메뉴 건너뛰기




Volumn 28, Issue 35, 2007, Pages 5215-5224

Facile coupling of synthetic peptides and peptide-polymer conjugates to cartilage via transglutaminase enzyme

Author keywords

Cartilage; Conjugation; Peptide; Polymer; Surface; Transglutaminase

Indexed keywords

BIOMOLECULES; CARTILAGE; CATALYST ACTIVITY; COLLAGEN; COVALENT BONDS; ENZYME ACTIVITY; TISSUE ENGINEERING;

EID: 34948839382     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2007.08.026     Document Type: Article
Times cited : (33)

References (77)
  • 1
    • 0031568914 scopus 로고    scopus 로고
    • Polymeric endoluminal gel paving: hydrogel systems for local barrier creation and site-specific drug delivery
    • Slepian M.J., and Hubbell J.A. Polymeric endoluminal gel paving: hydrogel systems for local barrier creation and site-specific drug delivery. Adv Drug Delivery Rev 24 (1997) 11-30
    • (1997) Adv Drug Delivery Rev , vol.24 , pp. 11-30
    • Slepian, M.J.1    Hubbell, J.A.2
  • 2
    • 0032188875 scopus 로고    scopus 로고
    • Reduction of fibrous adhesion formation by a copolymer possessing an affinity for anionic surfaces
    • Elbert D., and Hubbell J. Reduction of fibrous adhesion formation by a copolymer possessing an affinity for anionic surfaces. J Biomater Res 42 (1998) 55-65
    • (1998) J Biomater Res , vol.42 , pp. 55-65
    • Elbert, D.1    Hubbell, J.2
  • 3
    • 0037086736 scopus 로고    scopus 로고
    • Sterically blocking adhesion of cells to biological surfaces with a surface-active copolymer containing poly(ethylene glycol) and phenylboronic acid
    • Winblade N., Schmokel H., Baumann M., Hoffman A., and Hubbell J. Sterically blocking adhesion of cells to biological surfaces with a surface-active copolymer containing poly(ethylene glycol) and phenylboronic acid. J Biomed Mater Res 59 (2002) 618-631
    • (2002) J Biomed Mater Res , vol.59 , pp. 618-631
    • Winblade, N.1    Schmokel, H.2    Baumann, M.3    Hoffman, A.4    Hubbell, J.5
  • 4
    • 0034574053 scopus 로고    scopus 로고
    • Blocking adhesion to cell and tissue surfaces by the chemisorption of a poly-l-lysine-graft-(poly(ethylene glycol): phenylboronic acid) copolymer
    • Winblade N., Nikolic I., Hoffman A., and Hubbell J. Blocking adhesion to cell and tissue surfaces by the chemisorption of a poly-l-lysine-graft-(poly(ethylene glycol): phenylboronic acid) copolymer. Biomacromolecules 1 (2000) 523-533
    • (2000) Biomacromolecules , vol.1 , pp. 523-533
    • Winblade, N.1    Nikolic, I.2    Hoffman, A.3    Hubbell, J.4
  • 5
    • 0032659433 scopus 로고    scopus 로고
    • Thin polymer layers formed by polyelectrolyte multilayer techniques on biological surfaces
    • Elbert D.L., Herbert C.B., and Hubbell J.A. Thin polymer layers formed by polyelectrolyte multilayer techniques on biological surfaces. Langmuir 15 (1999) 5355-5362
    • (1999) Langmuir , vol.15 , pp. 5355-5362
    • Elbert, D.L.1    Herbert, C.B.2    Hubbell, J.A.3
  • 6
    • 0038208277 scopus 로고    scopus 로고
    • Nanocoatings onto arteries via layer-by-layer deposition: toward the in vivo repair of damaged blood vessels
    • Thierry B., Winnik F., Merhi Y., and Tabrizian M. Nanocoatings onto arteries via layer-by-layer deposition: toward the in vivo repair of damaged blood vessels. J Am Chem Soc 125 (2003) 7494-7495
    • (2003) J Am Chem Soc , vol.125 , pp. 7494-7495
    • Thierry, B.1    Winnik, F.2    Merhi, Y.3    Tabrizian, M.4
  • 7
    • 33749679216 scopus 로고    scopus 로고
    • Multilayer nanoencapsulation. New approach for immune protection of human pancreatic islets
    • Krol S., del Guerra S., Grupillo M., Diaspro A., Gliozzi A., and Marchetti P. Multilayer nanoencapsulation. New approach for immune protection of human pancreatic islets. Nanoletters 6 (2006) 1933-1939
    • (2006) Nanoletters , vol.6 , pp. 1933-1939
    • Krol, S.1    del Guerra, S.2    Grupillo, M.3    Diaspro, A.4    Gliozzi, A.5    Marchetti, P.6
  • 8
    • 33750161411 scopus 로고    scopus 로고
    • Glycosaminoglycan-targeted fixation for improved bioprosthetic heart valve stabilization
    • Mercuri J., Lovekamp J., Simionescu D., and Vyavahare N. Glycosaminoglycan-targeted fixation for improved bioprosthetic heart valve stabilization. Biomaterials 28 (2007) 496-503
    • (2007) Biomaterials , vol.28 , pp. 496-503
    • Mercuri, J.1    Lovekamp, J.2    Simionescu, D.3    Vyavahare, N.4
  • 9
    • 0037114405 scopus 로고    scopus 로고
    • Optimization of monomethoxy-polyethylene glycol grafting on the pancreatic islet capsules
    • Lee D.Y., Yang K., Lee S., Chae S.Y., Kim K.W., Lee M.K., et al. Optimization of monomethoxy-polyethylene glycol grafting on the pancreatic islet capsules. J Biomed Mater Res 62 (2002) 372-377
    • (2002) J Biomed Mater Res , vol.62 , pp. 372-377
    • Lee, D.Y.1    Yang, K.2    Lee, S.3    Chae, S.Y.4    Kim, K.W.5    Lee, M.K.6
  • 10
    • 33749552389 scopus 로고    scopus 로고
    • Surface treatment of flexor tendon autographs with carbodiimide-derivatized hyaluronic acid. An in vivo canine model
    • Zhao C., Sun Y., Amadio P., Tanaka T., Ettema A., and An K. Surface treatment of flexor tendon autographs with carbodiimide-derivatized hyaluronic acid. An in vivo canine model. J Bone Joint Surg 88 (2006) 2181-2191
    • (2006) J Bone Joint Surg , vol.88 , pp. 2181-2191
    • Zhao, C.1    Sun, Y.2    Amadio, P.3    Tanaka, T.4    Ettema, A.5    An, K.6
  • 12
    • 0032144459 scopus 로고    scopus 로고
    • Creating molecular barriers to acute platelet deposition on damaged arteries with reactive polyethylene glycol
    • Deible C., Beckman E., Russell A., and Wagner W. Creating molecular barriers to acute platelet deposition on damaged arteries with reactive polyethylene glycol. J Biomater Res 41 (1998) 251-256
    • (1998) J Biomater Res , vol.41 , pp. 251-256
    • Deible, C.1    Beckman, E.2    Russell, A.3    Wagner, W.4
  • 13
    • 0035985001 scopus 로고    scopus 로고
    • Polyethylene glycol diisocyanate decreases platelet deposition after balloon injury of rabbit femoral arteries
    • Burchenal J., Deible C., Deglau T., Russell A., Beckman E., and Wagner W. Polyethylene glycol diisocyanate decreases platelet deposition after balloon injury of rabbit femoral arteries. J Thromb Thrombolysis 13 (2002) 27-33
    • (2002) J Thromb Thrombolysis , vol.13 , pp. 27-33
    • Burchenal, J.1    Deible, C.2    Deglau, T.3    Russell, A.4    Beckman, E.5    Wagner, W.6
  • 14
    • 0032891242 scopus 로고    scopus 로고
    • Molecular barriers to biomaterial thrombosis by modification of surface proteins with polyethylene glycol
    • Deible C.R., Petrosko P., Johnson P.C., Beckman E.J., Russell A.J., and Wagner W.R. Molecular barriers to biomaterial thrombosis by modification of surface proteins with polyethylene glycol. Biomaterials 20 (1999) 101-109
    • (1999) Biomaterials , vol.20 , pp. 101-109
    • Deible, C.R.1    Petrosko, P.2    Johnson, P.C.3    Beckman, E.J.4    Russell, A.J.5    Wagner, W.R.6
  • 17
    • 33645382628 scopus 로고    scopus 로고
    • An analysis of the integration between articular cartilage and nondegradable hydrogel using magnetic resonance imaging
    • Ramaswamy S., Wang D.A., Fishbein K.W., Elisseeff J.H., and Spencer R.G. An analysis of the integration between articular cartilage and nondegradable hydrogel using magnetic resonance imaging. J Biomed Mater Res Part B-Appl Biomater 77B (2006) 144-148
    • (2006) J Biomed Mater Res Part B-Appl Biomater , vol.77 B , pp. 144-148
    • Ramaswamy, S.1    Wang, D.A.2    Fishbein, K.W.3    Elisseeff, J.H.4    Spencer, R.G.5
  • 18
    • 34247863703 scopus 로고    scopus 로고
    • Multifunctional chondroitin sulphate for cartilage tissue-biomaterial integration
    • Wang D., Varghese S., Sharma B., Strehin I., Fermanian S., Gorham J., et al. Multifunctional chondroitin sulphate for cartilage tissue-biomaterial integration. Nature Mater 6 (2007) 385-392
    • (2007) Nature Mater , vol.6 , pp. 385-392
    • Wang, D.1    Varghese, S.2    Sharma, B.3    Strehin, I.4    Fermanian, S.5    Gorham, J.6
  • 19
    • 11444269099 scopus 로고    scopus 로고
    • Enhancing the tissue-biomaterial interface: Tissue-initiated integration of biomaterials
    • Wang D., Williams C., Yang F., and Elisseeff J. Enhancing the tissue-biomaterial interface: Tissue-initiated integration of biomaterials. Adv Funct Mater 14 (2004) 1152-1159
    • (2004) Adv Funct Mater , vol.14 , pp. 1152-1159
    • Wang, D.1    Williams, C.2    Yang, F.3    Elisseeff, J.4
  • 20
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., and Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 4 (2003) 140-156
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 21
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama K., Nio N., and Kikuchi Y. Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol 64 (2004) 447-454
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 24
    • 0034049521 scopus 로고    scopus 로고
    • Enzymatic incorporation of bioactive peptides into fibrin matrices enhances neurite extension
    • Schense J.C., Bloch J., Aebischer P., and Hubbell J.A. Enzymatic incorporation of bioactive peptides into fibrin matrices enhances neurite extension. Nat Biotechnol 18 (2000) 415-419
    • (2000) Nat Biotechnol , vol.18 , pp. 415-419
    • Schense, J.C.1    Bloch, J.2    Aebischer, P.3    Hubbell, J.A.4
  • 25
    • 0034753876 scopus 로고    scopus 로고
    • Molecular properties of fibrin-based matrices for promotion of angiogenesis in vitro
    • Hall H., Baechi T., and Hubbell J.A. Molecular properties of fibrin-based matrices for promotion of angiogenesis in vitro. Microvasc Res 62 (2001) 315-326
    • (2001) Microvasc Res , vol.62 , pp. 315-326
    • Hall, H.1    Baechi, T.2    Hubbell, J.A.3
  • 30
    • 0032940534 scopus 로고    scopus 로고
    • Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa
    • Schense J.C., and Hubbell J.A. Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa. Bioconjugate Chem 10 (1999) 75-81
    • (1999) Bioconjugate Chem , vol.10 , pp. 75-81
    • Schense, J.C.1    Hubbell, J.A.2
  • 31
    • 0032764946 scopus 로고    scopus 로고
    • Incorporation of heparin-binding peptides into fibrin gels enhances neurite extension: an example of designer matrices in tissue engineering
    • Sakiyama S.E., Schense J.C., and Hubbell J.A. Incorporation of heparin-binding peptides into fibrin gels enhances neurite extension: an example of designer matrices in tissue engineering. FASEB J 13 (1999) 2214-2224
    • (1999) FASEB J , vol.13 , pp. 2214-2224
    • Sakiyama, S.E.1    Schense, J.C.2    Hubbell, J.A.3
  • 33
    • 0036242363 scopus 로고    scopus 로고
    • In situ crosslinking of a biomimetic peptide-PEG hydrogel via thermally triggered activation of factor XIII
    • Sanborn T.J., Messersmith P.B., and Barron A.E. In situ crosslinking of a biomimetic peptide-PEG hydrogel via thermally triggered activation of factor XIII. Biomaterials 23 (2002) 2703-2710
    • (2002) Biomaterials , vol.23 , pp. 2703-2710
    • Sanborn, T.J.1    Messersmith, P.B.2    Barron, A.E.3
  • 34
    • 0031559845 scopus 로고    scopus 로고
    • Synthesis and characterization of enzymatically-cross-linked poly(ethylene glycol) hydrogels
    • Sperinde J.J., and Griffith L.G. Synthesis and characterization of enzymatically-cross-linked poly(ethylene glycol) hydrogels. Macromolecules 30 (1997) 5255-5264
    • (1997) Macromolecules , vol.30 , pp. 5255-5264
    • Sperinde, J.J.1    Griffith, L.G.2
  • 35
    • 0344443364 scopus 로고    scopus 로고
    • Rational design of transglutaminase substrate peptides for rapid enzymatic formation of hydrogels
    • Hu B., and Messersmith P. Rational design of transglutaminase substrate peptides for rapid enzymatic formation of hydrogels. J Am Chem Soc 125 (2003) 14298-14299
    • (2003) J Am Chem Soc , vol.125 , pp. 14298-14299
    • Hu, B.1    Messersmith, P.2
  • 36
    • 24344476349 scopus 로고    scopus 로고
    • Enzymatically cross-linked hydrogels and their adhesive strength to biosurfaces
    • Hu B., and Messersmith P. Enzymatically cross-linked hydrogels and their adhesive strength to biosurfaces. Orthodont Craniofac Res 8 (2005) 145-149
    • (2005) Orthodont Craniofac Res , vol.8 , pp. 145-149
    • Hu, B.1    Messersmith, P.2
  • 37
    • 31044449508 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of enzymatically cross-linked elastin-like polypeptide gels for cartilaginous tissue repair
    • McHale M.K., Setton L.A., and Chilkoti A. Synthesis and in vitro evaluation of enzymatically cross-linked elastin-like polypeptide gels for cartilaginous tissue repair. Tissue Eng 11 (2005) 1768-1779
    • (2005) Tissue Eng , vol.11 , pp. 1768-1779
    • McHale, M.K.1    Setton, L.A.2    Chilkoti, A.3
  • 38
    • 0037778904 scopus 로고    scopus 로고
    • Enzymatic modification of self-assembled peptide structures with tissue transglutaminase
    • Collier J.H., and Messersmith P.B. Enzymatic modification of self-assembled peptide structures with tissue transglutaminase. Bioconjugate Chem 14 (2003) 748-755
    • (2003) Bioconjugate Chem , vol.14 , pp. 748-755
    • Collier, J.H.1    Messersmith, P.B.2
  • 40
    • 0037086740 scopus 로고    scopus 로고
    • Involvement of tissue transglutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices
    • Heath D.J., Christian P., and Griffin M. Involvement of tissue transglutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices. Biomaterials 23 (2002) 1519-1526
    • (2002) Biomaterials , vol.23 , pp. 1519-1526
    • Heath, D.J.1    Christian, P.2    Griffin, M.3
  • 41
    • 0034093354 scopus 로고    scopus 로고
    • Protein crosslinking in assembly and remodeling of extracellular matrices: the role of transglutaminase
    • Aeschlimann D., and Thomazy V. Protein crosslinking in assembly and remodeling of extracellular matrices: the role of transglutaminase. Connect Tissue Res 41 (2000) 1-27
    • (2000) Connect Tissue Res , vol.41 , pp. 1-27
    • Aeschlimann, D.1    Thomazy, V.2
  • 42
    • 0026338017 scopus 로고
    • Transglutaminases-multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg C.S., Birckbichler P.J., and Rice R.H. Transglutaminases-multifunctional cross-linking enzymes that stabilize tissues. FASEB J 5 (1991) 3071-3077
    • (1991) FASEB J , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 43
    • 33646038598 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells
    • Lin C.W., and Ting A.Y. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J Am Chem Soc 128 (2006) 4542-4543
    • (2006) J Am Chem Soc , vol.128 , pp. 4542-4543
    • Lin, C.W.1    Ting, A.Y.2
  • 44
    • 0036145043 scopus 로고    scopus 로고
    • Tissue transglutaminase localization and activity regulation in the extracellular matrix of articular cartilage
    • Summey B.T., Graff R.D., Lai T.S., Greenberg C.S., and Lee G.M. Tissue transglutaminase localization and activity regulation in the extracellular matrix of articular cartilage. J Orthop Res 20 (2002) 76-82
    • (2002) J Orthop Res , vol.20 , pp. 76-82
    • Summey, B.T.1    Graff, R.D.2    Lai, T.S.3    Greenberg, C.S.4    Lee, G.M.5
  • 45
    • 0027516486 scopus 로고
    • Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes
    • Aeschlimann D., Wetterwald A., Fleisch H., and Paulsson M. Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes. J Cell Biol 120 (1993) 1461-1470
    • (1993) J Cell Biol , vol.120 , pp. 1461-1470
    • Aeschlimann, D.1    Wetterwald, A.2    Fleisch, H.3    Paulsson, M.4
  • 46
    • 0030450884 scopus 로고    scopus 로고
    • Tissue transglutaminase and factor XIII in cartilage and bone remodeling
    • Aeschlimann D., Mosher D., and Paulsson M. Tissue transglutaminase and factor XIII in cartilage and bone remodeling. Sem Thromb Hemostasis 22 (1996) 437-443
    • (1996) Sem Thromb Hemostasis , vol.22 , pp. 437-443
    • Aeschlimann, D.1    Mosher, D.2    Paulsson, M.3
  • 47
    • 0028946284 scopus 로고
    • Transglutaminase-catalyzed matrix crosslinking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate
    • Aeschlimann D., Kaupp O., and Paulsson M. Transglutaminase-catalyzed matrix crosslinking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate. J Cell Biol 129 (1995) 881-892
    • (1995) J Cell Biol , vol.129 , pp. 881-892
    • Aeschlimann, D.1    Kaupp, O.2    Paulsson, M.3
  • 48
    • 28444476698 scopus 로고    scopus 로고
    • ε(γ-glutaminyl)lysine crosslinks are concentrated in a non-collagenous microfibrillar fraction of cartilage
    • Bowness J., and Tarr A. ε(γ-glutaminyl)lysine crosslinks are concentrated in a non-collagenous microfibrillar fraction of cartilage. Biochem Cell Biol 75 (1997) 89-91
    • (1997) Biochem Cell Biol , vol.75 , pp. 89-91
    • Bowness, J.1    Tarr, A.2
  • 50
    • 0039904744 scopus 로고    scopus 로고
    • A new biological glue for cartilage-cartilage interfaces: tissue transglutaminase
    • Jurgensen K., Aeschlimann D., Cavin V., Genge M., and Hunziker E. A new biological glue for cartilage-cartilage interfaces: tissue transglutaminase. J Bone Joint Surg 79-A (1997) 185-193
    • (1997) J Bone Joint Surg , vol.79 -A , pp. 185-193
    • Jurgensen, K.1    Aeschlimann, D.2    Cavin, V.3    Genge, M.4    Hunziker, E.5
  • 51
    • 0030975473 scopus 로고    scopus 로고
    • Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides
    • Hamai A., Hashimoto N., Mochizuki H., Kato F., Makiguchi Y., Horie K., et al. Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides. J Biol Chem 272 (1997) 9123-9130
    • (1997) J Biol Chem , vol.272 , pp. 9123-9130
    • Hamai, A.1    Hashimoto, N.2    Mochizuki, H.3    Kato, F.4    Makiguchi, Y.5    Horie, K.6
  • 52
    • 0017735718 scopus 로고
    • Amine binding sites in acyl intermediates of transglutaminase
    • Gross M., Whetzel N., and Folk J. Amine binding sites in acyl intermediates of transglutaminase. J Biol Chem 252 (1977) 3752-3759
    • (1977) J Biol Chem , vol.252 , pp. 3752-3759
    • Gross, M.1    Whetzel, N.2    Folk, J.3
  • 53
    • 0034567635 scopus 로고    scopus 로고
    • Comparison of substrate specificities of transglutaminases using synthetic peptides as acyl donors
    • Ohtsuka T., Ota M., Nio N., and Motoki M. Comparison of substrate specificities of transglutaminases using synthetic peptides as acyl donors. Biosci Biotechnol Biochem 64 (2000) 2608-2613
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2608-2613
    • Ohtsuka, T.1    Ota, M.2    Nio, N.3    Motoki, M.4
  • 54
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed ε(γ-glutamyl)lysine bond formation
    • Folk J. Mechanism and basis for specificity of transglutaminase-catalyzed ε(γ-glutamyl)lysine bond formation. Adv Enzymol 54 (1983) 1-56
    • (1983) Adv Enzymol , vol.54 , pp. 1-56
    • Folk, J.1
  • 55
    • 0015787876 scopus 로고
    • A colorimetric method for measurement of the (peroxidase-mediated) oxidation of 3, 3′-diaminobenzidine
    • Fahmi D., and Herzog V. A colorimetric method for measurement of the (peroxidase-mediated) oxidation of 3, 3′-diaminobenzidine. J Histochem Cytochem 21 (1973)
    • (1973) J Histochem Cytochem , vol.21
    • Fahmi, D.1    Herzog, V.2
  • 57
    • 0028149514 scopus 로고
    • Localization of transglutaminase-reactive glutamine residues in bovine osteopontin
    • Sorensen E., Rasmussen L., Moller L., Jensen P., Hojrup P., and Petersen T. Localization of transglutaminase-reactive glutamine residues in bovine osteopontin. Biochem J 304 (1994) 13-16
    • (1994) Biochem J , vol.304 , pp. 13-16
    • Sorensen, E.1    Rasmussen, L.2    Moller, L.3    Jensen, P.4    Hojrup, P.5    Petersen, T.6
  • 58
    • 0028973138 scopus 로고
    • Transglutaminase-catalyzed cross-linking of fibrils of collagen V/Xi in A204 rhabdomyosarcoma cells
    • Kleman J.P., Aeschlimann D., Paulsson M., and Vanderrest M. Transglutaminase-catalyzed cross-linking of fibrils of collagen V/Xi in A204 rhabdomyosarcoma cells. Biochemistry 34 (1995) 13768-13775
    • (1995) Biochemistry , vol.34 , pp. 13768-13775
    • Kleman, J.P.1    Aeschlimann, D.2    Paulsson, M.3    Vanderrest, M.4
  • 60
    • 0023048837 scopus 로고
    • Transglutaminase-sensitive glutamine residues of human-plasma fibronectin revealed by studying its proteolytic fragments
    • Fesus L., Metsis M.L., Muszbek L., and Koteliansky V.E. Transglutaminase-sensitive glutamine residues of human-plasma fibronectin revealed by studying its proteolytic fragments. Eur J Biochem 154 (1986) 371-374
    • (1986) Eur J Biochem , vol.154 , pp. 371-374
    • Fesus, L.1    Metsis, M.L.2    Muszbek, L.3    Koteliansky, V.E.4
  • 62
    • 0025261220 scopus 로고
    • Highly sulfated glycosaminoglycans augment the cross-linking of vitronectin by guinea-pig liver transglutaminase-functional-studies of the cross-linked vitronectin multimers
    • Sane D.C., Moser T.L., Parker C.J., Seiffert D., Loskutoff D.J., and Greenberg C.S. Highly sulfated glycosaminoglycans augment the cross-linking of vitronectin by guinea-pig liver transglutaminase-functional-studies of the cross-linked vitronectin multimers. J Biol Chem 265 (1990) 3543-3548
    • (1990) J Biol Chem , vol.265 , pp. 3543-3548
    • Sane, D.C.1    Moser, T.L.2    Parker, C.J.3    Seiffert, D.4    Loskutoff, D.J.5    Greenberg, C.S.6
  • 63
    • 0025213864 scopus 로고
    • Sequence location of a putative transglutaminase cross-linking site in human vitronectin
    • Skorstengaard K., Halkier T., Hojrup P., and Mosher D. Sequence location of a putative transglutaminase cross-linking site in human vitronectin. FEBS Lett 262 (1990) 269-274
    • (1990) FEBS Lett , vol.262 , pp. 269-274
    • Skorstengaard, K.1    Halkier, T.2    Hojrup, P.3    Mosher, D.4
  • 64
    • 0026612802 scopus 로고
    • Identification of Gln(726) in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes
    • Aeschlimann D., Paulsson M., and Mann K. Identification of Gln(726) in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes. J Biol Chem 267 (1992) 11316-11321
    • (1992) J Biol Chem , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 65
    • 33745846379 scopus 로고    scopus 로고
    • Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library
    • Sugimura Y., Hosono M., Wada F., Yoshimura T., Maki M., and Hitomi K. Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library. J Biol Chem 281 (2006) 17699-17706
    • (2006) J Biol Chem , vol.281 , pp. 17699-17706
    • Sugimura, Y.1    Hosono, M.2    Wada, F.3    Yoshimura, T.4    Maki, M.5    Hitomi, K.6
  • 66
    • 33751071631 scopus 로고    scopus 로고
    • Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase
    • Keresztessy Z., Csosz E., Harsfalvi J., Csomos K., Gray J., Lightowlers R., et al. Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase. Protein Sci 15 (2006) 2466-2480
    • (2006) Protein Sci , vol.15 , pp. 2466-2480
    • Keresztessy, Z.1    Csosz, E.2    Harsfalvi, J.3    Csomos, K.4    Gray, J.5    Lightowlers, R.6
  • 67
    • 0037018095 scopus 로고    scopus 로고
    • Specificity of tissue transglutaminase explains cereal toxicity in celiac disease
    • Vader L., de Ru A., van der Wal Y., Kooy Y., Benckuijsen W., Mearin M., et al. Specificity of tissue transglutaminase explains cereal toxicity in celiac disease. J Exp Med 195 (2002) 643-649
    • (2002) J Exp Med , vol.195 , pp. 643-649
    • Vader, L.1    de Ru, A.2    van der Wal, Y.3    Kooy, Y.4    Benckuijsen, W.5    Mearin, M.6
  • 70
    • 0033567396 scopus 로고    scopus 로고
    • Noncollagenous, nonproteoglycan macromolecules of cartilage
    • Neame P., Tapp H., and Azizan A. Noncollagenous, nonproteoglycan macromolecules of cartilage. Cell, Mol Life Sci 55 (1999) 1327-1340
    • (1999) Cell, Mol Life Sci , vol.55 , pp. 1327-1340
    • Neame, P.1    Tapp, H.2    Azizan, A.3
  • 71
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminase: nature's biological glues
    • Griffin M., Casadio R., and Bergamini C. Transglutaminase: nature's biological glues. Biochem J 368 (2002) 377-396
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.3
  • 72
    • 28244476534 scopus 로고    scopus 로고
    • Biology of the normal joint
    • Harris E., et al. (Ed), Saunders Co., St. Louis, MO
    • Goldring S., and Goldring M. Biology of the normal joint. In: Harris E., et al. (Ed). Kelley's textbook of rheumatology (2005), Saunders Co., St. Louis, MO 6-26
    • (2005) Kelley's textbook of rheumatology , pp. 6-26
    • Goldring, S.1    Goldring, M.2
  • 73
    • 0024291657 scopus 로고
    • Amino-acid sequence of guinea-pig liver transglutaminase from its cDNA sequence
    • Ikura K., Nasu T., Yokota H., Tsuchiya Y., Sasaki R., and Chiba H. Amino-acid sequence of guinea-pig liver transglutaminase from its cDNA sequence. Biochemistry 27 (1988) 2898-2905
    • (1988) Biochemistry , vol.27 , pp. 2898-2905
    • Ikura, K.1    Nasu, T.2    Yokota, H.3    Tsuchiya, Y.4    Sasaki, R.5    Chiba, H.6
  • 75
    • 33744995585 scopus 로고    scopus 로고
    • Short-duration enzymatic treatment promotes integration of a cartilage graft in defect
    • Janssen L., In der Maur C., Bos P., Hardillo J., and van Osch G. Short-duration enzymatic treatment promotes integration of a cartilage graft in defect. Ann Otol Rhinol Laryngol 115 (2006) 461-468
    • (2006) Ann Otol Rhinol Laryngol , vol.115 , pp. 461-468
    • Janssen, L.1    In der Maur, C.2    Bos, P.3    Hardillo, J.4    van Osch, G.5
  • 77
    • 34948847071 scopus 로고    scopus 로고
    • Biology, physiology, and morphology of bone
    • Harris E., et al. (Ed), Saunders Co., St. Louis, MO
    • Rubin C., and Rubin J. Biology, physiology, and morphology of bone. In: Harris E., et al. (Ed). Kelley's textbook of rheumatology (2005), Saunders Co., St. Louis, MO 1449-1469
    • (2005) Kelley's textbook of rheumatology , pp. 1449-1469
    • Rubin, C.1    Rubin, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.