메뉴 건너뛰기




Volumn 38, Issue , 2016, Pages 1-9

Modular construction of multi-subunit protein complexes using engineered tags and microbial transglutaminase

Author keywords

Biofabrication; Metabolon; Protein complex; Quorum sensing; Transglutaminase

Indexed keywords

AMINO ACIDS; ANTIBODIES; BIOCHEMISTRY; BIOSYNTHESIS; DISPLAY DEVICES; ENZYMES; HYDROGELS; MODULAR CONSTRUCTION; STOICHIOMETRY;

EID: 84976407600     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2016.05.004     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 84976388347 scopus 로고    scopus 로고
    • Analyzing biochemical flux generated from enzyme complexes built using modular construction approach
    • (Submitted for publication)
    • Bhokisham N., et al. Analyzing biochemical flux generated from enzyme complexes built using modular construction approach. Data in Brief 2016, (Submitted for publication).
    • (2016) Data in Brief
    • Bhokisham, N.1
  • 2
    • 0021276488 scopus 로고
    • Purification and some properties of streptococcal protein G, a novel IgG-binding reagent
    • Björck L., Kronvall G. Purification and some properties of streptococcal protein G, a novel IgG-binding reagent. J. Immunol. 1984, 133(2):969-974.
    • (1984) J. Immunol. , vol.133 , Issue.2 , pp. 969-974
    • Björck, L.1    Kronvall, G.2
  • 3
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilisation
    • Brady D., Jordaan J. Advances in enzyme immobilisation. Biotechnol. Lett. 2009, 31(11):1639-1650.
    • (2009) Biotechnol. Lett. , vol.31 , Issue.11 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 4
    • 33845910922 scopus 로고    scopus 로고
    • Lab-on-a-chip devices for global health: past studies and future opportunities
    • Chin C.D., Linder V., Sia S.K. Lab-on-a-chip devices for global health: past studies and future opportunities. Lab Chip 2007, 7(1):41-57.
    • (2007) Lab Chip , vol.7 , Issue.1 , pp. 41-57
    • Chin, C.D.1    Linder, V.2    Sia, S.K.3
  • 5
    • 0032481609 scopus 로고    scopus 로고
    • Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product
    • Cornell K.A., Riscoe M.K. Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product. Biochim. Biophys. Acta 1998, 1396(1):8-14.
    • (1998) Biochim. Biophys. Acta , vol.1396 , Issue.1 , pp. 8-14
    • Cornell, K.A.1    Riscoe, M.K.2
  • 6
    • 33644777646 scopus 로고    scopus 로고
    • Lab-on-a-chip: microfluidics in drug discovery
    • Dittrich P.S., Manz A. Lab-on-a-chip: microfluidics in drug discovery. Nat. Rev. Drug Discov. 2006, 5(3):210-218.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , Issue.3 , pp. 210-218
    • Dittrich, P.S.1    Manz, A.2
  • 7
    • 68449088806 scopus 로고    scopus 로고
    • Synthetic protein scaffolds provide modular control over metabolic flux
    • Dueber J.E., et al. Synthetic protein scaffolds provide modular control over metabolic flux. Nat. Biotechnol. 2009, 27(8):753-759.
    • (2009) Nat. Biotechnol. , vol.27 , Issue.8 , pp. 753-759
    • Dueber, J.E.1
  • 8
    • 77949270750 scopus 로고    scopus 로고
    • Engineered biological nanofactories trigger quorum sensing response in targeted bacteria
    • Fernandes R., et al. Engineered biological nanofactories trigger quorum sensing response in targeted bacteria. Nat. Nanotechnol. 2010, 5(3):213-217.
    • (2010) Nat. Nanotechnol. , vol.5 , Issue.3 , pp. 213-217
    • Fernandes, R.1
  • 9
    • 77950836054 scopus 로고    scopus 로고
    • Biological nanofactories facilitate spatially selective capture and manipulation of quorum sensing bacteria in a bioMEMS device
    • Fernandes R., et al. Biological nanofactories facilitate spatially selective capture and manipulation of quorum sensing bacteria in a bioMEMS device. Lab Chip 2010, 10(9):1128-1134.
    • (2010) Lab Chip , vol.10 , Issue.9 , pp. 1128-1134
    • Fernandes, R.1
  • 10
    • 84905818967 scopus 로고    scopus 로고
    • Electronic modulation of biochemical signal generation
    • Gordonov T., et al. Electronic modulation of biochemical signal generation. Nat. Nanotechnol. 2014, 9(8):605-610.
    • (2014) Nat. Nanotechnol. , vol.9 , Issue.8 , pp. 605-610
    • Gordonov, T.1
  • 11
    • 34548077793 scopus 로고    scopus 로고
    • Microfluidic platforms for lab-on-a-chip applications
    • Haeberle S., Zengerle R. Microfluidic platforms for lab-on-a-chip applications. Lab Chip 2007, 7(9):1094-1110.
    • (2007) Lab Chip , vol.7 , Issue.9 , pp. 1094-1110
    • Haeberle, S.1    Zengerle, R.2
  • 12
    • 62449121836 scopus 로고    scopus 로고
    • Understanding enzyme immobilisation
    • Hanefeld U., Gardossi L., Magner E. Understanding enzyme immobilisation. Chem. Soc. Rev. 2009, 38(2):453-468.
    • (2009) Chem. Soc. Rev. , vol.38 , Issue.2 , pp. 453-468
    • Hanefeld, U.1    Gardossi, L.2    Magner, E.3
  • 13
    • 0035949513 scopus 로고    scopus 로고
    • Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site
    • Hilgers M.T., Ludwig M.L. Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site. Proc. Natl. Acad. Sci. USA 2001, 98(20):11169-11174.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.20 , pp. 11169-11174
    • Hilgers, M.T.1    Ludwig, M.L.2
  • 14
    • 35348837263 scopus 로고    scopus 로고
    • Intramolecular electron transfer in a cytochrome P450cam system with a site-specific branched structure
    • Hirakawa H., et al. Intramolecular electron transfer in a cytochrome P450cam system with a site-specific branched structure. Protein Eng. Des. Sel. 2007, 20(9):453-459.
    • (2007) Protein Eng. Des. Sel. , vol.20 , Issue.9 , pp. 453-459
    • Hirakawa, H.1
  • 15
    • 79955037982 scopus 로고    scopus 로고
    • Transglutaminase-mediated synthesis of a DNA-(Enzyme)n probe for highly sensitive DNA detection
    • Kitaoka M., et al. Transglutaminase-mediated synthesis of a DNA-(Enzyme)n probe for highly sensitive DNA detection. Chem. Eur. J. 2011, 17(19):5387-5392.
    • (2011) Chem. Eur. J. , vol.17 , Issue.19 , pp. 5387-5392
    • Kitaoka, M.1
  • 16
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller K.M., Wong C.-H. Enzymes for chemical synthesis. Nature 2001, 409(6817):232-240.
    • (2001) Nature , vol.409 , Issue.6817 , pp. 232-240
    • Koeller, K.M.1    Wong, C.-H.2
  • 17
    • 0034793650 scopus 로고    scopus 로고
    • Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases
    • Lee J.E., et al. Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure 2001, 9(10):941-953.
    • (2001) Structure , vol.9 , Issue.10 , pp. 941-953
    • Lee, J.E.1
  • 18
    • 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., 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. 2006, 128(14):4542-4543.
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.14 , pp. 4542-4543
    • Lin, C.-W.1    Ting, A.Y.2
  • 19
    • 84863957785 scopus 로고    scopus 로고
    • Biofabricating multifunctional soft matter with enzymes and stimuli-responsive materials
    • Liu Y., et al. Biofabricating multifunctional soft matter with enzymes and stimuli-responsive materials. Adv. Funct. Mater. 2012, 22(14):3004-3012.
    • (2012) Adv. Funct. Mater. , vol.22 , Issue.14 , pp. 3004-3012
    • Liu, Y.1
  • 21
    • 79751471817 scopus 로고    scopus 로고
    • Fundamentals and applications of immobilized microfluidic enzymatic reactors
    • Matosevic S., Szita N., Baganz F. Fundamentals and applications of immobilized microfluidic enzymatic reactors. J. Chem. Technol. Biotechnol. 2011, 86(3):325-334.
    • (2011) J. Chem. Technol. Biotechnol. , vol.86 , Issue.3 , pp. 325-334
    • Matosevic, S.1    Szita, N.2    Baganz, F.3
  • 22
    • 67349139601 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed covalent multimerization of camelidae anti-human TNF single domain antibodies improves neutralizing activity
    • Plagmann I., et al. Transglutaminase-catalyzed covalent multimerization of camelidae anti-human TNF single domain antibodies improves neutralizing activity. J. Biotechnol. 2009, 142(2):170-178.
    • (2009) J. Biotechnol. , vol.142 , Issue.2 , pp. 170-178
    • Plagmann, I.1
  • 23
    • 0003903343 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, J. Sambrook, D.W. Russell (Eds.)
    • Sambrook J. Molecular Cloning : A Laboratory Manual 2001, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. J. Sambrook, D.W. Russell (Eds.).
    • (2001) Molecular Cloning : A Laboratory Manual
    • Sambrook, J.1
  • 24
    • 77953295630 scopus 로고    scopus 로고
    • Graphene based electrochemical sensors and biosensors: a review
    • Shao Y., et al. Graphene based electrochemical sensors and biosensors: a review. Electroanalysis 2010, 22(10):1027-1036.
    • (2010) Electroanalysis , vol.22 , Issue.10 , pp. 1027-1036
    • Shao, Y.1
  • 25
    • 84868094876 scopus 로고    scopus 로고
    • Local unfolding is required for the site-specific protein modification by transglutaminase
    • Spolaore B., et al. Local unfolding is required for the site-specific protein modification by transglutaminase. Biochemistry 2012, 51(43):8679-8689.
    • (2012) Biochemistry , vol.51 , Issue.43 , pp. 8679-8689
    • Spolaore, B.1
  • 26
    • 84901052647 scopus 로고    scopus 로고
    • Versatility of microbial transglutaminase
    • Strop P. Versatility of microbial transglutaminase. Bioconjugate Chem. 2014, 25(5):855-862.
    • (2014) Bioconjugate Chem. , vol.25 , Issue.5 , pp. 855-862
    • Strop, P.1
  • 27
    • 2442679406 scopus 로고    scopus 로고
    • Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase
    • Tanaka T., Kamiya N., Nagamune T. Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase. Bioconjugate Chem. 2004, 15(3):491-497.
    • (2004) Bioconjugate Chem. , vol.15 , Issue.3 , pp. 491-497
    • Tanaka, T.1    Kamiya, N.2    Nagamune, T.3
  • 28
    • 17844389564 scopus 로고    scopus 로고
    • Making 'sense' of metabolism: autoinducer-2, LUXS and pathogenic bacteria
    • Vendeville A., et al. Making 'sense' of metabolism: autoinducer-2, LUXS and pathogenic bacteria. Nat. Rev. Microbiol. 2005, 3(5):383-396.
    • (2005) Nat. Rev. Microbiol. , vol.3 , Issue.5 , pp. 383-396
    • Vendeville, A.1
  • 29
    • 14344256125 scopus 로고    scopus 로고
    • Carbon-nanotube based electrochemical biosensors: a review
    • Wang J. Carbon-nanotube based electrochemical biosensors: a review. Electroanalysis 2005, 17(1):7-14.
    • (2005) Electroanalysis , vol.17 , Issue.1 , pp. 7-14
    • Wang, J.1
  • 30
    • 40449109054 scopus 로고    scopus 로고
    • Electrochemical glucose biosensors
    • Wang J. Electrochemical glucose biosensors. Chem. Rev. 2008, 108(2):814-825.
    • (2008) Chem. Rev. , vol.108 , Issue.2 , pp. 814-825
    • Wang, J.1
  • 31
    • 84873868922 scopus 로고    scopus 로고
    • Autonomous bacterial localization and gene expression based on nearby cell receptor density
    • Wu H.C., et al. Autonomous bacterial localization and gene expression based on nearby cell receptor density. Mol. Syst. Biol. 2013, 9.
    • (2013) Mol. Syst. Biol. , vol.9
    • Wu, H.C.1
  • 32
    • 84874095104 scopus 로고    scopus 로고
    • Self-assembly of synthetic metabolons through synthetic protein scaffolds: one-step purification, co-immobilization, and substrate channeling
    • You C., Zhang Y.H.P. Self-assembly of synthetic metabolons through synthetic protein scaffolds: one-step purification, co-immobilization, and substrate channeling. ACS Synth. Biol. 2012, 2(2):102-110.
    • (2012) ACS Synth. Biol. , vol.2 , Issue.2 , pp. 102-110
    • You, C.1    Zhang, Y.H.P.2
  • 33
    • 84874095104 scopus 로고    scopus 로고
    • Self-assembly of synthetic metabolons through synthetic protein scaffolds: one-step purification, co-immobilization, and substrate channeling
    • You C., Zhang Y.H.P. Self-assembly of synthetic metabolons through synthetic protein scaffolds: one-step purification, co-immobilization, and substrate channeling. ACS Synth. Biol. 2013, 2(2):102-110.
    • (2013) ACS Synth. Biol. , vol.2 , Issue.2 , pp. 102-110
    • You, C.1    Zhang, Y.H.P.2
  • 34
    • 36849001355 scopus 로고    scopus 로고
    • Transglutaminase crosslinked gelatin as a tissue engineering scaffold
    • Yung C.W., et al. Transglutaminase crosslinked gelatin as a tissue engineering scaffold. J. Biomed. Mater. Res. Part A 2007, 83A(4):1039-1046.
    • (2007) J. Biomed. Mater. Res. Part A , vol.83A , Issue.4 , pp. 1039-1046
    • Yung, C.W.1
  • 35
    • 84940781154 scopus 로고    scopus 로고
    • A 'bioproduction breadboard': programming, assembling, and actuating cellular networks
    • Zargar A., Payne G.F., Bentley W.E. A 'bioproduction breadboard': programming, assembling, and actuating cellular networks. Curr. Opin. Biotechnol. 2015, 36:154-160.
    • (2015) Curr. Opin. Biotechnol. , vol.36 , pp. 154-160
    • Zargar, A.1    Payne, G.F.2    Bentley, W.E.3
  • 36
    • 0037472109 scopus 로고    scopus 로고
    • S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein
    • Zhu J., et al. S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein. Biochemistry 2003, 42(16):4717-4726.
    • (2003) Biochemistry , vol.42 , Issue.16 , pp. 4717-4726
    • Zhu, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.