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Volumn 28, Issue 24, 2007, Pages 3560-3568

Practical recombinant hybrid mussel bioadhesive fp-151

Author keywords

Bioadhesive; Cell adhesive; Escherichia coli; Fusion protein; Hybrid fp 151; Mussel adhesive protein

Indexed keywords

BIOADHESIVES; CELL ADHESIVES; FUSION PROTEINS; MUSSEL ADHESIVE PROTEINS;

EID: 34249307818     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2007.04.039     Document Type: Article
Times cited : (196)

References (34)
  • 1
    • 0022737072 scopus 로고
    • Adhesive protein from mussels: possibilities for dentistry, medicine, and industry
    • Dove J., and Sheridan P. Adhesive protein from mussels: possibilities for dentistry, medicine, and industry. J Am Dent Assoc 112 (1986) 879
    • (1986) J Am Dent Assoc , vol.112 , pp. 879
    • Dove, J.1    Sheridan, P.2
  • 3
    • 0024087251 scopus 로고
    • The use of adhesives in chondrocyte transplantation surgery: preliminary studies
    • Grande D.A., and Pitman M.I. The use of adhesives in chondrocyte transplantation surgery: preliminary studies. Bull Hospital JT Dis Otrhop Inst 48 (1988) 140-148
    • (1988) Bull Hospital JT Dis Otrhop Inst , vol.48 , pp. 140-148
    • Grande, D.A.1    Pitman, M.I.2
  • 4
    • 0003139123 scopus 로고
    • Adhesion in byssally attached bivalves
    • Waite J.H. Adhesion in byssally attached bivalves. Biol Rev 58 (1983) 209-231
    • (1983) Biol Rev , vol.58 , pp. 209-231
    • Waite, J.H.1
  • 5
    • 0001336813 scopus 로고
    • Characterization of a cystein-rich polyphenolic protein family from Mytilus edulis
    • Rzepecki L.M., Hansen K.M., and Waite J.H. Characterization of a cystein-rich polyphenolic protein family from Mytilus edulis. 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
  • 6
    • 0029166187 scopus 로고
    • Hydroxyarginine-containing polyphenolic proteins in the adhesive plaques of the marine mussel Mytilus edulis
    • Papov V.V., Diamond T.V., Biemann K., and Waite J.H. 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
  • 7
    • 0035814883 scopus 로고    scopus 로고
    • Polyphosphoprotein from the adhesive pads of Mytilus edulis
    • Waite J.H., and Qin X.X. Polyphosphoprotein from the adhesive pads of Mytilus edulis. Biochemistry 40 (2001) 2887-2893
    • (2001) Biochemistry , vol.40 , pp. 2887-2893
    • Waite, J.H.1    Qin, X.X.2
  • 8
    • 0021099316 scopus 로고
    • Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis
    • Waite J.H. Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis. J Biol Chem 258 (1983) 2911-2915
    • (1983) J Biol Chem , vol.258 , pp. 2911-2915
    • Waite, J.H.1
  • 9
    • 0024863703 scopus 로고
    • Adhesives from marine mussels
    • Hemingway R.W., Conner A.H., and Branham S.J. (Eds), American Chemical Society, Washington, DC
    • Benedict C.V., and Picciano P.T. Adhesives from marine mussels. In: Hemingway R.W., Conner A.H., and Branham S.J. (Eds). Adhesives from renewable resources. No. 385 (1989), American Chemical Society, Washington, DC 465-483
    • (1989) Adhesives from renewable resources. No. 385 , pp. 465-483
    • Benedict, C.V.1    Picciano, P.T.2
  • 11
    • 34249301518 scopus 로고
    • Development of a microbial system for production of mussel adhesive protein
    • Hemingway R.W., Conner A.H., and Branham S.J. (Eds), American Chemical Society, Washington, DC
    • Strausberg R.L., Andersen D.M., Filpula D.R., Finkelman M., Link R.P., McCandliss R., et al. Development of a microbial system for production of mussel adhesive protein. In: Hemingway R.W., Conner A.H., and Branham S.J. (Eds). Adhesives from renewable resources. No. 385 (1989), American Chemical Society, Washington, DC 452-464
    • (1989) Adhesives from renewable resources. No. 385 , pp. 452-464
    • Strausberg, R.L.1    Andersen, D.M.2    Filpula, D.R.3    Finkelman, M.4    Link, R.P.5    McCandliss, R.6
  • 12
    • 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
    • Kitamura M., Kawakami K., Nakamura N., Tsumoto K., Uchiyama H., Ueda Y., et al. 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 Part A: Polym Chem 37 (1999) 729-736
    • (1999) J Polym Sci Part A: 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
  • 13
    • 0033080860 scopus 로고    scopus 로고
    • Cultured mussel foot cells expressing byssal protein genes
    • Takeuchi Y., Inoue K., Miki D., Odo S., and Harayama S. Cultured mussel foot cells expressing byssal protein genes. J Exp Zool 283 (1999) 131-136
    • (1999) J Exp Zool , vol.283 , pp. 131-136
    • Takeuchi, Y.1    Inoue, K.2    Miki, D.3    Odo, S.4    Harayama, S.5
  • 14
    • 0032120933 scopus 로고    scopus 로고
    • Synthetic polypeptide mimics of marine adhesives
    • Yu M.E., and Deming T.J. Synthetic polypeptide mimics of marine adhesives. Macromolecules 31 (1998) 4739-4745
    • (1998) Macromolecules , vol.31 , pp. 4739-4745
    • Yu, M.E.1    Deming, T.J.2
  • 15
    • 0033597620 scopus 로고    scopus 로고
    • Role of l-3,4-dihydroxyphenylalanine in mussel adhesive proteins
    • Yu M.E., Hwang J.Y., and Deming T.J. Role of l-3,4-dihydroxyphenylalanine in mussel adhesive proteins. J Am Chem Soc 121 (1999) 5825-5826
    • (1999) J Am Chem Soc , vol.121 , pp. 5825-5826
    • Yu, M.E.1    Hwang, J.Y.2    Deming, T.J.3
  • 16
    • 0033893993 scopus 로고    scopus 로고
    • Model polypeptide of mussel adhesive protein. I. Synthesis and adhesive studies of sequential polypeptides (X-Tyr-Lys)(n) and (Y-Lys)(n)
    • Tatehata H., Mochizuki A., Kawashima T., Yamashita S., and Yamamoto H. Model polypeptide of mussel adhesive protein. I. Synthesis and adhesive studies of sequential polypeptides (X-Tyr-Lys)(n) and (Y-Lys)(n). J Appl Polym Sci 76 (2000) 929-937
    • (2000) J Appl Polym Sci , vol.76 , pp. 929-937
    • Tatehata, H.1    Mochizuki, A.2    Kawashima, T.3    Yamashita, S.4    Yamamoto, H.5
  • 17
    • 2942532196 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli
    • Hwang D.S., Yoo H.J., Jun J.H., Moon W.K., and Cha H.J. Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli. Appl Environ Microbiol 70 (2004) 3352-3359
    • (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
  • 18
    • 20144366711 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli
    • Hwang D.S., Gim Y., and Cha H.J. Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli. Biotechnol Prog 21 (2005) 965-970
    • (2005) Biotechnol Prog , vol.21 , pp. 965-970
    • Hwang, D.S.1    Gim, Y.2    Cha, H.J.3
  • 19
    • 0036498663 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of peptidyl 3,4-dihydroxyphenylalanine for structure-activity relationships in marine invertebrate polypeptides
    • Taylor S.W. Chemoenzymatic synthesis of peptidyl 3,4-dihydroxyphenylalanine for structure-activity relationships in marine invertebrate polypeptides. Anal Biochem 302 (2002) 70-74
    • (2002) Anal Biochem , vol.302 , pp. 70-74
    • Taylor, S.W.1
  • 20
    • 0021494574 scopus 로고
    • Determinatnion of (catecholato)-borate complex using difference spectrometry
    • Waite J.H. Determinatnion of (catecholato)-borate complex using difference spectrometry. Anal Chem 56 (1984) 1935-1939
    • (1984) Anal Chem , vol.56 , pp. 1935-1939
    • Waite, J.H.1
  • 21
    • 84951279351 scopus 로고
    • Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung
    • Sauerbrey G. Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung. Z Phys 155 (1959) 206
    • (1959) Z Phys , vol.155 , pp. 206
    • Sauerbrey, G.1
  • 23
    • 12044257837 scopus 로고
    • Direct measurement of colloidal forces using an atomic force microscope
    • Ducker W.A., Senden T.J., and Pashley R.M. Direct measurement of colloidal forces using an atomic force microscope. Nature 353 (1991) 239-241
    • (1991) Nature , vol.353 , pp. 239-241
    • Ducker, W.A.1    Senden, T.J.2    Pashley, R.M.3
  • 24
    • 0036861435 scopus 로고    scopus 로고
    • Facile and statistical optimization of transfection conditions for secretion of foreign proteins from insect Drosophila S2 cells using green fluorescent protein reporter
    • Shin H.S., and Cha H.J. Facile and statistical optimization of transfection conditions for secretion of foreign proteins from insect Drosophila S2 cells using green fluorescent protein reporter. Biotechnol Prog 18 (2002) 1187-1194
    • (2002) Biotechnol Prog , vol.18 , pp. 1187-1194
    • Shin, H.S.1    Cha, H.J.2
  • 25
    • 0029143664 scopus 로고
    • Precursors of quinone tanning-dopa-containing proteins
    • Academic Press, Inc., London
    • Waite J.H. Precursors of quinone tanning-dopa-containing proteins. Methods in enzymology vol. 258 (1995), Academic Press, Inc., London 1-20
    • (1995) Methods in enzymology , vol.258 , pp. 1-20
    • Waite, J.H.1
  • 26
    • 0022498770 scopus 로고
    • Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase
    • Marumo K., and Waite J.H. Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase. Biochim Biophys Acta 872 (1986) 98-103
    • (1986) Biochim Biophys Acta , vol.872 , pp. 98-103
    • Marumo, K.1    Waite, J.H.2
  • 27
    • 0038067927 scopus 로고    scopus 로고
    • Adhesion á la Moule
    • Waite J.H. Adhesion á la Moule. Integr Comp Biol 42 (2002) 1172-1180
    • (2002) Integr Comp Biol , vol.42 , pp. 1172-1180
    • Waite, J.H.1
  • 28
    • 0033856899 scopus 로고    scopus 로고
    • Tyrosinase-induced cross-linking of tyrosine-containing peptides investigated by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Jee J.G., Park S.J., and Kim H.J. Tyrosinase-induced cross-linking of tyrosine-containing peptides investigated by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun Mass Sp 14 (2000) 1563-1567
    • (2000) Rapid Commun Mass Sp , vol.14 , pp. 1563-1567
    • Jee, J.G.1    Park, S.J.2    Kim, H.J.3
  • 29
    • 0034060011 scopus 로고    scopus 로고
    • Surface-enhanced Raman spectroscopy of DOPA-containing peptides related to adhesive protein of marine mussel, Mytilus edulis
    • Akemi Ooka A., and Garrell R.L. Surface-enhanced Raman spectroscopy of DOPA-containing peptides related to adhesive protein of marine mussel, Mytilus edulis. Biopolymers 57 (2000) 92-102
    • (2000) Biopolymers , vol.57 , pp. 92-102
    • Akemi Ooka, A.1    Garrell, R.L.2
  • 30
    • 0037791563 scopus 로고    scopus 로고
    • Improvement of the biocompatibility of alginate/poly-l-lysine/alginate microcapsules by the use of epimerized alginate as a coating
    • King A., Strand B., Rokstad A.M., Kulseng B., Andersson A., Skjak-Braek G., et al. Improvement of the biocompatibility of alginate/poly-l-lysine/alginate microcapsules by the use of epimerized alginate as a coating. J Biomed Mater Res A 64 (2003) 533-539
    • (2003) J Biomed Mater Res A , vol.64 , pp. 533-539
    • King, A.1    Strand, B.2    Rokstad, A.M.3    Kulseng, B.4    Andersson, A.5    Skjak-Braek, G.6
  • 32
    • 0042164323 scopus 로고    scopus 로고
    • Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase
    • Russo G.L., De Nisco E., Fiore G., Di Donato P., d'Ischia M., and Palumbo A. Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase. Biochem Biophys Res Commun 308 (2003) 293-299
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 293-299
    • Russo, G.L.1    De Nisco, E.2    Fiore, G.3    Di Donato, P.4    d'Ischia, M.5    Palumbo, A.6
  • 33
    • 2342517486 scopus 로고    scopus 로고
    • Cross-linking the protein precursor of marine mussel adhesives: bulk measurements and reagents for curing
    • Monahan J., and Wilker J.J. Cross-linking the protein precursor of marine mussel adhesives: bulk measurements and reagents for curing. Langmuir 20 (2004) 3724-3729
    • (2004) Langmuir , vol.20 , pp. 3724-3729
    • Monahan, J.1    Wilker, J.J.2
  • 34


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.