메뉴 건너뛰기




Volumn 14, Issue 4, 2003, Pages 748-755

Enzymatic modification of self-assembled peptide structures with tissue transglutaminase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AZO DYES; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; DRUG DELIVERY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MASS SPECTROMETRY; MEDICAL APPLICATIONS; TISSUE; TISSUE ENGINEERING;

EID: 0037778904     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc034017t     Document Type: Article
Times cited : (148)

References (52)
  • 1
    • 0036139571 scopus 로고    scopus 로고
    • Novel peptide-based biomaterial scaffolds for tissue engineering
    • Holmes, T. C. (2002) Novel peptide-based biomaterial scaffolds for tissue engineering. Trends Biotechnol. 20, 16-21.
    • (2002) Trends Biotechnol. , vol.20 , pp. 16-21
    • Holmes, T.C.1
  • 2
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes, T. C., de Lacalle, S., Su, X., Liu, G. S., Rich, A., and Zhang, S. G. (2000) Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc. Nat. Acad. Sci. U.S.A. 97, 6728-6733.
    • (2000) Proc. Nat. Acad. Sci. U.S.A. , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    De Lacalle, S.2    Su, X.3    Liu, G.S.4    Rich, A.5    Zhang, S.G.6
  • 3
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
    • Kisiday, J., Jin, M., Kurz, B., Hung, H., Semino, C., Zhang, S., and Grodzinsky, A. J. (2002) Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair. Proc. Nat. Acad. Sci. U.S.A. 99, 9996-10001.
    • (2002) Proc. Nat. Acad. Sci. U.S.A. , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Kurz, B.3    Hung, H.4    Semino, C.5    Zhang, S.6    Grodzinsky, A.J.7
  • 4
    • 0029411957 scopus 로고
    • Self-complementary oligopeptide matrices support mammalian cell attachment
    • Zhang, S. G., Holmes, T. C., DiPersio, C. M., Hynes, R. O., Su, X., and Rich, A. (1995) Self-complementary oligopeptide matrices support mammalian cell attachment. Biomaterials 16, 1385-1393.
    • (1995) Biomaterials , vol.16 , pp. 1385-1393
    • Zhang, S.G.1    Holmes, T.C.2    DiPersio, C.M.3    Hynes, R.O.4    Su, X.5    Rich, A.6
  • 5
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink, J. D., Beniash, E., and Stupp, S. I. (2001) Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 294, 1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 6
    • 0031603860 scopus 로고    scopus 로고
    • Proteinlike molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction
    • Fields, G. B., Lauer, J. L., Dori, Y., Forns, P., Yu, Y. C., and Tirrell, M. (1998) Proteinlike molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction. Biopolymers 47, 143-151.
    • (1998) Biopolymers , vol.47 , pp. 143-151
    • Fields, G.B.1    Lauer, J.L.2    Dori, Y.3    Forns, P.4    Yu, Y.C.5    Tirrell, M.6
  • 8
    • 0037028657 scopus 로고    scopus 로고
    • Nature's complex copolymers: Engineering design of oligopeptide materials
    • Caplan, M. R., and Lauffenburger, D. A. (2002) Nature's complex copolymers: Engineering design of oligopeptide materials. Ind. Eng. Chem. Res. 41, 403-412.
    • (2002) Ind. Eng. Chem. Res. , vol.41 , pp. 403-412
    • Caplan, M.R.1    Lauffenburger, D.A.2
  • 9
    • 0032541038 scopus 로고    scopus 로고
    • Reversible hydrogels from self-assembling artificial proteins
    • Petka, W. A., Harden, J. L., McGrath, K. P., Wirtz, D., and Tirrell, D. A. (1998) Reversible hydrogels from self-assembling artificial proteins. Science 281, 389-392.
    • (1998) Science , vol.281 , pp. 389-392
    • Petka, W.A.1    Harden, J.L.2    McGrath, K.P.3    Wirtz, D.4    Tirrell, D.A.5
  • 10
    • 0030934379 scopus 로고    scopus 로고
    • Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes
    • Aggeli, A., Bell, M., Boden, N., Keen, J. N., Knowles, P. F., McLeish, T. C. B., Pitkeathly, M., and Radford, S. E. (1997) Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes. Nature 386, 259-262.
    • (1997) Nature , vol.386 , pp. 259-262
    • Aggeli, A.1    Bell, M.2    Boden, N.3    Keen, J.N.4    Knowles, P.F.5    McLeish, T.C.B.6    Pitkeathly, M.7    Radford, S.E.8
  • 11
    • 0037132592 scopus 로고    scopus 로고
    • Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide
    • Schneider, J. P., Pochan, D. J., Ozbas, B., Rajagopal, K., Pakstis, L., and Kretsinger, J. (2002) Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide. J. Am. Chem. Soc. 124 15030-15037.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15030-15037
    • Schneider, J.P.1    Pochan, D.J.2    Ozbas, B.3    Rajagopal, K.4    Pakstis, L.5    Kretsinger, J.6
  • 12
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • Zhang, S. G., Holmes, T., Lockshin, C., and Rich, A. (1993) Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc. Nat. Acad. Sci. U.S.A. 90, 3334-3338.
    • (1993) Proc. Nat. Acad. Sci. U.S.A. , vol.90 , pp. 3334-3338
    • Zhang, S.G.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 13
    • 0034616839 scopus 로고    scopus 로고
    • Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid formation and materials science
    • Lashuel, H. A., LaBrenz, S. R., Woo, L., Serpell, L. C., and Kelly, J. W. (2000) Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid formation and materials science. J. Am. Chem. Soc. 122, 5262-5277.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5262-5277
    • Lashuel, H.A.1    LaBrenz, S.R.2    Woo, L.3    Serpell, L.C.4    Kelly, J.W.5
  • 14
    • 0034722985 scopus 로고    scopus 로고
    • Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures
    • MacPhee, C. E., and Dobson, C. M. (2000) Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures. J. Am. Chem. Soc. 122, 12707-12713.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12707-12713
    • MacPhee, C.E.1    Dobson, C.M.2
  • 16
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • West, M. W., and Hecht, M. H. (1995) Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Sci. 4, 2032-2039.
    • (1995) Protein Sci. , vol.4 , pp. 2032-2039
    • West, M.W.1    Hecht, M.H.2
  • 17
    • 0016715114 scopus 로고
    • Beta structures of alternating polypeptides and their possible prebiotic significance
    • Brack, A., and Orgel, L. E. (1975) Beta structures of alternating polypeptides and their possible prebiotic significance. Nature 256, 383-387.
    • (1975) Nature , vol.256 , pp. 383-387
    • Brack, A.1    Orgel, L.E.2
  • 18
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino-acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong, H. Y., Buckwalter, B. L., Shieh, H. M., and Hecht, M. H. (1995) Periodicity of Polar and Nonpolar Amino-Acids Is the Major Determinant of Secondary Structure in Self-Assembling Oligomeric Peptides. Proc. Nat. Acad. Sci. U.S.A. 92, 6349-6353.
    • (1995) Proc. Nat. Acad. Sci. U.S.A. , vol.92 , pp. 6349-6353
    • Xiong, H.Y.1    Buckwalter, B.L.2    Shieh, H.M.3    Hecht, M.H.4
  • 19
    • 0034571041 scopus 로고    scopus 로고
    • Self-assembly of a beta-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction
    • Caplan, M. R., Moore, P. N., Zhang, S., Kamm, R. D., and Lauffenburger, D. A. (2000) Self-assembly of a beta-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction. Biomacromolecules 1, 627-631.
    • (2000) Biomacromolecules , vol.1 , pp. 627-631
    • Caplan, M.R.1    Moore, P.N.2    Zhang, S.3    Kamm, R.D.4    Lauffenburger, D.A.5
  • 20
    • 0035284541 scopus 로고    scopus 로고
    • Tethered-TGF-beta increases extracellular matrix production of vascular smooth muscle cells
    • Mann, B. K., Schmedlen, R. H., and West, J. L. (2001) Tethered-TGF-beta increases extracellular matrix production of vascular smooth muscle cells. Biomaterials 22, 439-444.
    • (2001) Biomaterials , vol.22 , pp. 439-444
    • Mann, B.K.1    Schmedlen, R.H.2    West, J.L.3
  • 21
    • 0029791838 scopus 로고    scopus 로고
    • Tethered epidermal growth factor as a paradigm for growth factor-induced stimulation from the solid phase
    • Kuhl, P. R., and Griffith-Cima, L. G. (1996) Tethered epidermal growth factor as a paradigm for growth factor-induced stimulation from the solid phase. Nat. Med. 2, 1022-1027.
    • (1996) Nat. Med. , vol.2 , pp. 1022-1027
    • Kuhl, P.R.1    Griffith-Cima, L.G.2
  • 22
    • 0032521332 scopus 로고    scopus 로고
    • Improved local delivery of TGF-beta 2 by binding to injectable fibrillar collagen via difunctional polyethylene glycol
    • Bentz, H., Schroeder, J. A., and Estridge, T. D. (1998) Improved local delivery of TGF-beta 2 by binding to injectable fibrillar collagen via difunctional polyethylene glycol. J. Biomed. Mater. Res. 39, 539-548.
    • (1998) J. Biomed. Mater. Res. , vol.39 , pp. 539-548
    • Bentz, H.1    Schroeder, J.A.2    Estridge, T.D.3
  • 23
    • 0002766824 scopus 로고
    • Endothelial cell-selective materials for tissue engineering in the vascular graft via a new receptor
    • Hubbell, J. A., Massia, S. P., Desai, N. P., and Drumheller, P. D. (1991) Endothelial Cell-Selective Materials for Tissue Engineering in the Vascular Graft Via a New Receptor. Bio/Technology 9, 568-572.
    • (1991) Bio/Technology , vol.9 , pp. 568-572
    • Hubbell, J.A.1    Massia, S.P.2    Desai, N.P.3    Drumheller, P.D.4
  • 24
    • 0025087925 scopus 로고
    • Covalently attached GRGD on polymer surfaces promotes biospecific adhesion of mammalian-cells
    • Massia, S. P., and Hubbell, J. A. (1990) Covalently Attached GRGD on Polymer Surfaces Promotes Biospecific Adhesion of Mammalian-Cells. Ann. N. Y. Acad. Sci. 589, 261-270.
    • (1990) Ann. N. Y. Acad. Sci. , vol.589 , pp. 261-270
    • Massia, S.P.1    Hubbell, J.A.2
  • 25
    • 8244221666 scopus 로고    scopus 로고
    • Characterization and development of RGD-peptide-modified poly(lactic acid-co-lysine) as an interactive, resorbable biomaterial
    • Cook, A. D., Hrkach, J. S., Gao, N. N., Johnson, I. M., Pajvani, U. B., Cannizzaro, S. M., and Langer, R. (1997) Characterization and development of RGD-peptide-modified poly(lactic acid-co-lysine) as an interactive, resorbable biomaterial. J. Biomed. Mater. Res. 35, 513-523.
    • (1997) J. Biomed. Mater. Res. , vol.35 , pp. 513-523
    • Cook, A.D.1    Hrkach, J.S.2    Gao, N.N.3    Johnson, I.M.4    Pajvani, U.B.5    Cannizzaro, S.M.6    Langer, R.7
  • 26
    • 0033997601 scopus 로고    scopus 로고
    • Development of fibrin derivatives for controlled release of heparin-binding growth factors
    • Sakiyama-Elbert, S. E., and Hubbell, J. A. (2000) Development of fibrin derivatives for controlled release of heparin-binding growth factors. J. Controlled Release 65, 389-402.
    • (2000) J. Controlled Release , vol.65 , pp. 389-402
    • Sakiyama-Elbert, S.E.1    Hubbell, J.A.2
  • 27
    • 0032940534 scopus 로고    scopus 로고
    • Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa
    • Schense, J. C., and Hubbell, J. A. (1999) Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa. Bioconjugate Chem. 10, 75-81.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 75-81
    • Schense, J.C.1    Hubbell, J.A.2
  • 28
    • 0034629303 scopus 로고    scopus 로고
    • Three-dimensional migration of neurites is mediated by adhesion site density and affinity
    • Schense, J. C., and Hubbell, J. A. (2000) Three-dimensional migration of neurites is mediated by adhesion site density and affinity. J. Biol. Chem. 275, 6813-6818.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6813-6818
    • Schense, J.C.1    Hubbell, J.A.2
  • 30
    • 0001146033 scopus 로고    scopus 로고
    • Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid beta-peptide
    • Jao, S. C., Ma, K., Talafous, J., Orlando, R., and Zagorski, M. G. (1997) Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid beta-peptide. Amyloid 4, 240-252.
    • (1997) Amyloid , vol.4 , pp. 240-252
    • Jao, S.C.1    Ma, K.2    Talafous, J.3    Orlando, R.4    Zagorski, M.G.5
  • 34
    • 0036000156 scopus 로고    scopus 로고
    • Formation of fibrinogen-based hydrogels using phototriggerable diplasmalogen liposomes
    • Zhang, Z. Y., Shum, P., Yates, M., Messersmith, P. B., and Thompson, D. H. (2002) Formation of fibrinogen-based hydrogels using phototriggerable diplasmalogen liposomes. Bioconjugate Chem. 13, 640-646.
    • (2002) Bioconjugate Chem. , vol.13 , pp. 640-646
    • Zhang, Z.Y.1    Shum, P.2    Yates, M.3    Messersmith, P.B.4    Thompson, D.H.5
  • 35
    • 0032538447 scopus 로고    scopus 로고
    • Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases - Evidence for transglutaminase-catalyzed cross-linking to fibrin
    • Valnickova, Z., and Enghild, J. J. (1998) Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases - Evidence for transglutaminase-catalyzed cross-linking to fibrin. J. Biol. Chem. 273, 27220-27224.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27220-27224
    • Valnickova, Z.1    Enghild, J.J.2
  • 36
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson, W. C. (1988) Secondary structure of proteins through circular dichroism spectroscopy. Annu. Rev. Biophys. Biophys. Chem. 17, 145-166.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 145-166
    • Johnson, W.C.1
  • 37
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D. (1969) Computed Circular Dichroism Spectra for Evaluation of Protein Conformation. Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 38
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris, P. I., and Chapman, D. (1995) The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers 37, 251-263.
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 39
    • 0033855775 scopus 로고    scopus 로고
    • Review: Model peptides and the physicochemical approach to beta-amyloids
    • Lynn, D. G., and Meredith, S. C. (2000) Review: Model peptides and the physicochemical approach to beta-amyloids. J. Struct. Biol. 130, 153-173.
    • (2000) J. Struct. Biol. , vol.130 , pp. 153-173
    • Lynn, D.G.1    Meredith, S.C.2
  • 40
    • 0000590549 scopus 로고    scopus 로고
    • Left-handed helical ribbon intermediates in the self-assembly of a beta-sheet peptide
    • Marini, D. M., Hwang, W., Lauffenburger, D. A., Zhang, S. G., and Kamm, R. D. (2002) Left-handed helical ribbon intermediates in the self-assembly of a beta-sheet peptide. Nano Lett. 2, 295-299.
    • (2002) Nano Lett. , vol.2 , pp. 295-299
    • Marini, D.M.1    Hwang, W.2    Lauffenburger, D.A.3    Zhang, S.G.4    Kamm, R.D.5
  • 41
    • 0017735718 scopus 로고
    • Amine binding-sites in acyl intermediates of transglutaminases - Human-blood plasma enzyme (activated coagulation factor-XIII) and guinea-pig liver-enzyme
    • Gross, M., Whetzel, N. K., and Folk, J. E. (1977) Amine Binding-Sites in Acyl Intermediates of Transglutaminases - Human-Blood Plasma Enzyme (Activated Coagulation Factor-XIII) and Guinea-Pig Liver-Enzyme. J. Biol. Chem. 252, 3752-3759.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3752-3759
    • Gross, M.1    Whetzel, N.K.2    Folk, J.E.3
  • 43
    • 0035836519 scopus 로고    scopus 로고
    • Posttranslational modifications of microfibril associated glycoprotein-1 (MAGP-1)
    • Trask, B. C., Broekelmann, T., Ritty, T. M., Trask, T. M., Tisdale, C., and Mecham, R. P. (2001) Posttranslational modifications of microfibril associated glycoprotein-1 (MAGP-1). Biochemistry 40, 4372-80.
    • (2001) Biochemistry , vol.40 , pp. 4372-4380
    • Trask, B.C.1    Broekelmann, T.2    Ritty, T.M.3    Trask, T.M.4    Tisdale, C.5    Mecham, R.P.6
  • 44
    • 1842845084 scopus 로고    scopus 로고
    • Effects of systematic variation of amino acid sequence on the mechanical properties of a self-assembling, oligopeptide biomaterial
    • Caplan, M. R., Schwartzfarb, E. M., Zhang, S. G., Kamm, R. D., and Lauffenburger, D. A. (2002) Effects of systematic variation of amino acid sequence on the mechanical properties of a self-assembling, oligopeptide biomaterial. J. Biomater. Sci. Polym. Ed. 13, 225-236.
    • (2002) J. Biomater. Sci. Polym. Ed. , vol.13 , pp. 225-236
    • Caplan, M.R.1    Schwartzfarb, E.M.2    Zhang, S.G.3    Kamm, R.D.4    Lauffenburger, D.A.5
  • 45
    • 0036027555 scopus 로고    scopus 로고
    • Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence
    • Caplan, M. R., Schwartzfarb, E. M., Zhang, S. G., Kamm, R. D., and Lauffenburger, D. A. (2002) Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence. Biomaterials 23, 219-227.
    • (2002) Biomaterials , vol.23 , pp. 219-227
    • Caplan, M.R.1    Schwartzfarb, E.M.2    Zhang, S.G.3    Kamm, R.D.4    Lauffenburger, D.A.5
  • 46
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • Kahlem, P., Terre, C., Green, H., and Djian, P. (1996) Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system. Proc. Nat. Acad. Sci. U.S.A. 93, 14580-5.
    • (1996) Proc. Nat. Acad. Sci. U.S.A. , vol.93 , pp. 14580-14585
    • Kahlem, P.1    Terre, C.2    Green, H.3    Djian, P.4
  • 48
    • 0028298620 scopus 로고
    • Transglutaminase facilitates the formation of polymers of the beta-amyloid peptide
    • Dudek, S. M., and Johnson, G. V. W. (1994) Transglutaminase Facilitates the Formation of Polymers of the Beta-Amyloid Peptide. Brain Res. 651, 129-133.
    • (1994) Brain Res. , vol.651 , pp. 129-133
    • Dudek, S.M.1    Johnson, G.V.W.2
  • 49
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H. Y., and Orr, H. T. (2000) Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23, 217-47.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 50
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo, E. H., Lansbury, P. T., and Kelly, J. W. (1999) Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Nat. Acad. Sci. U.S.A. 96, 9989-90.
    • (1999) Proc. Nat. Acad. Sci. U.S.A. , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 51
    • 0026338017 scopus 로고
    • Transglutaminases - Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S., Birckbichler, P. J., and Rice, R. H. (1991) Transglutaminases - Multifunctional Cross-Linking Enzymes That Stabilize Tissues. FASEB J. 5, 3071-3077.
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 52
    • 0033047616 scopus 로고    scopus 로고
    • Covalent capture and stabilization of cylindrical β-sheet peptide assemblies
    • Clark, T. D., Kobayashi, K., and Ghadiri, M. R. (1999) Covalent capture and stabilization of cylindrical β-sheet peptide assemblies. Chem. Eur. J. 5, 782-792.
    • (1999) Chem. Eur. J. , vol.5 , pp. 782-792
    • Clark, T.D.1    Kobayashi, K.2    Ghadiri, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.