baum, and B. Brodsky Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models J Mol Biol 376 2008 736 748
    • (2008) J Mol Biol , vol.376 , pp. 736-748
    • Thiagarajan, G.1    Li, Y.2    Mohs, A.3    Strafaci, C.4    Popiel, M.5    Baum, J.6    Brodsky, B.7
  • 122
    • 57749106685 scopus 로고    scopus 로고
    • Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries
    • S.P. Boudko, J. Engel, K. Okuyama, K. Mizuno, H.P. Bachinger, and M.A. Schumacher Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries J Biol Chem 283 2008 32580 32589
    • (2008) J Biol Chem , vol.283 , pp. 32580-32589
    • Boudko, S.P.1    Engel, J.2    Okuyama, K.3    Mizuno, K.4    Bachinger, H.P.5    Schumacher, M.A.6
  • 123
    • 47749145413 scopus 로고    scopus 로고
    • Triple-helical peptides: An approach to collagen conformation, stability and self-association
    • B. Brodsky, G. Thiagarajan, B. Madhan, and K. Kar Triple-helical peptides: an approach to collagen conformation, stability and self-association Biopolymers 89 2008 345 353
    • (2008) Biopolymers , vol.89 , pp. 345-353
    • Brodsky, B.1    Thiagarajan, G.2    Madhan, B.3    Kar, K.4
  • 124
    • 0029609620 scopus 로고
    • Protein motifs. 8. The triple-helix motif in proteins
    • B. Brodsky, and N.K. Shah Protein motifs. 8. The triple-helix motif in proteins FASEB J 9 1995 1537 1546
    • (1995) FASEB J , vol.9 , pp. 1537-1546
    • Brodsky, B.1    Shah, N.K.2
  • 125
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • DOI 10.1074/jbc.M501657200
    • A.V. Persikov, J.A. Ramshaw, and B. Brodsky Prediction of collagen stability from amino acid sequence J Biol Chem 280 2005 19343 19349 (Pubitemid 41379641)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 127
    • 0033099169 scopus 로고    scopus 로고
    • Expression of a model peptide of a marine mussel adhesive protein in Escherichia coli and characterization of its structural and functional properties
    • M. Kitamura, K. Kawakami, N. Nakamura, K. Tsumoto, H. Uchiyama, Y. Ueda, I. Kumagai, and T. Nakaya Expression of a model peptide of a marine mussel adhesive protein in Escherichia coli and characterization of its structural and functional properties J Polym Sci Polym Chem 37 1999 729 736
    • (1999) J Polym Sci Polym Chem , vol.37 , pp. 729-736
    • Kitamura, M.1    Kawakami, K.2    Nakamura, N.3    Tsumoto, K.4    Uchiyama, H.5    Ueda, Y.6    Kumagai, I.7    Nakaya, T.8
  • 128
    • 53449089869 scopus 로고    scopus 로고
    • A novel expression system for recombinant marine mussel adhesive protein Mefp1 using a truncated OmpA signal peptide
    • S.J. Lee, Y.H. Han, B.H. Nam, Y.O. Kim, and P.R. Reeves A novel expression system for recombinant marine mussel adhesive protein Mefp1 using a truncated OmpA signal peptide Mol Cells 26 2008 34 40
    • (2008) Mol Cells , vol.26 , pp. 34-40
    • Lee, S.J.1    Han, Y.H.2    Nam, B.H.3    Kim, Y.O.4    Reeves, P.R.5
  • 129
    • 0027312161 scopus 로고
    • Cloning, expression, and characterization of a synthetic analog to the bioadhesive precursor protein of the sea mussel Mytilus edulis
    • A.J. Salerno, and I. Goldberg Cloning, expression and characterization of a synthetic analog to the bioadhesive precursor protein of the sea mussel Mytilus edulis Appl Microbiol Biotechnol 39 1993 221 226 (Pubitemid 23134611)
    • (1993) Applied Microbiology and Biotechnology , vol.39 , Issue.2 , pp. 221-226
    • Salerno, A.J.1    Goldberg, I.2
  • 130
    • 0033742794 scopus 로고    scopus 로고
    • Immunolocalization of Dpfp1, a byssal protein of the zebra mussel Dreissena polymorpha
    • K.E. Anderson, and J.H. Waite Immunolocalization of Dpfp1, a byssal protein of the zebra mussel Dreissena polymorpha J Exp Biol 203 2000 3065 3076
    • (2000) J Exp Biol , vol.203 , pp. 3065-3076
    • Anderson, K.E.1    Waite, J.H.2
  • 131
    • 2942532196 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli
    • DOI 10.1128/AEM.70.6.3352-3359.2004
    • D.S. Hwang, H.J. Yoo, J.H. Jun, W.K. Moon, and H.J. Cha Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli Appl Environ Microbiol 70 2004 3352 3359 (Pubitemid 38745878)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.6 , pp. 3352-3359
    • Hwang, D.S.1    Yoo, H.J.2    Jun, J.H.3    Moon, W.K.4    Cha, H.J.5
  • 132
    • 20144366711 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli
    • DOI 10.1021/bp050014e
    • D.S. Hwang, Y. Gim, and H.J. Cha Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli Biotechnol Progr 21 2005 965 970 (Pubitemid 40772305)
    • (2005) Biotechnology Progress , vol.21 , Issue.3 , pp. 965-970
    • Dong, S.H.1    Gim, Y.2    Hyung, J.C.3
  • 133
    • 84862832830 scopus 로고    scopus 로고
    • Recombinant mussel adhesive protein fp-5 (MAP fp-5) as a bulk bioadhesive and surface coating material
    • Y.S. Choi, D.G. Kang, S. Lim, Y.J. Yang, C.S. Kim, and H.J. Cha Recombinant mussel adhesive protein fp-5 (MAP fp-5) as a bulk bioadhesive and surface coating material Biofouling 27 2011 729 737
    • (2011) Biofouling , vol.27 , pp. 729-737
    • Choi, Y.S.1    Kang, D.G.2    Lim, S.3    Yang, Y.J.4    Kim, C.S.5    Cha, H.J.6
  • 135
  • 136
    • 77957311585 scopus 로고    scopus 로고
    • Cell behavior on extracellular matrix mimic materials based on mussel adhesive protein fused with functional peptides
    • B.H. Choi, Y.S. Choi, D.G. Kang, B.J. Kim, Y.H. Song, and H.J. Cha Cell behavior on extracellular matrix mimic materials based on mussel adhesive protein fused with functional peptides Biomaterials 31 2010 8980 8988
    • (2010) Biomaterials , vol.31 , pp. 8980-8988
    • Choi, B.H.1    Choi, Y.S.2    Kang, D.G.3    Kim, B.J.4    Song, Y.H.5    Cha, H.J.6
  • 137
    • 62249159188 scopus 로고    scopus 로고
    • Production of fusion mussel adhesive fp-353 in Escherichia coli
    • Y. Gim, D.S. Hwang, S. Lim, Y.H. Song, and H.J. Cha Production of fusion mussel adhesive fp-353 in Escherichia coli Biotechnol Progr 24 2008 1272 1277
    • (2008) Biotechnol Progr , vol.24 , pp. 1272-1277
    • Gim, Y.1    Hwang, D.S.2    Lim, S.3    Song, Y.H.4    Cha, H.J.5
  • 138
    • 34249307818 scopus 로고    scopus 로고
    • Practical recombinant hybrid mussel bioadhesive fp-151
    • DOI 10.1016/j.biomaterials.2007.04.039, PII S0142961207003651
    • D.S. Hwang, Y. Gim, H.J. Yoo, and H.J. Cha Practical recombinant hybrid mussel bloadhesive fp-151 Biomaterials 28 2007 3560 3568 (Pubitemid 46817658)
    • (2007) Biomaterials , vol.28 , Issue.24 , pp. 3560-3568
    • Hwang, D.S.1    Gim, Y.2    Yoo, H.J.3    Cha, H.J.4
  • 139
    • 34447279470 scopus 로고    scopus 로고
    • Cell adhesion biomaterial based on mussel adhesive protein fused with RGD peptide
    • DOI 10.1016/j.biomaterials.2007.05.028, PII S0142961207004450
    • D.S. Hwang, S.B. Sim, and H.J. Cha Cell adhesion biomaterial based on mussel adhesive protein fused with RGD peptide Biomaterials 28 2007 4039 4046 (Pubitemid 47048378)
    • (2007) Biomaterials , vol.28 , Issue.28 , pp. 4039-4046
    • Hwang, D.S.1    Sim, S.B.2    Cha, H.J.3
  • 140
    • 76649089944 scopus 로고    scopus 로고
    • Towards the recombinant production of mussel byssal collagens
    • A. Hagenau, and T. Scheibel Towards the recombinant production of mussel byssal collagens J Adhes 86 2010 10 24
    • (2010) J Adhes , vol.86 , pp. 10-24
    • Hagenau, A.1    Scheibel, T.2
  • 141
    • 36749099994 scopus 로고    scopus 로고
    • Understanding marine mussel adhesion
    • DOI 10.1007/s10126-007-9053-x
    • H.G. Silverman, and F.F. Roberto Understanding marine mussel adhesion Mar Biotechnol NY 9 2007 661 681 (Pubitemid 50001748)
    • (2007) Marine Biotechnology , vol.9 , Issue.6 , pp. 661-681
    • Silverman, H.G.1    Roberto, F.F.2
  • 142
    • 33845668340 scopus 로고    scopus 로고
    • Recombinant mussel adhesive protein Mgfp-5 as cell adhesion biomaterial
    • DOI 10.1016/j.jbiotec.2006.08.005, PII S0168165606006936
    • D.S. Hwang, Y. Gim, D.G. Kang, Y.K. Kim, and H.J. Cha Recombinant mussel adhesive protein Mgfp-5 as cell adhesion biomaterial J Biotechnol 127 2007 727 735 (Pubitemid 44959115)
    • (2007) Journal of Biotechnology , vol.127 , Issue.4 , pp. 727-735
    • Hwang, D.S.1    Gim, Y.2    Kang, D.G.3    Kim, Y.K.4    Cha, H.J.5
  • 143
    • 0035912971 scopus 로고    scopus 로고
    • Biomedical applications of collagen
    • DOI 10.1016/S0378-5173(01)00691-3, PII S0378517301006913
    • C.H. Lee, A. Singla, and Y. Lee Biomedical applications of collagen Int J Pharm 221 2001 1 22 (Pubitemid 32524031)
    • (2001) International Journal of Pharmaceutics , vol.221 , Issue.1-2 , pp. 1-22
    • Lee, C.H.1    Singla, A.2    Lee, Y.3
  • 144
    • 0344642607 scopus 로고    scopus 로고
    • Collagen based dressings - A review
    • S.K. Purna, and M. Babu Collagen based dressings - a review Burns 26 2000 54 62
    • (2000) Burns , vol.26 , pp. 54-62
    • Purna, S.K.1    Babu, M.2
  • 145
    • 42449118993 scopus 로고    scopus 로고
    • Collagen tissue engineering: Development of novel biomaterials and applications
    • DOI 10.1203/PDR.0b013e31816c5bc3, PII 0000645020080500000007
    • L. Cen, W. Liu, L. Cui, W. Zhang, and Y. Cao Collagen tissue engineering: development of novel biomaterials and applications Pediatr Res 63 2008 492 496 (Pubitemid 351572218)
    • (2008) Pediatric Research , vol.63 , Issue.5 , pp. 492-496
    • Cen, L.1    Liu, W.2    Cui, L.3    Zhang, W.4    Cao, Y.5
  • 146
    • 0034031879 scopus 로고    scopus 로고
    • Collagen-based biomaterials as 3D scaffold for cell cultures: Applications for tissue engineering and gene therapy
    • B. Chevallay, and D. Herbage Collagen-based biomaterials as 3D scaffold for cell cultures: applications for tissue engineering and gene therapy Med Biol Eng Comput 38 2000 211 218 (Pubitemid 30192997)
    • (2000) Medical and Biological Engineering and Computing , vol.38 , Issue.2 , pp. 211-218
    • Chevallay, B.1    Herbage, D.2
  • 147
    • 33744768410 scopus 로고    scopus 로고
    • Collagen fillers
    • DOI 10.1111/j.1529-8019.2006.00067.x
    • L. Baumann, J. Kaufman, and S. Saghari Collagen fillers Dermatol Ther 19 2006 134 140 (Pubitemid 43825125)
    • (2006) Dermatologic Therapy , vol.19 , Issue.3 , pp. 134-140
    • Baumann, L.1    Kaufman, J.2    Saghari, S.3
  • 148
    • 34447309024 scopus 로고    scopus 로고
    • The utility of soft tissue fillers in clinical dermatology: Treatment of fine wrinkles and skin defects
    • DOI 10.1586/17434440.4.4.559
    • N. Sadick, and L. Sorhaindo The utility of soft tissue fillers in clinical dermatology: treatment of fine wrinkles and skin defects Expert Rev Med Devices 4 2007 559 565 (Pubitemid 47050202)
    • (2007) Expert Review of Medical Devices , vol.4 , Issue.4 , pp. 559-565
    • Sadick, N.1    Sorhaindo, L.2
  • 149
    • 0026414058 scopus 로고
    • Mussel beards - A coming of age
    • J.H. Waite Mussel beards - a coming of age Chem Ind 1991 607 611
    • (1991) Chem Ind , pp. 607-611
    • Waite, J.H.1
  • 151
    • 0023356309 scopus 로고
    • Mussel adhesive protein - Permeability characteristics when used as a basement-membrane
    • K. Green, R. Berdecia, and L. Cheeks Mussel adhesive protein - permeability characteristics when used as a basement-membrane Curr Eye Res 6 1987 835 838
    • (1987) Curr Eye Res , vol.6 , pp. 835-838
    • Green, K.1    Berdecia, R.2    Cheeks, L.3
  • 153
    • 0032477983 scopus 로고    scopus 로고
    • Enzymatic tempering of a mussel adhesive protein film
    • D.C. Hansen, S.G. Corcoran, and J.H. Waite Enzymatic tempering of a mussel adhesive protein film Langmuir 14 1998 1139 1147 (Pubitemid 128620515)
    • (1998) Langmuir , vol.14 , Issue.5 , pp. 1139-1147
    • Hansen, D.C.1    Corcoran, S.G.2    Waite, J.H.3
  • 154
    • 67149133194 scopus 로고    scopus 로고
    • Mimicking biopolymers on a molecular scale: Nano(bio)technology based on engineered proteins
    • I. Grunwald, K. Rischka, S.M. Kast, T. Scheibel, and H. Bargel Mimicking biopolymers on a molecular scale: nano(bio)technology based on engineered proteins Phil Trans R Soc A 367 2009 1727 1747
    • (2009) Phil Trans R Soc A , vol.367 , pp. 1727-1747
    • Grunwald, I.1    Rischka, K.2    Kast, S.M.3    Scheibel, T.4    Bargel, H.5
  • 155
    • 0030347496 scopus 로고    scopus 로고
    • Marine adhesive proteins and some biotechnological applications
    • H. Yamamoto Marine adhesive proteins and some biotechnological applications Biotechnol Genet Eng 13 1996 133 165
    • (1996) Biotechnol Genet Eng , vol.13 , pp. 133-165
    • Yamamoto, H.1
  • 156
    • 0032120933 scopus 로고    scopus 로고
    • Synthetic polypeptide mimics of marine adhesives
    • M.E. Yu, and T.J. Deming Synthetic polypeptide mimics of marine adhesives Macromolecules 31 1998 4739 4745 (Pubitemid 128565485)
    • (1998) Macromolecules , vol.31 , Issue.15 , pp. 4739-4745
    • Yu, M.1    Deming, T.J.2
  • 157
    • 0034641671 scopus 로고    scopus 로고
    • Cross-linking in adhesive quinoproteins: Studies with model decapeptides
    • L.A. Burzio, and J.H. Waite Cross-linking in adhesive quinoproteins: studies with model decapeptides Biochemistry 39 2000 11147 11153
    • (2000) Biochemistry , vol.39 , pp. 11147-11153
    • Burzio, L.A.1    Waite, J.H.2
  • 158
    • 76649130915 scopus 로고    scopus 로고
    • Structural and biophysical characterization of a cyclic bioadhesive with cell attachment ability
    • M.P. Olivieri, R.M. Wollman, M.I. Hurley, and M.F. Swartz Structural and biophysical characterization of a cyclic bioadhesive with cell attachment ability J Adhes 86 2010 111 130
    • (2010) J Adhes , vol.86 , pp. 111-130
    • Olivieri, M.P.1    Wollman, R.M.2    Hurley, M.I.3    Swartz, M.F.4
  • 159
    • 34248163353 scopus 로고    scopus 로고
    • Co-polypeptides of 3,4-dihydroxyphenylalanine and l-lysine to mimic marine adhesive protein
    • DOI 10.1016/j.biomaterials.2007.04.009, PII S0142961207002876
    • J. Wang, C.S. Liu, X. Lu, and M. Yin Co-polypeptides of 3,4-dihydroxyphenylalanine and l-lysine to mimic marine adhesive protein Biomaterials 28 2007 3456 3468 (Pubitemid 46726631)
    • (2007) Biomaterials , vol.28 , Issue.23 , pp. 3456-3468
    • Wang, J.1    Liu, C.2    Lu, X.3    Yin, M.4
  • 160
    • 61549097511 scopus 로고    scopus 로고
    • Development of mussel adhesive polypeptide mimics coating for in-situ inducing re-endothelialization of intravascular stent devices
    • M. Yin, Y. Yuan, C.S. Liu, and J. Wang Development of mussel adhesive polypeptide mimics coating for in-situ inducing re-endothelialization of intravascular stent devices Biomaterials 30 2009 2764 2773
    • (2009) Biomaterials , vol.30 , pp. 2764-2773
    • Yin, M.1    Yuan, Y.2    Liu, C.S.3    Wang, J.4
  • 162
    • 66749187252 scopus 로고    scopus 로고
    • Enhanced reversible adhesion of dopamine methacrylamide-coated elastomer microfibrillar structures under wet conditions
    • P. Glass, H.Y. Chung, N.R. Washburn, and M. Sitti Enhanced reversible adhesion of dopamine methacrylamide-coated elastomer microfibrillar structures under wet conditions Langmuir 25 2009 6607 6612
    • (2009) Langmuir , vol.25 , pp. 6607-6612
    • Glass, P.1    Chung, H.Y.2    Washburn, N.R.3    Sitti, M.4
  • 163
    • 0037427331 scopus 로고    scopus 로고
    • Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces
    • DOI 10.1021/ja0284963
    • J.L. Dalsin, B.H. Hu, B.P. Lee, and P.B. Messersmith Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces J Am Chem Soc 125 2003 4253 4258 (Pubitemid 36512318)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.14 , pp. 4253-4258
    • Dalsin, J.L.1    Hu, B.-H.2    Lee, B.P.3    Messersmith, P.B.4
  • 164
    • 73249116006 scopus 로고    scopus 로고
    • Functionalizable and ultra-low fouling zwitterionic surfaces via adhesive mussel mimetic linkages
    • C.L. Gao, G.Z. Li, H. Xue, W. Yang, F.B. Zhang, and S.Y. Jiang Functionalizable and ultra-low fouling zwitterionic surfaces via adhesive mussel mimetic linkages Biomaterials 31 2010 1486 1492
    • (2010) Biomaterials , vol.31 , pp. 1486-1492
    • Gao, C.L.1    Li, G.Z.2    Xue, H.3    Yang, W.4    Zhang, F.B.5    Jiang, S.Y.6
  • 167
    • 34250745855 scopus 로고    scopus 로고
    • Simplified polymer mimics of cross-linking adhesive proteins
    • DOI 10.1021/ma0703002
    • G. Westwood, T.N. Horton, and J.J. Wilker Simplified polymer mimics of cross-linking adhesive proteins Macromolecules 40 2007 3960 3964 (Pubitemid 46953838)
    • (2007) Macromolecules , vol.40 , Issue.11 , pp. 3960-3964
    • Westwood, G.1    Horton, T.N.2    Wilker, J.J.3
  • 169
    • 4043089079 scopus 로고    scopus 로고
    • Dopamine as a robust anchor to immobilize functional molecules on the iron oxide shell of magnetic nanoparticles
    • DOI 10.1021/ja0464802
    • C. Xu, K. Xu, H. Gu, R. Zheng, H. Liu, X. Zhang, Z. Guo, and B. Xu Dopamine as a robust anchor to immobilize functional molecules on the iron oxide shell of magnetic nanoparticles J Am Chem Soc 126 2004 9938 9939 (Pubitemid 39079411)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.32 , pp. 9938-9939
    • Xu, C.1    Xu, K.2    Gu, H.3    Zheng, R.4    Liu, H.5    Zhang, X.6    Guo, Z.7    Xu, B.8
  • 170
    • 44149117460 scopus 로고    scopus 로고
    • Mimicking mussel adhesion to improve interfacial properties in composites
    • L.M. Hamming, X.W. Fan, P.B. Messersmith, and L.C. Brinson Mimicking mussel adhesion to improve interfacial properties in composites Compos Sci Technol 68 2008 2042 2048
    • (2008) Compos Sci Technol , vol.68 , pp. 2042-2048
    • Hamming, L.M.1    Fan, X.W.2    Messersmith, P.B.3    Brinson, L.C.4
  • 171
    • 70349392872 scopus 로고    scopus 로고
    • Norepinephrine: Material-independent, multifunctional surface modification reagent
    • S.M. Kang, J. Rho, I.S. Choi, P.B. Messersmith, and H. Lee Norepinephrine: material-independent, multifunctional surface modification reagent J Am Chem Soc 131 2009 13224 13225
    • (2009) J Am Chem Soc , vol.131 , pp. 13224-13225
    • Kang, S.M.1    Rho, J.2    Choi, I.S.3    Messersmith, P.B.4    Lee, H.5
  • 173
    • 35348945857 scopus 로고    scopus 로고
    • Mussel-inspired surface chemistry for multifunctional coatings
    • DOI 10.1126/science.1147241
    • H. Lee, S.M. Dellatore, W.M. Miller, and P.B. Messersmith Mussel-inspired surface chemistry for multifunctional coatings Science 318 2007 426 430 (Pubitemid 47614522)
    • (2007) Science , vol.318 , Issue.5849 , pp. 426-430
    • Lee, H.1    Dellatore, S.M.2    Miller, W.M.3    Messersmith, P.B.4
  • 174
    • 34447517407 scopus 로고    scopus 로고
    • A reversible wet/dry adhesive inspired by mussels and geckos
    • H. Lee, B.P. Lee, and P.B. Messersmith A reversible wet/dry adhesive inspired by mussels and geckos Nature 448 2007 U338 U341
    • (2007) Nature , vol.448
    • Lee, H.1    Lee, B.P.2    Messersmith, P.B.3
  • 175
    • 84856465441 scopus 로고    scopus 로고
    • Learning from nature: Synthesis and characterization of longitudinal polymer gradient materials inspired by mussel byssus threads
    • K.U. Claussen, R. Giesa, T. Scheibel, and H.W. Schmidt Learning from nature: synthesis and characterization of longitudinal polymer gradient materials inspired by mussel byssus threads Macromol Rapid Commun 33 2012 206 211
    • (2012) Macromol Rapid Commun , vol.33 , pp. 206-211
    • Claussen, K.U.1    Giesa, R.2    Scheibel, T.3    Schmidt, H.W.4
  • 177
    • 79958854439 scopus 로고    scopus 로고
    • Effects of interfacial redox in mussel adhesive protein films on mica
    • J. Yu, W. Wei, E. Danner, J.N. Israelachvili, and J.H. Waite Effects of interfacial redox in mussel adhesive protein films on mica Adv Mater 23 2011 2362 2366
    • (2011) Adv Mater , vol.23 , pp. 2362-2366
    • Yu, J.1    Wei, W.2    Danner, E.3    Israelachvili, J.N.4    Waite, J.H.5


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