메뉴 건너뛰기




Volumn 97, Issue 2, 2013, Pages 461-475

Enzyme-catalyzed protein crosslinking

Author keywords

Conjugation; Cross linking; Fusion proteins; Ligation; Sortase A; Transglutaminase

Indexed keywords

CONJUGATION; FUSION PROTEINS; LIGATION; SORTASE A; TRANSGLUTAMINASES;

EID: 84873996105     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4569-z     Document Type: Review
Times cited : (257)

References (126)
  • 1
    • 0024801107 scopus 로고
    • Purification and characteristics of a novel transglutaminase derived from microorganisms
    • 1:CAS:528:DyaK3cXjt1em 10.1271/bbb1961.53.2613
    • Ando H, Adachi M, Umeda K, Matsuura A, Nonaka M, Uchio R, Tanaka H, Motoki M (1989) Purification and characteristics of a novel transglutaminase derived from microorganisms. Agr Biol Chem Tokyo 53:2613-2617
    • (1989) Agr Biol Chem Tokyo , vol.53 , pp. 2613-2617
    • Ando, H.1    Adachi, M.2    Umeda, K.3    Matsuura, A.4    Nonaka, M.5    Uchio, R.6    Tanaka, H.7    Motoki, M.8
  • 2
    • 67650179211 scopus 로고    scopus 로고
    • A straight path to circular proteins
    • 10.1074/jbc.M901752200 1:CAS:528:DC%2BD1MXmsF2jsro%3D 10.1074/jbc.M901752200
    • Antos JM, Popp MWL, Ernst R, Chew GL, Spooner E, Ploegh HL (2009) A straight path to circular proteins. J Biol Chem 284:16028-16036. doi: 10.1074/jbc.M901752200
    • (2009) J Biol Chem , vol.284 , pp. 16028-16036
    • Antos, J.M.1    Popp, M.W.L.2    Ernst, R.3    Chew, G.L.4    Spooner, E.5    Ploegh, H.L.6
  • 3
    • 13944267448 scopus 로고    scopus 로고
    • Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough
    • 10.1021/Jf0485032 1:CAS:528:DC%2BD2MXnsVCktQ%3D%3D 10.1021/jf0485032
    • Autio K, Kruus K, Knaapila A, Gerber N, Flander L, Buchert J (2005) Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough. J Agric Food Chem 53:1039-1045. doi: 10.1021/Jf0485032
    • (2005) J Agric Food Chem , vol.53 , pp. 1039-1045
    • Autio, K.1    Kruus, K.2    Knaapila, A.3    Gerber, N.4    Flander, L.5    Buchert, J.6
  • 4
    • 78651281327 scopus 로고    scopus 로고
    • Enzymatic cross-linking of a nanofibrous peptide hydrogel
    • 10.1021/Bm1010195 1:CAS:528:DC%2BC3cXhsFaisbrP 10.1021/bm1010195
    • Bakota EL, Aulisa L, Galler KM, Hartgerink JD (2011) Enzymatic cross-linking of a nanofibrous peptide hydrogel. Biomacromolecules 12:82-87. doi: 10.1021/Bm1010195
    • (2011) Biomacromolecules , vol.12 , pp. 82-87
    • Bakota, E.L.1    Aulisa, L.2    Galler, K.M.3    Hartgerink, J.D.4
  • 5
    • 0036751964 scopus 로고    scopus 로고
    • Effects of transglutaminase on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends
    • 10.1111/j.1365-2621.2002.tb08794.x 1:CAS:528:DC%2BD38XotVGmtL8%3D 10.1111/j.1365-2621.2002.tb08794.x
    • Basman A, Köksel H, Ng PKW (2002) Effects of transglutaminase on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends. J Food Sci 67:2654-2658. doi: 10.1111/j.1365-2621.2002.tb08794.x
    • (2002) J Food Sci , vol.67 , pp. 2654-2658
    • Basman, A.1    Köksel, H.2    Ng, P.K.W.3
  • 6
    • 33646564345 scopus 로고    scopus 로고
    • When quinones meet amino acids: Chemical, physical and biological consequences
    • 10.1007/s00726-005-0298-2 1:CAS:528:DC%2BD28Xktlaks7w%3D 10.1007/s00726-005-0298-2
    • Bittner S (2006) When quinones meet amino acids: chemical, physical and biological consequences. Amino Acids 30:205-224. doi: 10.1007/s00726-005-0298-2
    • (2006) Amino Acids , vol.30 , pp. 205-224
    • Bittner, S.1
  • 7
    • 34548673743 scopus 로고    scopus 로고
    • Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties
    • 10.1016/j.idairyj.2007.01.019 10.1016/j.idairyj.2007.01.019 1:CAS:528:DC%2BD2sXhtVOis73F
    • Bönisch MP, Huss M, Weitl K, Kulozik U (2007) Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties. Int Dairy J 17:1360-1371. doi: 10.1016/j.idairyj.2007.01.019
    • (2007) Int Dairy J , vol.17 , pp. 1360-1371
    • Bönisch, M.P.1    Huss, M.2    Weitl, K.3    Kulozik, U.4
  • 8
    • 0036882398 scopus 로고    scopus 로고
    • Proteases in organic synthesis
    • 10.1021/Cr010164d 1:CAS:528:DC%2BD38XovVeqtLw%3D 10.1021/cr010164d
    • Bordusa F (2002) Proteases in organic synthesis. Chem Rev 102:4817-4867. doi: 10.1021/Cr010164d
    • (2002) Chem Rev , vol.102 , pp. 4817-4867
    • Bordusa, F.1
  • 10
    • 84856667080 scopus 로고    scopus 로고
    • Comparative study on protein cross-linking and gel enhancing effect of microbial transglutaminase on surimi from different fish
    • 10.1002/Jsfa.4656 1:CAS:528:DC%2BC38XhvVSns74%3D 10.1002/jsfa.4656
    • Chanarat S, Benjakul S, H-Kittikun A (2012) Comparative study on protein cross-linking and gel enhancing effect of microbial transglutaminase on surimi from different fish. J Sci Food Agric 92:844-852. doi: 10.1002/Jsfa.4656
    • (2012) J Sci Food Agric , vol.92 , pp. 844-852
    • Chanarat, S.1    Benjakul, S.2    H-Kittikun, A.3
  • 11
    • 30844444172 scopus 로고    scopus 로고
    • Bacterial tyrosinases
    • 10.1016/j.syapm.2005.07.012 1:CAS:528:DC%2BD28Xjt1Krs7s%3D 10.1016/j.syapm.2005.07.012
    • Claus H, Decker H (2006) Bacterial tyrosinases. Syst Appl Microbiol 29:3-14. doi: 10.1016/j.syapm.2005.07.012
    • (2006) Syst Appl Microbiol , vol.29 , pp. 3-14
    • Claus, H.1    Decker, H.2
  • 12
    • 0344665625 scopus 로고    scopus 로고
    • Application of transglutaminases in the modification of wool textiles
    • 10.1016/j.enzmictec.2003.08.004 1:CAS:528:DC%2BD3sXps1OltL0%3D 10.1016/j.enzmictec.2003.08.004
    • Cortez J, Bonner PLR, Griffin M (2004) Application of transglutaminases in the modification of wool textiles. Enzyme Microb Technol 34:64-72. doi: 10.1016/j.enzmictec.2003.08.004
    • (2004) Enzyme Microb Technol , vol.34 , pp. 64-72
    • Cortez, J.1    Bonner, P.L.R.2    Griffin, M.3
  • 13
    • 20044362194 scopus 로고    scopus 로고
    • Transglutaminase treatment of wool fabrics leads to resistance to detergent damage
    • 10.1016/j.jbiotec.2004.12.007 10.1016/j.jbiotec.2004.12.007 1:CAS:528:DC%2BD2MXhvVersLs%3D
    • Cortez J, Bonner PLR, Griffin M (2005) Transglutaminase treatment of wool fabrics leads to resistance to detergent damage. J Biotechnol 116:379-386. doi: 10.1016/j.jbiotec.2004.12.007
    • (2005) J Biotechnol , vol.116 , pp. 379-386
    • Cortez, J.1    Bonner, P.L.R.2    Griffin, M.3
  • 14
    • 34247376390 scopus 로고    scopus 로고
    • Transglutaminase mediated grafting of silk proteins onto wool fabrics leading to improved physical and mechanical properties
    • 10.1016/j.enzmictec.2006.10.013 1:CAS:528:DC%2BD2sXkslKrsbk%3D 10.1016/j.enzmictec.2006.10.013
    • Cortez J, Anghieri A, Bonner PLR, Griffin M, Freddi G (2007) Transglutaminase mediated grafting of silk proteins onto wool fabrics leading to improved physical and mechanical properties. Enzyme Microb Technol 40:1698-1704. doi: 10.1016/j.enzmictec.2006.10.013
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1698-1704
    • Cortez, J.1    Anghieri, A.2    Bonner, P.L.R.3    Griffin, M.4    Freddi, G.5
  • 15
    • 67649921901 scopus 로고    scopus 로고
    • Transglutaminase-mediated crosslinking of gelatin onto wool surfaces to improve the fabric properties
    • 10.1002/App.30300 1:CAS:528:DC%2BD1MXmt1agt7Y%3D 10.1002/app.30300
    • Cui L, Wang Q, Wang P, Huan Q, Fan X (2009) Transglutaminase-mediated crosslinking of gelatin onto wool surfaces to improve the fabric properties. J Appl Polym Sci 113:2598-2604. doi: 10.1002/App.30300
    • (2009) J Appl Polym Sci , vol.113 , pp. 2598-2604
    • Cui, L.1    Wang, Q.2    Wang, P.3    Huan, Q.4    Fan, X.5
  • 16
    • 79955379014 scopus 로고    scopus 로고
    • Casein and transglutaminase-mediated modification of wool surface
    • 10.1002/elsc.201000110 1:CAS:528:DC%2BC3MXmt1yitbw%3D 10.1002/elsc.201000110
    • Cui L, Fan X, Wang P, Wang Q, Fu G (2011) Casein and transglutaminase- mediated modification of wool surface. Eng Life Sci 11:201-206. doi: 10.1002/elsc.201000110
    • (2011) Eng Life Sci , vol.11 , pp. 201-206
    • Cui, L.1    Fan, X.2    Wang, P.3    Wang, Q.4    Fu, G.5
  • 17
    • 67649391054 scopus 로고    scopus 로고
    • Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis
    • 10.1038/Nrmicro2148 1:CAS:528:DC%2BD1MXms1altbc%3D 10.1038/nrmicro2148
    • Darwin KH (2009) Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis. Nat Rev Microbiol 7:485-491. doi: 10.1038/Nrmicro2148
    • (2009) Nat Rev Microbiol , vol.7 , pp. 485-491
    • Darwin, K.H.1
  • 18
    • 77955274184 scopus 로고    scopus 로고
    • Modular enzymatically crosslinked protein polymer hydrogels for in situ gelation
    • 10.1016/j.biomaterials.2010.06.003 1:CAS:528:DC%2BC3cXpsFSjsLg%3D 10.1016/j.biomaterials.2010.06.003
    • Davis NE, Ding S, Forster RE, Pinkas DM, Barron AE (2010) Modular enzymatically crosslinked protein polymer hydrogels for in situ gelation. Biomaterials 31:7288-7297. doi: 10.1016/j.biomaterials.2010.06.003
    • (2010) Biomaterials , vol.31 , pp. 7288-7297
    • Davis, N.E.1    Ding, S.2    Forster, R.E.3    Pinkas, D.M.4    Barron, A.E.5
  • 19
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • 10.1146/annurev.biochem.69.1.923 1:CAS:528:DC%2BD3cXnt1ajurc%3D 10.1146/annurev.biochem.69.1.923
    • Dawson PE, Kent SBH (2000) Synthesis of native proteins by chemical ligation. Annual Rev Biochem 69:923-960. doi: 10.1146/annurev.biochem.69.1.923
    • (2000) Annual Rev Biochem , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.H.2
  • 20
    • 33645508502 scopus 로고    scopus 로고
    • Chitosan-whey protein edible films produced in the absence or presence of transglutaminase: Analysis of their mechanical and barrier properties
    • 10.1021/Bm050661u 10.1021/bm050661u 1:CAS:528:DC%2BD28XhslCit7c%3D
    • Di Pierro P, Chico B, Villalonga R, Mariniello L, Damiao AE, Masi P, Porta R (2006) Chitosan-whey protein edible films produced in the absence or presence of transglutaminase: analysis of their mechanical and barrier properties. Biomacromolecules 7:744-749. doi: 10.1021/Bm050661u
    • (2006) Biomacromolecules , vol.7 , pp. 744-749
    • Di Pierro, P.1    Chico, B.2    Villalonga, R.3    Mariniello, L.4    Damiao, A.E.5    Masi, P.6    Porta, R.7
  • 21
    • 34247365327 scopus 로고    scopus 로고
    • Improvement of shrink-resistance and tensile strength of wool fabric treated with a novel microbial transglutaminase from Streptomyces hygroscopicus
    • 10.1016/j.enzmictec.2006.12.001 1:CAS:528:DC%2BD2sXkslKrtrs%3D 10.1016/j.enzmictec.2006.12.001
    • Du G, Cui L, Zhu Y, Chen J (2007) Improvement of shrink-resistance and tensile strength of wool fabric treated with a novel microbial transglutaminase from Streptomyces hygroscopicus. Enzyme Microb Technol 40:1753-1757. doi: 10.1016/j.enzmictec.2006.12.001
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1753-1757
    • Du, G.1    Cui, L.2    Zhu, Y.3    Chen, J.4
  • 22
    • 77956618691 scopus 로고    scopus 로고
    • Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels
    • 10.1016/j.idairyj.2010.06.008 1:CAS:528:DC%2BC3cXhtFOktL%2FO 10.1016/j.idairyj.2010.06.008
    • Ercili Cura D, Lille M, Partanen R, Kruus K, Buchert J, Lantto R (2010) Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels. Int Dairy J 20:830-837. doi: 10.1016/j.idairyj.2010.06.008
    • (2010) Int Dairy J , vol.20 , pp. 830-837
    • Ercili Cura, D.1    Lille, M.2    Partanen, R.3    Kruus, K.4    Buchert, J.5    Lantto, R.6
  • 23
    • 0001629518 scopus 로고    scopus 로고
    • Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase
    • 10.1046/j.1432-1327.2000.01013.x 10.1046/j.1432-1327.2000.01013.x
    • Espín JC, Varón R, Fenoll LG, Gilabert MA, García-Ruíz PA, Tudela J, García-Cánovas F (2000) Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase. Eur J Biochem 267:1270-1279. doi: 10.1046/j.1432-1327.2000.01013.x
    • (2000) Eur J Biochem , vol.267 , pp. 1270-1279
    • Espín, J.C.1    Varón, R.2    Fenoll, L.G.3    Gilabert, M.A.4    García-Ruíz, P.A.5    Tudela, J.6    García-Cánovas, F.7
  • 24
    • 80052642533 scopus 로고    scopus 로고
    • Sulfhydryl oxidases: Sources, properties, production and applications
    • 10.1007/s00253-011-3440-y 1:CAS:528:DC%2BC3MXpsVWrt78%3D 10.1007/s00253-011-3440-y
    • Faccio G, Nivala O, Kruus K, Buchert J, Saloheimo M (2011) Sulfhydryl oxidases: sources, properties, production and applications. Appl Microbiol Biotechnol 91:957-966. doi: 10.1007/s00253-011-3440-y
    • (2011) Appl Microbiol Biotechnol , vol.91 , pp. 957-966
    • Faccio, G.1    Nivala, O.2    Kruus, K.3    Buchert, J.4    Saloheimo, M.5
  • 25
    • 84870817930 scopus 로고    scopus 로고
    • Bacterial tyrosinases and their applications
    • doi: 10.1016/j.procbio.2012.08.018
    • Faccio G, Kruus K, Saloheimo M, Thöny-Meyer L (2012) Bacterial tyrosinases and their applications. Process Biochem. doi: 10.1016/j.procbio. 2012.08.018
    • (2012) Process Biochem.
    • Faccio G, K.1
  • 26
    • 78649451634 scopus 로고    scopus 로고
    • Cross-linking and immobilisation of different proteins with recombinant Verrucomicrobium spinosum tyrosinase
    • 10.1016/j.jbiotec.2010.10.068 1:CAS:528:DC%2BC3cXhsVyhur3N 10.1016/j.jbiotec.2010.10.068
    • Fairhead M, Thöny-Meyer L (2010) Cross-linking and immobilisation of different proteins with recombinant Verrucomicrobium spinosum tyrosinase. J Biotechnol 150:546-551. doi: 10.1016/j.jbiotec.2010.10.068
    • (2010) J Biotechnol , vol.150 , pp. 546-551
    • Fairhead, M.1    Thöny-Meyer, L.2
  • 27
    • 84855812531 scopus 로고    scopus 로고
    • Bacterial tyrosinases: Old enzymes with new relevance to biotechnology
    • 10.1016/j.nbt.2011.05.007 1:CAS:528:DC%2BC38XovFymtA%3D%3D 10.1016/j.nbt.2011.05.007
    • Fairhead M, Thöny-Meyer L (2012) Bacterial tyrosinases: old enzymes with new relevance to biotechnology. New Biotechnol 29:183-191. doi: 10.1016/j.nbt.2011.05.007
    • (2012) New Biotechnol , vol.29 , pp. 183-191
    • Fairhead, M.1    Thöny-Meyer, L.2
  • 28
    • 0036980061 scopus 로고    scopus 로고
    • Protein-protein crosslinking in food: Methods, consequences, applications
    • 10.1016/S0924-2244(02)00257-1 1:CAS:528:DC%2BD3sXht1Giuro%3D 10.1016/S0924-2244(02)00257-1
    • Gerrard JA (2002) Protein-protein crosslinking in food: methods, consequences, applications. Trends Food Sci Technol 13:391-399. doi: 10.1016/S0924-2244(02)00257-1
    • (2002) Trends Food Sci Technol , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 29
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • 10.1042/BJ20021234 1:CAS:528:DC%2BD38XovF2jt78%3D 10.1042/BJ20021234
    • Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: nature's biological glues. Biochem J 368:377-396. doi: 10.1042/BJ20021234
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 30
    • 77954310525 scopus 로고    scopus 로고
    • An analysis of substrate binding interactions in the heme peroxidase enzymes: A structural perspective
    • 10.1016/j.abb.2010.02.015 1:CAS:528:DC%2BC3cXosV2itro%3D 10.1016/j.abb.2010.02.015
    • Gumiero A, Murphy EJ, Metcalfe CL, Moody PCE, Raven EL (2010) An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective. Arch Biochem Biophys 500:13-20. doi: 10.1016/j.abb.2010.02.015
    • (2010) Arch Biochem Biophys , vol.500 , pp. 13-20
    • Gumiero, A.1    Murphy, E.J.2    Metcalfe, C.L.3    Moody, P.C.E.4    Raven, E.L.5
  • 31
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: Molecular approaches and industrial applications
    • 10.1007/s00253-002-0975-y 1:CAS:528:DC%2BD38XlsVSksbg%3D 10.1007/s00253-002-0975-y
    • Gupta R, Beg QK, Lorenz P (2002) Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol 59:15-32. doi: 10.1007/s00253-002-0975-y
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, P.3
  • 32
    • 79953005868 scopus 로고    scopus 로고
    • Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate
    • 10.1074/jbc.M110.189282 1:CAS:528:DC%2BC3MXhsFGlt7k%3D 10.1074/jbc.M110.189282
    • Guth E, Thommen M, Weber-Ban E (2011) Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate. J Biol Chem 286:4412-4419. doi: 10.1074/jbc.M110.189282
    • (2011) J Biol Chem , vol.286 , pp. 4412-4419
    • Guth, E.1    Thommen, M.2    Weber-Ban, E.3
  • 33
    • 33645163110 scopus 로고    scopus 로고
    • Fungal tyrosinases: New prospects in molecular characteristics, bioengineering and biotechnological applications
    • 10.1111/j.1365-2672.2006.02866.x 1:CAS:528:DC%2BD28XjsFartb4%3D 10.1111/j.1365-2672.2006.02866.x
    • Halaouli S, Asther M, Sigoillot JC, Hamdi M, Lomascolo A (2006) Fungal tyrosinases: new prospects in molecular characteristics, bioengineering and biotechnological applications. J Appl Microbiol 100:219-232. doi: 10.1111/j.1365-2672.2006.02866.x
    • (2006) J Appl Microbiol , vol.100 , pp. 219-232
    • Halaouli, S.1    Asther, M.2    Sigoillot, J.C.3    Hamdi, M.4    Lomascolo, A.5
  • 34
    • 77952166417 scopus 로고    scopus 로고
    • Directing the oligomer size distribution of peroxidase-mediated cross-linked bovine α-lactalbumin
    • 10.1021/Jf100168x 1:CAS:528:DC%2BC3cXjsFSlsLk%3D 10.1021/jf100168x
    • Heijnis WH, Wierenga PA, Berkel WJH, Gruppen H (2010) Directing the oligomer size distribution of peroxidase-mediated cross-linked bovine α-lactalbumin. J Agr Food Chem 58:5692-5697. doi: 10.1021/Jf100168x
    • (2010) J Agr Food Chem , vol.58 , pp. 5692-5697
    • Heijnis, W.H.1    Wierenga, P.A.2    Berkel, W.J.H.3    Gruppen, H.4
  • 36
    • 78650676786 scopus 로고    scopus 로고
    • Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear magnetic resonance spectroscopy
    • 10.1016/j.jbiotec.2010.11.006 1:CAS:528:DC%2BC3MXht1Slug%3D%3D 10.1016/j.jbiotec.2010.11.006
    • Hellman M, Mattinen ML, Fu B, Buchert J, Permi P (2011) Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear magnetic resonance spectroscopy. J Biotechnol 151:143-150. doi: 10.1016/j.jbiotec.2010.11.006
    • (2011) J Biotechnol , vol.151 , pp. 143-150
    • Hellman, M.1    Mattinen, M.L.2    Fu, B.3    Buchert, J.4    Permi, P.5
  • 37
    • 79951816315 scopus 로고    scopus 로고
    • Architects at the bacterial surface - Sortases and the assembly of pili with isopeptide bonds
    • 10.1038/Nrmicro2520 1:CAS:528:DC%2BC3MXhvFCntrk%3D 10.1038/nrmicro2520
    • Hendrickx APA, Budzik JM, Oh SY, Schneewind O (2011) Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds. Nat Rev Microbiol 9:166-176. doi: 10.1038/Nrmicro2520
    • (2011) Nat Rev Microbiol , vol.9 , pp. 166-176
    • Hendrickx, A.P.A.1    Budzik, J.M.2    Oh, S.Y.3    Schneewind, O.4
  • 38
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • 10.1146/annurev.biochem.67.1.425 1:CAS:528:DyaK1cXlsFOmsLc%3D 10.1146/annurev.biochem.67.1.425
    • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425-479. doi: 10.1146/annurev.biochem.67.1.425
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 39
    • 0020479850 scopus 로고
    • Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells - Relationship to the breakdown of abnormal proteins
    • 1:CAS:528:DyaL38XmtFegu7g%3D
    • Hershko A, Eytan E, Ciechanover A, Haas AL (1982) Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells - relationship to the breakdown of abnormal proteins. J Biol Chem 257:13964-13970
    • (1982) J Biol Chem , vol.257 , pp. 13964-13970
    • Hershko, A.1    Eytan, E.2    Ciechanover, A.3    Haas, A.L.4
  • 40
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • 10.1038/nature07958 1:CAS:528:DC%2BD1MXjs1Klsbg%3D 10.1038/nature07958
    • Hochstrasser M (2009) Origin and function of ubiquitin-like proteins. Nature 458:422-429. doi: 10.1038/nature07958
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 41
    • 0026641632 scopus 로고
    • Cross-linking of contractile proteins from skeletal muscle by treatment with microbial transglutaminase
    • 1:CAS:528:DyaK38XlvVOks7k%3D
    • Huang YP, Seguro K, Motoki M, Tawada K (1992) Cross-linking of contractile proteins from skeletal muscle by treatment with microbial transglutaminase. J Biochem Tokyo 112:229-234
    • (1992) J Biochem Tokyo , vol.112 , pp. 229-234
    • Huang, Y.P.1    Seguro, K.2    Motoki, M.3    Tawada, K.4
  • 42
    • 0021213448 scopus 로고
    • Oxidation of tyrosine residues in proteins by tyrosinase - Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4- dihydroxyphenylalanine
    • 1:CAS:528:DyaL2cXlsVOhtLo%3D
    • Ito S, Kato T, Shinpo K, Fujita K (1984) Oxidation of tyrosine residues in proteins by tyrosinase - formation of protein-bonded 3,4- dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine. Biochem J 222:407-411
    • (1984) Biochem J , vol.222 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 43
    • 0028518514 scopus 로고
    • A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues
    • 10.1126/science.7939659 1:CAS:528:DyaK2MXht12jsbk%3D 10.1126/science. 7939659
    • Jackson DY, Burnier J, Quan C, Stanley M, Tom J, Wells JA (1994) A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 266:243-247. doi: 10.1126/science.7939659
    • (1994) Science , vol.266 , pp. 243-247
    • Jackson, D.Y.1    Burnier, J.2    Quan, C.3    Stanley, M.4    Tom, J.5    Wells, J.A.6
  • 44
    • 33645726443 scopus 로고    scopus 로고
    • Transglutaminase in dairy products: Chemistry, physics, applications
    • 10.1111/j.1745-4603.2006.00042.x 10.1111/j.1745-4603.2006.00042.x
    • Jaros D, Partschefeld C, Henle T, Rohm H (2006) Transglutaminase in dairy products: chemistry, physics, applications. J Texture Stud 37:113-155. doi: 10.1111/j.1745-4603.2006.00042.x
    • (2006) J Texture Stud , vol.37 , pp. 113-155
    • Jaros, D.1    Partschefeld, C.2    Henle, T.3    Rohm, H.4
  • 45
    • 61349111323 scopus 로고    scopus 로고
    • Injectable chitosan-based hydrogels for cartilage tissue engineering
    • 10.1016/j.biomaterials.2009.01.020 1:CAS:528:DC%2BD1MXisVCmt78%3D 10.1016/j.biomaterials.2009.01.020
    • Jin R, Moreira Teixeira LS, Dijkstra PJ, Karperien M, van Blitterswijk CA, Zhong ZY, Feijen J (2009) Injectable chitosan-based hydrogels for cartilage tissue engineering. Biomaterials 30:2544-2551. doi: 10.1016/j.biomaterials.2009. 01.020
    • (2009) Biomaterials , vol.30 , pp. 2544-2551
    • Jin, R.1    Moreira Teixeira, L.S.2    Dijkstra, P.J.3    Karperien, M.4    Van Blitterswijk, C.A.5    Zhong, Z.Y.6    Feijen, J.7
  • 46
    • 77049093185 scopus 로고    scopus 로고
    • Enzymatically-crosslinked injectable hydrogels based on biomimetic dextran-hyaluronic acid conjugates for cartilage tissue engineering
    • 10.1016/j.biomaterials.2010.01.013 1:CAS:528:DC%2BC3cXit1Sgtbs%3D 10.1016/j.biomaterials.2010.01.013
    • Jin R, Moreira Teixeira LS, Dijkstra PJ, van Blitterswijk CA, Karperien M, Feijen J (2010) Enzymatically-crosslinked injectable hydrogels based on biomimetic dextran-hyaluronic acid conjugates for cartilage tissue engineering. Biomaterials 31:3103-3113. doi: 10.1016/j.biomaterials.2010.01.013
    • (2010) Biomaterials , vol.31 , pp. 3103-3113
    • Jin, R.1    Moreira Teixeira, L.S.2    Dijkstra, P.J.3    Van Blitterswijk, C.A.4    Karperien, M.5    Feijen, J.6
  • 47
    • 67649185211 scopus 로고    scopus 로고
    • Use of chemical redox agents and exogenous enzymes to modify the protein network during breadmaking - A review
    • 10.1016/j.jcs.2009.04.001 1:CAS:528:DC%2BD1MXnvVaksrk%3D 10.1016/j.jcs.2009.04.001
    • Joye IJ, Lagrain B, Delcour JA (2009) Use of chemical redox agents and exogenous enzymes to modify the protein network during breadmaking - a review. J Cereal Sci 50:11-21. doi: 10.1016/j.jcs.2009.04.001
    • (2009) J Cereal Sci , vol.50 , pp. 11-21
    • Joye, I.J.1    Lagrain, B.2    Delcour, J.A.3
  • 48
    • 59649127636 scopus 로고    scopus 로고
    • Tyrosinase-catalysed coating of wool fibres with different protein-based biomaterials
    • 10.1163/156856209X404523 1:CAS:528:DC%2BD1MXisVWmsrw%3D 10.1163/156856209X404523
    • Jus S, Kokol V, Guebitz GM (2009) Tyrosinase-catalysed coating of wool fibres with different protein-based biomaterials. J Biomater Sci 20:253-269. doi: 10.1163/156856209X404523
    • (2009) J Biomater Sci , vol.20 , pp. 253-269
    • Jus, S.1    Kokol, V.2    Guebitz, G.M.3
  • 49
    • 84856498760 scopus 로고    scopus 로고
    • Enzymatic cross-linking of gelatine with laccase and tyrosinase
    • 10.3109/10242422.2012.646036 1:CAS:528:DC%2BC38XhsVOmtL0%3D 10.3109/10242422.2012.646036
    • Jus S, Stachel I, Fairhead M, Meyer M, Thöny-Meyer L, Guebitz GM (2012) Enzymatic cross-linking of gelatine with laccase and tyrosinase. Biocatal Biotransfor 30:86-95. doi: 10.3109/10242422.2012.646036
    • (2012) Biocatal Biotransfor , vol.30 , pp. 86-95
    • Jus, S.1    Stachel, I.2    Fairhead, M.3    Meyer, M.4    Thöny-Meyer, L.5    Guebitz, G.M.6
  • 50
    • 78249236203 scopus 로고    scopus 로고
    • Film formation and surface properties of enzymatically crosslinked casein films
    • 10.1002/App.32943 1:CAS:528:DC%2BC3cXht12ksL3M 10.1002/app.32943
    • Juvonen H, Smolander M, Boer H, Pere J, Buchert J, Peltonen J (2011) Film formation and surface properties of enzymatically crosslinked casein films. J Appl Polym Sci 119:2205-2213. doi: 10.1002/App.32943
    • (2011) J Appl Polym Sci , vol.119 , pp. 2205-2213
    • Juvonen, H.1    Smolander, M.2    Boer, H.3    Pere, J.4    Buchert, J.5    Peltonen, J.6
  • 51
    • 54349120222 scopus 로고    scopus 로고
    • Effects of trehalose, transglutaminase, and gum on rheological, fermentation, and baking properties of frozen dough
    • 10.1016/j.foodres.2008.07.013 1:CAS:528:DC%2BD1cXht12gurnE 10.1016/j.foodres.2008.07.013
    • Kim YS, Huang W, Du G, Pan Z, Chung O (2008) Effects of trehalose, transglutaminase, and gum on rheological, fermentation, and baking properties of frozen dough. Food Res Int 41:903-908. doi: 10.1016/j.foodres.2008.07.013
    • (2008) Food Res Int , vol.41 , pp. 903-908
    • Kim, Y.S.1    Huang, W.2    Du, G.3    Pan, Z.4    Chung, O.5
  • 52
    • 84865696769 scopus 로고    scopus 로고
    • Antibody-cytokine fusion proteins
    • 10.1016/j.abb.2012.03.001 1:CAS:528:DC%2BC38XlsVSjsbo%3D 10.1016/j.abb.2012.03.001
    • Kontermann RE (2012) Antibody-cytokine fusion proteins. Arch Biochem Biophys 526:194-205. doi: 10.1016/j.abb.2012.03.001
    • (2012) Arch Biochem Biophys , vol.526 , pp. 194-205
    • Kontermann, R.E.1
  • 53
    • 58149187900 scopus 로고    scopus 로고
    • PeroxiBase: A database with new tools for peroxidase family classification
    • 10.1093/Nar/Gkn680 1:CAS:528:DC%2BD1cXhsFejt7bK 10.1093/nar/gkn680
    • Koua D, Cerutti L, Falquet L, Sigrist CJA, Theiler G, Hulo N, Dunand C (2009) PeroxiBase: a database with new tools for peroxidase family classification. Nucleic Acids Res 37:D261-D266. doi: 10.1093/Nar/Gkn680
    • (2009) Nucleic Acids Res , vol.37
    • Koua, D.1    Cerutti, L.2    Falquet, L.3    Sigrist, C.J.A.4    Theiler, G.5    Hulo, N.6    Dunand, C.7
  • 54
    • 1042288291 scopus 로고    scopus 로고
    • Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA
    • 10.1021/bi035920j 1:CAS:528:DC%2BD2cXlvFyjtg%3D%3D 10.1021/bi035920j
    • Kruger RG, Otvos B, Frankel BA, Bentley M, Dostal P, McCafferty DG (2004) Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA. Biochemistry 43:1541-1551. doi: 10.1021/bi035920j
    • (2004) Biochemistry , vol.43 , pp. 1541-1551
    • Kruger, R.G.1    Otvos, B.2    Frankel, B.A.3    Bentley, M.4    Dostal, P.5    McCafferty, D.G.6
  • 55
    • 1842408970 scopus 로고    scopus 로고
    • Production of restructured meat using microbial transglutaminase without salt or cooking
    • 10.1111/j.1365-2621.1997.tb04412.x 1:CAS:528:DyaK2sXjvVGrs7s%3D 10.1111/j.1365-2621.1997.tb04412.x
    • Kuraishi C, Sakamoto J, Yamazaki K, Susa Y, Kuhara C, Soeda T (1997) Production of restructured meat using microbial transglutaminase without salt or cooking. J Food Sci 62:488-490. doi: 10.1111/j.1365-2621.1997.tb04412.x
    • (1997) J Food Sci , vol.62 , pp. 488-490
    • Kuraishi, C.1    Sakamoto, J.2    Yamazaki, K.3    Susa, Y.4    Kuhara, C.5    Soeda, T.6
  • 56
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • 10.1081/FRI-100001258 1:CAS:528:DC%2BD3MXkslWisr8%3D 10.1081/FRI- 100001258
    • Kuraishi C, Yamazaki K, Susa Y (2001) Transglutaminase: its utilization in the food industry. Food Rev Int 17:221-246. doi: 10.1081/FRI-100001258
    • (2001) Food Rev Int , vol.17 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 57
    • 28444472469 scopus 로고    scopus 로고
    • Enzyme-aided modification of chicken-breast myofibril proteins: Effect of laccase and transglutaminase on gelation and thermal stability
    • 10.1021/Jf051602a 1:CAS:528:DC%2BD2MXhtV2jsLnJ 10.1021/jf051602a
    • Lantto R, Puolanne E, Kalkkinen N, Buchert J, Autio K (2005) Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability. J Agr Food Chem 53:9231-9237. doi: 10.1021/Jf051602a
    • (2005) J Agr Food Chem , vol.53 , pp. 9231-9237
    • Lantto, R.1    Puolanne, E.2    Kalkkinen, N.3    Buchert, J.4    Autio, K.5
  • 58
    • 84857990841 scopus 로고    scopus 로고
    • Influence of different pretreatments on the accessibility of transglutaminase and tyrosinase to wool fibre proteins
    • 10.1080/00405000.2010.544103 1:CAS:528:DC%2BC3MXhs1ert7%2FF 10.1080/00405000.2010.544103
    • Lantto R, Ellis J, Fatarella E, Cortez J (2012) Influence of different pretreatments on the accessibility of transglutaminase and tyrosinase to wool fibre proteins. J Text Inst 103:55-63. doi: 10.1080/00405000.2010.544103
    • (2012) J Text Inst , vol.103 , pp. 55-63
    • Lantto, R.1    Ellis, J.2    Fatarella, E.3    Cortez, J.4
  • 59
    • 33748786809 scopus 로고    scopus 로고
    • Overexpression of lysyl oxidase to increase matrix crosslinking and improve tissue strength in dermal wound healing
    • 10.1007/s10439-006-9130-8 10.1007/s10439-006-9130-8
    • Lau YKI, Gobin AM, West JL (2006) Overexpression of lysyl oxidase to increase matrix crosslinking and improve tissue strength in dermal wound healing. Ann Biomed Eng 34:1239-1246. doi: 10.1007/s10439-006-9130-8
    • (2006) Ann Biomed Eng , vol.34 , pp. 1239-1246
    • Lau, Y.K.I.1    Gobin, A.M.2    West, J.L.3
  • 60
    • 79953733187 scopus 로고    scopus 로고
    • Protein-protein fusion catalyzed by sortase A
    • 10.1371/journal.pone.0018342.g002 1:CAS:528:DC%2BC3MXltVWlsrk%3D 10.1371/journal.pone.0018342
    • Levary DA, Parthasarathy R, Boder ET, Ackerman ME (2011) Protein-protein fusion catalyzed by sortase A. PLoS One 6:e18342. doi: 10.1371/journal.pone. 0018342.g002
    • (2011) PLoS One , vol.6 , pp. 18342
    • Levary, D.A.1    Parthasarathy, R.2    Boder, E.T.3    Ackerman, M.E.4
  • 61
    • 79958787849 scopus 로고    scopus 로고
    • Influence of microbial transglutaminase modified gelatin-sodium caseinate, as a filler, on the subjective mechanical and structural properties of leather
    • 1:CAS:528:DC%2BC3MXos1KjtLs%3D
    • Liu Q, Liu L, Li J, Zhang D, Sun J, Du G, Chen J (2011) Influence of microbial transglutaminase modified gelatin-sodium caseinate, as a filler, on the subjective mechanical and structural properties of leather. J Am Leather Chem As 106:200-207
    • (2011) J Am Leather Chem As , vol.106 , pp. 200-207
    • Liu, Q.1    Liu, L.2    Li, J.3    Zhang, D.4    Sun, J.5    Du, G.6    Chen, J.7
  • 62
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • 10.1038/Nrm1014 1:CAS:528:DC%2BD3sXnsFaqtg%3D%3D 10.1038/nrm1014
    • Lorand L, Graham RM (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Bio 4:140-156. doi: 10.1038/Nrm1014
    • (2003) Nat Rev Mol Cell Bio , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 63
    • 33750437433 scopus 로고    scopus 로고
    • Lysyl oxidase: An oxidative enzyme and effector of cell function
    • 10.1007/s00018-006-6149-9 1:CAS:528:DC%2BD28XhtFyrtrrF 10.1007/s00018-006-6149-9
    • Lucero HA, Kagan HM (2006) Lysyl oxidase: an oxidative enzyme and effector of cell function. Cell Mol Life Sci 63:2304-2316. doi: 10.1007/s00018-006-6149-9
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2304-2316
    • Lucero, H.A.1    Kagan, H.M.2
  • 64
    • 0242323634 scopus 로고    scopus 로고
    • Expressed enzymatic ligation for the semisynthesis of chemically modified proteins
    • 10.1002/anie.200351774 1:CAS:528:DC%2BD3sXos1Oit7s%3D 10.1002/anie.200351774
    • Machova Z, von Eggelkraut-Gottanka R, Wehofsky N, Bordusa F, Beck-Sickinger AG (2003) Expressed enzymatic ligation for the semisynthesis of chemically modified proteins. Angew Chem Int Ed 42:4916-4918. doi: 10.1002/anie.200351774
    • (2003) Angew Chem Int Ed , vol.42 , pp. 4916-4918
    • MacHova, Z.1    Von Eggelkraut-Gottanka, R.2    Wehofsky, N.3    Bordusa, F.4    Beck-Sickinger, A.G.5
  • 65
    • 34250742375 scopus 로고    scopus 로고
    • Synthesis and resistance to in vitro proteolysis of transglutaminase cross-linked phaseolin, the major storage protein from Phaseolus vulgaris
    • 10.1021/Jf0637269 1:CAS:528:DC%2BD2sXls1SmtLo%3D 10.1021/jf0637269
    • Mariniello L, Giosafatto CVL, Di Pierro P, Sorrentino A, Porta R (2007) Synthesis and resistance to in vitro proteolysis of transglutaminase cross-linked phaseolin, the major storage protein from Phaseolus vulgaris. J Agr Food Chem 55:4717-4721. doi: 10.1021/Jf0637269
    • (2007) J Agr Food Chem , vol.55 , pp. 4717-4721
    • Mariniello, L.1    Giosafatto, C.V.L.2    Di Pierro, P.3    Sorrentino, A.4    Porta, R.5
  • 66
    • 77956514376 scopus 로고    scopus 로고
    • Swelling, mechanical, and barrier properties of albedo-based films prepared in the presence of phaseolin cross-linked or not by transglutaminase
    • 10.1021/Bm100566j 1:CAS:528:DC%2BC3cXhtVamtrnF 10.1021/bm100566j
    • Mariniello L, Giosafatto CVL, Di Pierro P, Sorrentino A, Porta R (2010) Swelling, mechanical, and barrier properties of albedo-based films prepared in the presence of phaseolin cross-linked or not by transglutaminase. Biomacromolecules 11:2394-2398. doi: 10.1021/Bm100566j
    • (2010) Biomacromolecules , vol.11 , pp. 2394-2398
    • Mariniello, L.1    Giosafatto, C.V.L.2    Di Pierro, P.3    Sorrentino, A.4    Porta, R.5
  • 67
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria
    • 10.1128/Mmbr.70.1.192-221.2006 1:CAS:528:DC%2BD28Xjs1Sgs78%3D 10.1128/MMBR.70.1.192-221.2006
    • Marraffini LA, DeDent AC, Schneewind O (2006) Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria. Microbiol Mol Biol Rev 70:192-221. doi: 10.1128/Mmbr.70.1.192-221.2006
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 68
    • 84986520447 scopus 로고
    • Modification of proteins by polyphenol oxidase and peroxidase and their products
    • 10.1111/j.1745-4514.1984.tb00322.x 1:CAS:528:DyaL2MXksVym 10.1111/j.1745-4514.1984.tb00322.x
    • Matheis G, Whitaker JR (1984a) Modification of proteins by polyphenol oxidase and peroxidase and their products. J Food Biochem 8:137-162. doi: 10.1111/j.1745-4514.1984.tb00322.x
    • (1984) J Food Biochem , vol.8 , pp. 137-162
    • Matheis, G.1    Whitaker, J.R.2
  • 69
    • 0021192057 scopus 로고
    • Peroxidase-catalyzed cross linking of proteins
    • 10.1007/BF01024835 1:CAS:528:DyaL2cXltV2isrs%3D 10.1007/BF01024835
    • Matheis G, Whitaker JR (1984b) Peroxidase-catalyzed cross linking of proteins. J Protein Chem 3:35-48. doi: 10.1007/BF01024835
    • (1984) J Protein Chem , vol.3 , pp. 35-48
    • Matheis, G.1    Whitaker, J.R.2
  • 70
    • 33751267287 scopus 로고    scopus 로고
    • Effect of protein structure on laccase-catalyzed protein oligomerization
    • 10.1021/Jf062397h 1:CAS:528:DC%2BD28XhtFSlsLrP 10.1021/jf062397h
    • Mattinen ML, Hellman M, Permi P, Autio K, Kalkkinen N, Buchert J (2006) Effect of protein structure on laccase-catalyzed protein oligomerization. J Agr Food Chem 54:8883-8890. doi: 10.1021/Jf062397h
    • (2006) J Agr Food Chem , vol.54 , pp. 8883-8890
    • Mattinen, M.L.1    Hellman, M.2    Permi, P.3    Autio, K.4    Kalkkinen, N.5    Buchert, J.6
  • 71
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: New functions for an old enzyme
    • 10.1016/S0031-9422(02)00171-1 1:CAS:528:DC%2BD38Xlt1Ois7w%3D 10.1016/S0031-9422(02)00171-1
    • Mayer AM, Staples RC (2002) Laccase: new functions for an old enzyme. Phytochemistry 60:551-565. doi: 10.1016/S0031-9422(02)00171-1
    • (2002) Phytochemistry , vol.60 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 72
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • 10.1126/science.285.5428.760 1:CAS:528:DyaK1MXltVehu7Y%3D 10.1126/science.285.5428.760
    • Mazmanian SK, Liu G, Ton-That H, Schneewind O (1999) Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285:760-763. doi: 10.1126/science.285.5428.760
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 73
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking
    • 1:CAS:528:DC%2BD2cXpvFOntL8%3D
    • Migneault I, Dartiguenave C, Bertrand MJ, Waldron KC (2004) Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. Biotechniques 37:790-802
    • (2004) Biotechniques , vol.37 , pp. 790-802
    • Migneault, I.1    Dartiguenave, C.2    Bertrand, M.J.3    Waldron, K.C.4
  • 74
    • 81255143187 scopus 로고    scopus 로고
    • Protein heteroconjugation by the peroxidase-catalyzed tyrosine coupling reaction
    • 10.1021/bc200420v 1:CAS:528:DC%2BC3MXhtlajtbnO 10.1021/bc200420v
    • Minamihata K, Goto M, Kamiya N (2011) Protein heteroconjugation by the peroxidase-catalyzed tyrosine coupling reaction. Bioconjugate Chem 22:2332-2338. doi: 10.1021/bc200420v
    • (2011) Bioconjugate Chem , vol.22 , pp. 2332-2338
    • Minamihata, K.1    Goto, M.2    Kamiya, N.3
  • 75
    • 79960483875 scopus 로고    scopus 로고
    • In vitro sortagging of an antibody Fab fragment: Overcoming unproductive reactions of sortase with water and lysine side chains
    • 10.1002/cbic.201100002 10.1002/cbic.201100002 1:CAS:528: DC%2BC3MXntV2qur0%3D
    • Möhlmann S, Mahlert C, Greven S, Scholz P, Harrenga A (2011) In vitro sortagging of an antibody Fab fragment: overcoming unproductive reactions of sortase with water and lysine side chains. Chembiochem 12:1774-1780. doi: 10.1002/cbic.201100002
    • (2011) Chembiochem , vol.12 , pp. 1774-1780
    • Möhlmann, S.1    Mahlert, C.2    Greven, S.3    Scholz, P.4    Harrenga, A.5
  • 76
    • 81455135444 scopus 로고    scopus 로고
    • Treatment of bleached wool with trans-glutaminases to enhance tensile strength, whiteness, and alkali resistance
    • 10.1007/s12010-011-9293-0 1:CAS:528:DC%2BC3MXht1WqtbvK 10.1007/s12010-011-9293-0
    • Montazer M, Lessan F, Pajootan E, Dadashian F (2011) Treatment of bleached wool with trans-glutaminases to enhance tensile strength, whiteness, and alkali resistance. Appl Biochem Biotech 165:748-759. doi: 10.1007/s12010-011-9293-0
    • (2011) Appl Biochem Biotech , vol.165 , pp. 748-759
    • Montazer, M.1    Lessan, F.2    Pajootan, E.3    Dadashian, F.4
  • 77
    • 83355177973 scopus 로고    scopus 로고
    • Enzyme-catalyzed crosslinkable hydrogels: Emerging strategies for tissue engineering
    • 10.1016/j.biomaterials.2011.10.067 1:CAS:528:DC%2BC3MXhsF2ltrnE 10.1016/j.biomaterials.2011.10.067
    • Moreira Teixeira LS, Feijen J, van Blitterswijk CA, Dijkstra PJ, Karperien M (2012) Enzyme-catalyzed crosslinkable hydrogels: emerging strategies for tissue engineering. Biomaterials 33:1281-1290. doi: 10.1016/j.biomaterials. 2011.10.067
    • (2012) Biomaterials , vol.33 , pp. 1281-1290
    • Moreira Teixeira, L.S.1    Feijen, J.2    Van Blitterswijk, C.A.3    Dijkstra, P.J.4    Karperien, M.5
  • 78
    • 0000633489 scopus 로고    scopus 로고
    • Recent trends in transglutaminase technology for food processing
    • 10.3136/fstr.6.151 1:CAS:528:DC%2BD3cXot1Sqsbg%3D 10.3136/fstr.6.151
    • Motoki M, Kumazawa Y (2000) Recent trends in transglutaminase technology for food processing. Food Sci Technol Res 6:151-160. doi: 10.3136/fstr.6.151
    • (2000) Food Sci Technol Res , vol.6 , pp. 151-160
    • Motoki, M.1    Kumazawa, Y.2
  • 80
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • 10.1038/Nmeth886 1:CAS:528:DC%2BD28XkvVWksrw%3D 10.1038/nmeth886
    • Muralidharan V, Muir TW (2006) Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat Methods 3:429-438. doi: 10.1038/Nmeth886
    • (2006) Nat Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 81
    • 33644636333 scopus 로고    scopus 로고
    • Gelatin based microfluidic devices for cell culture
    • 10.1039/b517524k 1:CAS:528:DC%2BD28XhvVKhurs%3D 10.1039/b517524k
    • Paguirigan A, Beebe DJ (2006) Gelatin based microfluidic devices for cell culture. Lab Chip 6:407-413. doi: 10.1039/b517524k
    • (2006) Lab Chip , vol.6 , pp. 407-413
    • Paguirigan, A.1    Beebe, D.J.2
  • 82
    • 33947664974 scopus 로고    scopus 로고
    • Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation
    • 10.1021/Bc060339w 1:CAS:528:DC%2BD2sXhslaisLg%3D 10.1021/bc060339w
    • Parthasarathy R, Subramanian S, Boder ET (2007) Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation. Bioconjugate Chem 18:469-476. doi: 10.1021/Bc060339w
    • (2007) Bioconjugate Chem , vol.18 , pp. 469-476
    • Parthasarathy, R.1    Subramanian, S.2    Boder, E.T.3
  • 83
    • 0032212390 scopus 로고    scopus 로고
    • Bacterial pro-transglutaminase from Streptoverticillium mobaraense - Purification, characterisation and sequence of the zymogen
    • 10.1046/j.1432-1327.1998.2570570.x 1:CAS:528:DyaK1cXntlejsb0%3D 10.1046/j.1432-1327.1998.2570570.x
    • Pasternack R, Dorsch S, Otterbach JT, Robenek IR, Wolf S, Fuchsbauer HL (1998) Bacterial pro-transglutaminase from Streptoverticillium mobaraense - purification, characterisation and sequence of the zymogen. Eur J Biochem 257:570-576. doi: 10.1046/j.1432-1327.1998.2570570.x
    • (1998) Eur J Biochem , vol.257 , pp. 570-576
    • Pasternack, R.1    Dorsch, S.2    Otterbach, J.T.3    Robenek, I.R.4    Wolf, S.5    Fuchsbauer, H.L.6
  • 84
    • 79956154315 scopus 로고    scopus 로고
    • Making and breaking peptide bonds: Protein engineering using sortase
    • 10.1002/anie.201008267 1:CAS:528:DC%2BC3MXmtFymu7g%3D 10.1002/anie.201008267
    • Popp MWL, Ploegh HL (2011) Making and breaking peptide bonds: protein engineering using sortase. Angew Chem Int Ed 50:5024-5032. doi: 10.1002/anie.201008267
    • (2011) Angew Chem Int Ed , vol.50 , pp. 5024-5032
    • Popp, M.W.L.1    Ploegh, H.L.2
  • 85
    • 65249086717 scopus 로고    scopus 로고
    • Site-specific protein labeling via sortase-mediated transpeptidation
    • 10.1002/0471140864.ps1503s56
    • Popp MWL, Antos JM, Ploegh HL (2009) Site-specific protein labeling via sortase-mediated transpeptidation. Curr Protoc Protein Sci 15:3.1-15.3.9. doi: 10.1002/0471140864.ps1503s56
    • (2009) Curr Protoc Protein Sci , vol.15 , pp. 31-39
    • Popp, M.W.L.1    Antos, J.M.2    Ploegh, H.L.3
  • 86
    • 34447310586 scopus 로고    scopus 로고
    • Shall we dance? How a multicopper oxidase chooses its electron transfer partner
    • 10.1021/Ar600051a 1:CAS:528:DC%2BD2sXkvFaltL0%3D 10.1021/ar600051a
    • Quintanar L, Stoj C, Taylor AB, Hart PJ, Kosman DJ, Solomon EI (2007) Shall we dance? How a multicopper oxidase chooses its electron transfer partner. Acc Chem Res 40:445-452. doi: 10.1021/Ar600051a
    • (2007) Acc Chem Res , vol.40 , pp. 445-452
    • Quintanar, L.1    Stoj, C.2    Taylor, A.B.3    Hart, P.J.4    Kosman, D.J.5    Solomon, E.I.6
  • 87
    • 78951481967 scopus 로고    scopus 로고
    • Bacillus pumilus laccase: A heat stable enzyme with a wide substrate spectrum
    • 10.1186/1472-6750-11-9 1:CAS:528:DC%2BC3MXhvFansbk%3D 10.1186/1472-6750-11-9
    • Reiss R, Ihssen J, Thöny-Meyer L (2011) Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC Biotechnol 11:9. doi: 10.1186/1472-6750-11-9
    • (2011) BMC Biotechnol , vol.11 , pp. 9
    • Reiss, R.1    Ihssen, J.2    Thöny-Meyer, L.3
  • 88
    • 80052797352 scopus 로고    scopus 로고
    • Expression of industrially relevant laccases: Prokaryotic style
    • 10.1016/j.tibtech.2011.04.005 1:CAS:528:DC%2BC3MXhtFynsbzM 10.1016/j.tibtech.2011.04.005
    • Santhanam N, Vivanco JM, Decker SR, Reardon KF (2011) Expression of industrially relevant laccases: prokaryotic style. Trends Biotechnol 29:480-489. doi: 10.1016/j.tibtech.2011.04.005
    • (2011) Trends Biotechnol , vol.29 , pp. 480-489
    • Santhanam, N.1    Vivanco, J.M.2    Decker, S.R.3    Reardon, K.F.4
  • 90
    • 34547799272 scopus 로고    scopus 로고
    • Elucidating the mechanism of laccase and tyrosinase in wheat bread making
    • 10.1021/Jf0703349 1:CAS:528:DC%2BD2sXmvFKqsLw%3D 10.1021/jf0703349
    • Selinheimo E, Autio K, Krijus K, Buchert J (2007a) Elucidating the mechanism of laccase and tyrosinase in wheat bread making. J Agr Food Chem 55:6357-6365. doi: 10.1021/Jf0703349
    • (2007) J Agr Food Chem , vol.55 , pp. 6357-6365
    • Selinheimo, E.1    Autio, K.2    Krijus, K.3    Buchert, J.4
  • 92
    • 47649091159 scopus 로고    scopus 로고
    • Transglutaminases: Widespread cross-linking enzymes in plants
    • 10.1093/Aob/Mcn075 1:CAS:528:DC%2BD1cXhtVars77K 10.1093/aob/mcn075
    • Serafini-Fracassini D, Del Duca S (2008) Transglutaminases: widespread cross-linking enzymes in plants. Ann Bot London 102:145-152. doi: 10.1093/Aob/Mcn075
    • (2008) Ann Bot London , vol.102 , pp. 145-152
    • Serafini-Fracassini, D.1    Del Duca, S.2
  • 93
    • 0035209417 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking
    • 10.1016/S0958-6946(01)00096-6 1:CAS:528:DC%2BD3MXnsF2jtr4%3D 10.1016/S0958-6946(01)00096-6
    • Sharma R, Lorenzen PC, Qvist KB (2001) Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. Int Dairy J 11:785-793. doi: 10.1016/S0958-6946(01)00096-6
    • (2001) Int Dairy J , vol.11 , pp. 785-793
    • Sharma, R.1    Lorenzen, P.C.2    Qvist, K.B.3
  • 94
    • 82355169635 scopus 로고    scopus 로고
    • Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs)
    • 10.1007/s00253-011-3554-2 1:CAS:528:DC%2BC3MXht1yhurrP 10.1007/s00253-011-3554-2
    • Sheldon RA (2011) Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl Microbiol Biotechnol 92:467-477. doi: 10.1007/s00253-011-3554-2
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 467-477
    • Sheldon, R.A.1
  • 95
    • 0000959875 scopus 로고
    • Modification of food proteins by covalent crosslinking
    • 10.1016/0924-2244(91)90683-A 1:CAS:528:DyaK38Xhslanurc%3D 10.1016/0924-2244(91)90683-A
    • Singh H (1991) Modification of food proteins by covalent crosslinking. Trends Food Sci Technol 2:196-200. doi: 10.1016/0924-2244(91)90683-A
    • (1991) Trends Food Sci Technol , vol.2 , pp. 196-200
    • Singh, H.1
  • 96
    • 77949300622 scopus 로고    scopus 로고
    • Ligninolytic fungal laccases and their biotechnological applications
    • 10.1007/s12010-009-8676-y 10.1007/s12010-009-8676-y 1:CAS:528: DC%2BC3cXktVWmtb8%3D
    • Singh Arora D, Kumar Sharma R (2010) Ligninolytic fungal laccases and their biotechnological applications. Appl Biochem Biotechnol 160:1760-1788. doi: 10.1007/s12010-009-8676-y
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 1760-1788
    • Singh Arora, D.1    Kumar Sharma, R.2
  • 97
    • 0036451802 scopus 로고    scopus 로고
    • Peroxidase-catalyzed crosslinking of functionalized polyaspartic acid polymers
    • 10.1081/Ma-120014843 10.1081/MA-120014843 1:CAS:528:DC%2BD38XotlCiu7Y%3D
    • Sofia SJ, Singh A, Kaplan DL (2002) Peroxidase-catalyzed crosslinking of functionalized polyaspartic acid polymers. J Macromol Sci Part A: Pure Appl Chem 39:1151-1181. doi: 10.1081/Ma-120014843
    • (2002) J Macromol Sci Part A: Pure Appl Chem , vol.39 , pp. 1151-1181
    • Sofia, S.J.1    Singh, A.2    Kaplan, D.L.3
  • 98
    • 84863698636 scopus 로고    scopus 로고
    • Chemistry and biology of the ubiquitin signal
    • 10.1002/anie.201200020 10.1002/anie.201200020 1:CAS:528: DC%2BC38Xos1anu7Y%3D
    • Spasser L, Brik A (2012) Chemistry and biology of the ubiquitin signal. Angew Chem Int Ed 51:2-25. doi: 10.1002/anie.201200020
    • (2012) Angew Chem Int Ed , vol.51 , pp. 2-25
    • Spasser, L.1    Brik, A.2
  • 99
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • 10.1111/j.1365-2958.2011.07887.x 1:CAS:528:DC%2BC3MXhs1antrvF 10.1111/j.1365-2958.2011.07887.x
    • Spirig T, Weiner EM, Clubb RT (2011) Sortase enzymes in Gram-positive bacteria. Mol Microbiol 82:1044-1059. doi: 10.1111/j.1365-2958.2011.07887.x
    • (2011) Mol Microbiol , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 101
    • 58849160125 scopus 로고    scopus 로고
    • Cross-linking proteins by laccase-catalyzed oxidation: Importance relative to other modifications
    • 10.1021/jf801234v 1:CAS:528:DC%2BD1cXhsVShsL3M 10.1021/jf801234v
    • Steffensen CL, Andersen ML, Degn PE, Nielsen JH (2008) Cross-linking proteins by laccase-catalyzed oxidation: importance relative to other modifications. J Agric Food Chem 56:12002-12010. doi: 10.1021/jf801234v
    • (2008) J Agric Food Chem , vol.56 , pp. 12002-12010
    • Steffensen, C.L.1    Andersen, M.L.2    Degn, P.E.3    Nielsen, J.H.4
  • 102
    • 77953127870 scopus 로고    scopus 로고
    • Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
    • 10.1016/j.jcs.2010.01.010 1:CAS:528:DC%2BC3cXmsVeksr0%3D 10.1016/j.jcs.2010.01.010
    • Steffolani ME, Ribotta PD, Pérez GT, León AE (2010) Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: relationship with dough properties and bread-making quality. J Cereal Sci 51:366-373. doi: 10.1016/j.jcs.2010.01.010
    • (2010) J Cereal Sci , vol.51 , pp. 366-373
    • Steffolani, M.E.1    Ribotta, P.D.2    Pérez, G.T.3    León, A.E.4
  • 103
    • 79961024763 scopus 로고    scopus 로고
    • Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking
    • 10.1016/j.jfoodeng.2011.06.019 1:CAS:528:DC%2BC3MXpvFyjsb8%3D 10.1016/j.jfoodeng.2011.06.019
    • Sun XD, Arntfield SD (2011) Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking. J Food Eng 107:226-233. doi: 10.1016/j.jfoodeng.2011.06.019
    • (2011) J Food Eng , vol.107 , pp. 226-233
    • Sun, X.D.1    Arntfield, S.D.2
  • 105
    • 2442683103 scopus 로고    scopus 로고
    • Enzymatic labeling of a single chain variable fragment of an antibody with alkaline phosphatase by mircobial transglutaminase
    • 10.1002/Bit.20019 1:CAS:528:DC%2BD2cXjslGju70%3D 10.1002/bit.20019
    • Takazawa T, Kamiya N, Ueda H, Nagamune T (2004) Enzymatic labeling of a single chain variable fragment of an antibody with alkaline phosphatase by mircobial transglutaminase. Biotechnol Bioeng 86:399-404. doi: 10.1002/Bit.20019
    • (2004) Biotechnol Bioeng , vol.86 , pp. 399-404
    • Takazawa, T.1    Kamiya, N.2    Ueda, H.3    Nagamune, T.4
  • 106
    • 2442679406 scopus 로고    scopus 로고
    • Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase
    • 10.1021/Bc034209o 1:CAS:528:DC%2BD2cXjsFGgsrc%3D 10.1021/bc034209o
    • Tanaka T, Kamiya N, Nagamune T (2004) Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase. Bioconjugate Chem 15:491-497. doi: 10.1021/Bc034209o
    • (2004) Bioconjugate Chem , vol.15 , pp. 491-497
    • Tanaka, T.1    Kamiya, N.2    Nagamune, T.3
  • 107
    • 34248394391 scopus 로고    scopus 로고
    • Evaluation of polymers prepared from gelatin and casein or whey as potential fillers
    • 1:CAS:528:DC%2BD2sXlt1Grsbg%3D
    • Taylor MM, Marmer WN, Brown EM (2007) Evaluation of polymers prepared from gelatin and casein or whey as potential fillers. J Am Leather Chem As 102:111-120
    • (2007) J Am Leather Chem As , vol.102 , pp. 111-120
    • Taylor, M.M.1    Marmer, W.N.2    Brown, E.M.3
  • 108
    • 71049156732 scopus 로고    scopus 로고
    • Treatment of low-quality hides with fillers produced from sustainable resources: Effect on properties of leather
    • 1:CAS:528:DC%2BD1MXhtlCnsL%2FL
    • Taylor MM, Lee J, Bumanlag LP, Cooke PH, Brown EM, Hernandez Balada E (2009) Treatment of low-quality hides with fillers produced from sustainable resources: effect on properties of leather. J Am Leather Chem As 104:324-334
    • (2009) J Am Leather Chem As , vol.104 , pp. 324-334
    • Taylor, M.M.1    Lee, J.2    Bumanlag, L.P.3    Cooke, P.H.4    Brown, E.M.5    Hernandez Balada, E.6
  • 109
    • 13244252815 scopus 로고    scopus 로고
    • Enzymatic cross-linking of proteins with tyrosinase
    • 10.1007/s00217-001-0455-0 1:CAS:528:DC%2BD38XjvFSjtrc%3D 10.1007/s00217-001-0455-0
    • Thalmann CR, Lötzbeyer T (2002) Enzymatic cross-linking of proteins with tyrosinase. Eur Food Res Technol 214:276-281. doi: 10.1007/s00217-001-0455- 0
    • (2002) Eur Food Res Technol , vol.214 , pp. 276-281
    • Thalmann, C.R.1    Lötzbeyer, T.2
  • 110
    • 65549164210 scopus 로고    scopus 로고
    • Sortase-mediated ligation: A gift from Gram-positive bacteria to protein engineering
    • 10.1002/cbic.200800724 1:CAS:528:DC%2BD1MXktVajt7o%3D 10.1002/cbic.200800724
    • Tsukiji S, Nagamune T (2009) Sortase-mediated ligation: a gift from Gram-positive bacteria to protein engineering. Chembiochem 10:787-798. doi: 10.1002/cbic.200800724
    • (2009) Chembiochem , vol.10 , pp. 787-798
    • Tsukiji, S.1    Nagamune, T.2
  • 111
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: A modern view of a classic enzyme
    • 10.1016/j.phytochem.2003.10.022 1:CAS:528:DC%2BD2cXmvFGntA%3D%3D 10.1016/j.phytochem.2003.10.022
    • Veitch NC (2004) Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 65:249-259. doi: 10.1016/j.phytochem.2003.10.022
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 113
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • 10.1002/anie.200501023 1:CAS:528:DC%2BD2MXhtlSms77N 10.1002/anie. 200501023
    • Walsh CT, Garneau-Tsodikova S, Gatto GJ (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed 44:7342-7372. doi: 10.1002/anie.200501023
    • (2005) Angew Chem Int Ed , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.3
  • 114
    • 77949916023 scopus 로고    scopus 로고
    • Antibacterial functionalization of wool via mTGase-catalyzed grafting of ε-poly-l-lysine
    • 10.1007/s12010-009-8708-7 1:CAS:528:DC%2BC3cXkt12nt7s%3D 10.1007/s12010-009-8708-7
    • Wang Q, Jin G, Fan X, Zhao X, Cui L, Wang P (2010) Antibacterial functionalization of wool via mTGase-catalyzed grafting of ε-poly-l-lysine. Appl Biochem Biotechnol 160:2486-2497. doi: 10.1007/s12010-009-8708-7
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 2486-2497
    • Wang, Q.1    Jin, G.2    Fan, X.3    Zhao, X.4    Cui, L.5    Wang, P.6
  • 115
    • 80053329313 scopus 로고    scopus 로고
    • The combined use of cutinase, keratinase and protease treatments for wool bio-antifelting
    • 10.1007/s12221-011-0760-6 1:CAS:528:DC%2BC3MXht1GiurrO 10.1007/s12221-011-0760-6
    • Wang P, Wang Q, Cui L, Gao M, Fan X (2011) The combined use of cutinase, keratinase and protease treatments for wool bio-antifelting. Fiber Polym 12:760-764. doi: 10.1007/s12221-011-0760-6
    • (2011) Fiber Polym , vol.12 , pp. 760-764
    • Wang, P.1    Wang, Q.2    Cui, L.3    Gao, M.4    Fan, X.5
  • 116
    • 80051978811 scopus 로고    scopus 로고
    • The predator becomes the prey: Regulating the ubiquitin system by ubiquitylation and degradation
    • 10.1038/Nrm3191 1:CAS:528:DC%2BC3MXhtVGlu7fO 10.1038/nrm3173
    • Weissman AM, Shabek N, Ciechanover A (2011) The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation. Nat Rev Mol Cell Bio 12:605-620. doi: 10.1038/Nrm3191
    • (2011) Nat Rev Mol Cell Bio , vol.12 , pp. 605-620
    • Weissman, A.M.1    Shabek, N.2    Ciechanover, A.3
  • 118
    • 67549089664 scopus 로고    scopus 로고
    • Synthetic applications of laccase in green chemistry
    • 10.1002/adsc.200800775 1:CAS:528:DC%2BD1MXos1artbk%3D 10.1002/adsc.200800775
    • Witayakran S, Ragauskas AJ (2009) Synthetic applications of laccase in green chemistry. Adv Synth Catal 351:1187-1209. doi: 10.1002/adsc.200800775
    • (2009) Adv Synth Catal , vol.351 , pp. 1187-1209
    • Witayakran, S.1    Ragauskas, A.J.2
  • 120
    • 43549095197 scopus 로고    scopus 로고
    • Glucose oxidase: Natural occurrence, function, properties and industrial applications
    • 10.1007/s00253-008-1407-4 1:CAS:528:DC%2BD1cXkvFagtLw%3D 10.1007/s00253-008-1407-4
    • Wong CM, Wong KH, Chen XD (2008) Glucose oxidase: natural occurrence, function, properties and industrial applications. Appl Microbiol Biotechnol 78:927-938. doi: 10.1007/s00253-008-1407-4
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 927-938
    • Wong, C.M.1    Wong, K.H.2    Chen, X.D.3
  • 121
    • 29844457552 scopus 로고    scopus 로고
    • Quality of dried white salted noodles affected by microbial transglutaminase
    • 10.1002/Jsfa.2311 1:CAS:528:DC%2BD2MXht1Grt7%2FL 10.1002/jsfa.2311
    • Wu J, Corke H (2005) Quality of dried white salted noodles affected by microbial transglutaminase. J Sci Food Agric 85:2587-2594. doi: 10.1002/Jsfa.2311
    • (2005) J Sci Food Agric , vol.85 , pp. 2587-2594
    • Wu, J.1    Corke, H.2
  • 122
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • 10.1007/s00253-003-1539-5 1:CAS:528:DC%2BD2cXjtFyis7w%3D 10.1007/s00253-003-1539-5
    • Yokoyama K, Nio N, Kikuchi Y (2004) Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol 64:447-454. doi: 10.1007/s00253-003-1539-5
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 123
    • 36849001355 scopus 로고    scopus 로고
    • Transglutaminase crosslinked gelatin as a tissue engineering scaffold
    • 10.1002/Jbm.A.31431 1:CAS:528:DC%2BD2sXhsValt7bO 10.1002/jbm.a.31431
    • Yung CW, Wu LQ, Tullman JA, Payne GF, Bentley WE, Barbari TA (2007) Transglutaminase crosslinked gelatin as a tissue engineering scaffold. J Biomed Mater Res A 83A:1039-1046. doi: 10.1002/Jbm.A.31431
    • (2007) J Biomed Mater Res A , vol.83 , pp. 1039-1046
    • Yung, C.W.1    Wu, L.Q.2    Tullman, J.A.3    Payne, G.F.4    Bentley, W.E.5    Barbari, T.A.6
  • 124
    • 77956486047 scopus 로고    scopus 로고
    • Diffusion of interleukin-2 from cells overlaid with cytocompatible enzyme-crosslinked gelatin hydrogels
    • 10.1002/Jbm.A.32740 1:CAS:528:DC%2BC3cXhtVKltLzF 10.1002/jbm.a.32740
    • Yung CW, Bentley WE, Barbari TA (2010) Diffusion of interleukin-2 from cells overlaid with cytocompatible enzyme-crosslinked gelatin hydrogels. J Biomed Mater Res A 95A:25-32. doi: 10.1002/Jbm.A.32740
    • (2010) J Biomed Mater Res A , vol.95 , pp. 25-32
    • Yung, C.W.1    Bentley, W.E.2    Barbari, T.A.3
  • 125
    • 51249102955 scopus 로고    scopus 로고
    • Novel applications for microbial transglutaminase beyond food processing
    • 10.1016/j.tibtech.2008.06.006 1:CAS:528:DC%2BD1cXhtFajurvF 10.1016/j.tibtech.2008.06.006
    • Zhu Y, Tramper J (2008) Novel applications for microbial transglutaminase beyond food processing. Trends Biotechnol 26:559-565. doi: 10.1016/j.tibtech. 2008.06.006
    • (2008) Trends Biotechnol , vol.26 , pp. 559-565
    • Zhu, Y.1    Tramper, J.2
  • 126
    • 27744587880 scopus 로고    scopus 로고
    • Assembly and function of a spore coat-associated transglutaminase of Bacillus subtilis
    • 10.1128/Jb.187.22.7753-7764.2005 10.1128/JB.187.22.7753-7764.2005 1:CAS:528:DC%2BD2MXht1WnurfK
    • Zilhão R, Isticato R, Martins LO, Steil L, Völker U, Ricca E, Moran CP, Henriques AO (2005) Assembly and function of a spore coat-associated transglutaminase of Bacillus subtilis. J Bacteriol 187:7753-7764. doi: 10.1128/Jb.187.22.7753-7764.2005
    • (2005) J Bacteriol , vol.187 , pp. 7753-7764
    • Zilhão, R.1    Isticato, R.2    Martins, L.O.3    Steil, L.4    Völker, U.5    Ricca, E.6    Moran, C.P.7    Henriques, A.O.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.