메뉴 건너뛰기




Volumn 182, Issue 1, 2017, Pages 168-180

Effect of Linker Length and Flexibility on the Clostridium thermocellum Esterase Displayed on Bacillus subtilis Spores

Author keywords

Bacillus subtilis; Displayed; Esterase; Flexibility; Linker; Spore

Indexed keywords

BACTERIOLOGY; DIMETHYL SULFOXIDE; ENZYME ACTIVITY; ENZYMES; ESTERS; ORGANIC SOLVENTS;

EID: 85001578768     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-016-2318-y     Document Type: Article
Times cited : (28)

References (48)
  • 1
    • 77956598900 scopus 로고    scopus 로고
    • Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier [J]
    • COI: 1:CAS:528:DC%2BC3cXht1WmsL7N
    • Potot, S., Serra, C. R., Henriques, A. O., et al. (2010). Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier [J]. Applied and Environmental Microbiology, 76(17), 5926–5933.
    • (2010) Applied and Environmental Microbiology , vol.76 , Issue.17 , pp. 5926-5933
    • Potot, S.1    Serra, C.R.2    Henriques, A.O.3
  • 2
    • 84927787905 scopus 로고    scopus 로고
    • Spore surface display [J]
    • Ricca, R. I. E. (2014). Spore surface display [J]. Microbiology Spectrum, 2(5), 1–15.
    • (2014) Microbiology Spectrum , vol.2 , Issue.5 , pp. 1-15
    • Ricca, R.I.E.1
  • 3
    • 78649901662 scopus 로고    scopus 로고
    • Efficient binding of nickel ions to recombinant Bacillus subtilis spores [J]
    • COI: 1:CAS:528:DC%2BC3cXhsFWqtrrE
    • Hinc, K., Ghandili, S., Karbalaee, G., et al. (2010). Efficient binding of nickel ions to recombinant Bacillus subtilis spores [J]. Research in Microbiology, 161(9), 757–764.
    • (2010) Research in Microbiology , vol.161 , Issue.9 , pp. 757-764
    • Hinc, K.1    Ghandili, S.2    Karbalaee, G.3
  • 4
    • 1542270981 scopus 로고    scopus 로고
    • Display of heterologous antigens on the Bacillus Subtilis spore coat using CotC as a fusion partner [J]
    • COI: 1:CAS:528:DC%2BD2cXhslCjsr8%3D
    • Mauriello, E. M., le H, D., Isticato, R., et al. (2004). Display of heterologous antigens on the Bacillus Subtilis spore coat using CotC as a fusion partner [J]. Vaccine, 22(9–10), 1177–1187.
    • (2004) Vaccine , vol.22 , Issue.9-10 , pp. 1177-1187
    • Mauriello, E.M.1    le, D.2    Isticato, R.3
  • 5
    • 80053161551 scopus 로고    scopus 로고
    • Bacterial surface display of a co-factor containing enzyme, ω-transaminase from Vibrio fluvialis using the Bacillus subtilis spore display system [J]
    • COI: 1:CAS:528:DC%2BC3MXht12htLbN
    • Hwang, B. Y., Kim, B. G., & Kim, J. H. (2011). Bacterial surface display of a co-factor containing enzyme, ω-transaminase from Vibrio fluvialis using the Bacillus subtilis spore display system [J]. Bioscience Biotechnology & Biochemistry, 75(9), 1862–1865.
    • (2011) Bioscience Biotechnology & Biochemistry , vol.75 , Issue.9 , pp. 1862-1865
    • Hwang, B.Y.1    Kim, B.G.2    Kim, J.H.3
  • 6
    • 77956598900 scopus 로고    scopus 로고
    • Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier [J]
    • COI: 1:CAS:528:DC%2BC3cXht1WmsL7N
    • Potot, S., Serra, C. R., Henriques, A. O., et al. (2010). Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier [J]. Applied & Environmental Microbiology, 76(17), 5926–5933.
    • (2010) Applied & Environmental Microbiology , vol.76 , Issue.17 , pp. 5926-5933
    • Potot, S.1    Serra, C.R.2    Henriques, A.O.3
  • 7
    • 79951556377 scopus 로고    scopus 로고
    • Surface display of recombinant protein on the cell surface of Bacillus subtilis by the CotB anchor protein [J]
    • COI: 1:CAS:528:DC%2BC3MXhvV2gsb8%3D
    • Han, M., & Enomoto, K. (2011). Surface display of recombinant protein on the cell surface of Bacillus subtilis by the CotB anchor protein [J]. World Journal of Microbiology & Biotechnology, 27(3), 719–726.
    • (2011) World Journal of Microbiology & Biotechnology , vol.27 , Issue.3 , pp. 719-726
    • Han, M.1    Enomoto, K.2
  • 8
    • 0035171389 scopus 로고    scopus 로고
    • Functional analysis of the Bacillus subtilis [J]
    • Driks S L a A. Functional analysis of the Bacillus subtilis [J]. Molecular Microbiology, 2001, 42(4): 1107–1120.
    • (2001) Molecular Microbiology , vol.42 , Issue.4 , pp. 1107-1120
  • 9
    • 0035685619 scopus 로고    scopus 로고
    • Surface display of recombinant proteins on Bacillus subtilis spores [J]
    • COI: 1:CAS:528:DC%2BD3MXnsl2hu70%3D
    • Isticato, R., Cangiano, G., Tran, H. T., et al. (2001). Surface display of recombinant proteins on Bacillus subtilis spores [J]. Journal of Bacteriology, 183(21), 6294–6301.
    • (2001) Journal of Bacteriology , vol.183 , Issue.21 , pp. 6294-6301
    • Isticato, R.1    Cangiano, G.2    Tran, H.T.3
  • 10
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: a review [J]
    • COI: 1:CAS:528:DC%2BD3sXis1aqu7s%3D
    • Haki, G., & Rakshit, S. (2003). Developments in industrially important thermostable enzymes: a review [J]. Bioresource Technology, 89(1), 17–34.
    • (2003) Bioresource Technology , vol.89 , Issue.1 , pp. 17-34
    • Haki, G.1    Rakshit, S.2
  • 11
    • 84881018686 scopus 로고    scopus 로고
    • Fusion protein linkers: property, design and functionality [J]
    • COI: 1:CAS:528:DC%2BC38XhsFWitbvN
    • Chen, X., Zaro, J. L., & Shen, W.-C. (2013). Fusion protein linkers: property, design and functionality [J]. Advanced Drug Delivery Reviews, 65(10), 1357–1369.
    • (2013) Advanced Drug Delivery Reviews , vol.65 , Issue.10 , pp. 1357-1369
    • Chen, X.1    Zaro, J.L.2    Shen, W.-C.3
  • 12
    • 84924302954 scopus 로고    scopus 로고
    • Bringing functions together with fusion enzymes-from nature's inventions to biotechnological applications [J]
    • COI: 1:CAS:528:DC%2BC2cXitFClsLfJ
    • Elleuche, S. (2015). Bringing functions together with fusion enzymes-from nature's inventions to biotechnological applications [J]. Applied Microbiology & Biotechnology, 99(4), 1545–1556.
    • (2015) Applied Microbiology & Biotechnology , vol.99 , Issue.4 , pp. 1545-1556
    • Elleuche, S.1
  • 13
    • 47749104481 scopus 로고    scopus 로고
    • Increasing the homogeneity, stability and activity of human serum albumin and interferon-α2b fusion protein by linker engineering [J]
    • COI: 1:CAS:528:DC%2BD1cXptVOisL4%3D
    • Zhao, H. L., Yao, X. Q., Xue, C., et al. (2008). Increasing the homogeneity, stability and activity of human serum albumin and interferon-α2b fusion protein by linker engineering [J]. Protein Expression and Purification, 61(1), 73–77.
    • (2008) Protein Expression and Purification , vol.61 , Issue.1 , pp. 73-77
    • Zhao, H.L.1    Yao, X.Q.2    Xue, C.3
  • 14
    • 84874936274 scopus 로고    scopus 로고
    • Active inclusion bodies of acid phosphatase PhoC: aggregation induced by GFP fusion and activities modulated by linker flexibility [J]
    • Huang, Z., Zhang, C., Chen, S., et al. (2013). Active inclusion bodies of acid phosphatase PhoC: aggregation induced by GFP fusion and activities modulated by linker flexibility [J]. Microbial Cell Factories, 12(1), 1.
    • (2013) Microbial Cell Factories , vol.12 , Issue.1 , pp. 1
    • Huang, Z.1    Zhang, C.2    Chen, S.3
  • 15
    • 60049093597 scopus 로고    scopus 로고
    • Insertion of the designed helical linker led to increased expression of tf-based fusion proteins [J]
    • COI: 1:CAS:528:DC%2BD1cXhtlGgtrzJ
    • Amet, N., Lee, H.-F., & Shen, W.-C. (2009). Insertion of the designed helical linker led to increased expression of tf-based fusion proteins [J]. Pharmaceutical Research, 26(3), 523–528.
    • (2009) Pharmaceutical Research , vol.26 , Issue.3 , pp. 523-528
    • Amet, N.1    Lee, H.-F.2    Shen, W.-C.3
  • 16
    • 33750583939 scopus 로고    scopus 로고
    • Improving the oral efficacy of recombinant granulocyte colony-stimulating factor and transferrin fusion protein by spacer optimization [J]
    • COI: 1:CAS:528:DC%2BD28XptVaisLg%3D
    • Bai, Y., & Shen, W.-C. (2006). Improving the oral efficacy of recombinant granulocyte colony-stimulating factor and transferrin fusion protein by spacer optimization [J]. Pharmaceutical Research, 23(9), 2116–2121.
    • (2006) Pharmaceutical Research , vol.23 , Issue.9 , pp. 2116-2121
    • Bai, Y.1    Shen, W.-C.2
  • 17
    • 33746543618 scopus 로고    scopus 로고
    • Construction and characterization of a bifunctional fusion enzyme of Bacillus-sourced β-glucanase and xylanase expressed in Escherichia coli [J]
    • COI: 1:CAS:528:DC%2BD28XovFyhsLk%3D
    • Lu, P., Feng, M.-G., Li, W.-F., et al. (2006). Construction and characterization of a bifunctional fusion enzyme of Bacillus-sourced β-glucanase and xylanase expressed in Escherichia coli [J]. FEMS Microbiology Letters, 261(2), 224–230.
    • (2006) FEMS Microbiology Letters , vol.261 , Issue.2 , pp. 224-230
    • Lu, P.1    Feng, M.-G.2    Li, W.-F.3
  • 18
    • 33144464467 scopus 로고    scopus 로고
    • Control of protein functional dynamics by peptide linkers [J]
    • COI: 1:CAS:528:DC%2BD2MXhtlSqur%2FM
    • Wriggers, W., Chakravarty, S., & Jennings, P. A. (2005). Control of protein functional dynamics by peptide linkers [J]. Peptide Science, 80(6), 736–746.
    • (2005) Peptide Science , vol.80 , Issue.6 , pp. 736-746
    • Wriggers, W.1    Chakravarty, S.2    Jennings, P.A.3
  • 19
    • 33847309602 scopus 로고    scopus 로고
    • Design of a bifunctional fusion protein for ovarian cancer drug delivery: single-chain anti-CA125 core-streptavidin fusion protein [J]
    • COI: 1:CAS:528:DC%2BD2sXisVCgsb8%3D
    • Wang, W. W.-S., Das, D., McQuarrie, S. A., et al. (2007). Design of a bifunctional fusion protein for ovarian cancer drug delivery: single-chain anti-CA125 core-streptavidin fusion protein [J]. European Journal of Pharmaceutics and Biopharmaceutics, 65(3), 398–405.
    • (2007) European Journal of Pharmaceutics and Biopharmaceutics , vol.65 , Issue.3 , pp. 398-405
    • Wang, W.W.-S.1    Das, D.2    McQuarrie, S.A.3
  • 20
    • 84924663659 scopus 로고    scopus 로고
    • Effect of linker flexibility and length on the functionality of a cytotoxic engineered antibody fragment [J]
    • COI: 1:CAS:528:DC%2BC2MXjtV2lu78%3D
    • Klement, M., Liu, C., Loo, B. L. W., et al. (2015). Effect of linker flexibility and length on the functionality of a cytotoxic engineered antibody fragment [J]. Journal of Biotechnology, 199, 90–97.
    • (2015) Journal of Biotechnology , vol.199 , pp. 90-97
    • Klement, M.1    Liu, C.2    Loo, B.L.W.3
  • 21
    • 0033151952 scopus 로고    scopus 로고
    • Characterization of scFv-Ig constructs generated from the anti-CD20 mAb 1F5 using linker peptides of varying lengths [J]
    • COI: 1:CAS:528:DyaK1MXjtlKit70%3D
    • Shan, D., Press, O. W., Tsu, T. T., et al. (1999). Characterization of scFv-Ig constructs generated from the anti-CD20 mAb 1F5 using linker peptides of varying lengths [J]. The Journal of Immunology, 162(11), 6589–6595.
    • (1999) The Journal of Immunology , vol.162 , Issue.11 , pp. 6589-6595
    • Shan, D.1    Press, O.W.2    Tsu, T.T.3
  • 22
    • 84992135181 scopus 로고    scopus 로고
    • Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy [J]
    • COI: 1:CAS:528:DC%2BC28XhtValtLjJ
    • Liu, H., Qiao, H., Krajcikova, D., et al. (2016). Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy [J]. Journal of Structural Biology, 195(2), 245–251.
    • (2016) Journal of Structural Biology , vol.195 , Issue.2 , pp. 245-251
    • Liu, H.1    Qiao, H.2    Krajcikova, D.3
  • 23
    • 33751355259 scopus 로고    scopus 로고
    • Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis [J]
    • COI: 1:CAS:528:DC%2BD2sXit1Kiuw%3D%3D
    • Ramamurthi, K. S., Clapham, K. R., & Losick, R. (2006). Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis [J]. Molecular Microbiology, 62(6), 1547–1557.
    • (2006) Molecular Microbiology , vol.62 , Issue.6 , pp. 1547-1557
    • Ramamurthi, K.S.1    Clapham, K.R.2    Losick, R.3
  • 24
    • 25144498144 scopus 로고    scopus 로고
    • De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria [J]
    • COI: 1:CAS:528:DC%2BD2MXhtVGrtrfP
    • Chang, H.-C., Kaiser, C. M., Hartl, F. U., et al. (2005). De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria [J]. Journal of Molecular Biology, 353(2), 397–409.
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 397-409
    • Chang, H.-C.1    Kaiser, C.M.2    Hartl, F.U.3
  • 25
    • 84953875073 scopus 로고    scopus 로고
    • A study on the effects of linker flexibility on acid phosphatase PhoC-GFP fusion protein using a novel linker library [J]
    • Huang, Z., Li, G., Zhang, C., et al. (2016). A study on the effects of linker flexibility on acid phosphatase PhoC-GFP fusion protein using a novel linker library [J]. Enzyme and Microbial Technology, 83, 1–6.
    • (2016) Enzyme and Microbial Technology , vol.83 , pp. 1-6
    • Huang, Z.1    Li, G.2    Zhang, C.3
  • 26
    • 0031584314 scopus 로고    scopus 로고
    • Importance of the linker in expression of single-chain Fv antibody fragments: optimisation of peptide sequence using phage display technology [J]
    • COI: 1:CAS:528:DyaK2sXkslersbg%3D
    • Turner, D. J., Ritter, M. A., & George, A. J. (1997). Importance of the linker in expression of single-chain Fv antibody fragments: optimisation of peptide sequence using phage display technology [J]. Journal of Immunological Methods, 205(1), 43–54.
    • (1997) Journal of Immunological Methods , vol.205 , Issue.1 , pp. 43-54
    • Turner, D.J.1    Ritter, M.A.2    George, A.J.3
  • 27
    • 84962491420 scopus 로고    scopus 로고
    • Acyclic Cucurbit [n] uril-type molecular containers: influence of linker length on their function as solubilizing agents [J]
    • Sigwalt, D., Moncelet, D., Falcinelli, S., et al. (2016). Acyclic Cucurbit [n] uril-type molecular containers: influence of linker length on their function as solubilizing agents [J]. ChemMedChem.
    • (2016) ChemMedChem
    • Sigwalt, D.1    Moncelet, D.2    Falcinelli, S.3
  • 29
    • 84947968373 scopus 로고    scopus 로고
    • Linker engineering for fusion protein construction: improvement and characterization of a GLP-1 fusion protein [J]
    • COI: 1:CAS:528:DC%2BC2MXhvV2jsrrN
    • Kong, Y., Tong, Y., Gao, M., et al. (2016). Linker engineering for fusion protein construction: improvement and characterization of a GLP-1 fusion protein [J]. Enzyme and Microbial Technology, 82, 105–109.
    • (2016) Enzyme and Microbial Technology , vol.82 , pp. 105-109
    • Kong, Y.1    Tong, Y.2    Gao, M.3
  • 30
    • 84944278915 scopus 로고    scopus 로고
    • Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein [J]
    • Chen, H., Zhang, T., Jia, J., et al. (2015). Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein [J]. Journal of Industrial Microbiology, 42(11), 1–10.
    • (2015) Journal of Industrial Microbiology , vol.42 , Issue.11 , pp. 1-10
    • Chen, H.1    Zhang, T.2    Jia, J.3
  • 32
    • 0345196536 scopus 로고    scopus 로고
    • Construction of an efficient Bacillus subtilis system for extracellular production of heterologous proteins [J]
    • COI: 1:CAS:528:DyaK1cXls1Ort7c%3D
    • Lam, K., Chow, K., & Wong, W. (1998). Construction of an efficient Bacillus subtilis system for extracellular production of heterologous proteins [J]. Journal of Biotechnology, 63(3), 167–177.
    • (1998) Journal of Biotechnology , vol.63 , Issue.3 , pp. 167-177
    • Lam, K.1    Chow, K.2    Wong, W.3
  • 33
    • 33749015170 scopus 로고    scopus 로고
    • Construction and characterization of a novel maltose inducible expression vector in Bacillus subtilis [J]
    • Ming-Ming, Y., Wei-Wei, Z., Xi-Feng, Z., et al. (2006). Construction and characterization of a novel maltose inducible expression vector in Bacillus subtilis [J]. Biotechnology Letters, 28(21), 1713–1718.
    • (2006) Biotechnology Letters , vol.28 , Issue.21 , pp. 1713-1718
    • Ming-Ming, Y.1    Wei-Wei, Z.2    Xi-Feng, Z.3
  • 34
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines [J]
    • COI: 1:CAS:528:DyaK2sXislCitw%3D%3D
    • Georgiou, G., Stathopoulos, C., Daugherty, P. S., et al. (1997). Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines [J]. Nature Biotechnology, 15(1), 29–34.
    • (1997) Nature Biotechnology , vol.15 , Issue.1 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3
  • 35
    • 62149133544 scopus 로고    scopus 로고
    • Fusion-proteins as biopharmaceuticals—applications and challenges [J]
    • COI: 1:CAS:528:DC%2BD1MXnt12lu7k%3D
    • Schmidt, S. R. (2009). Fusion-proteins as biopharmaceuticals—applications and challenges [J]. Current Opinion in Drug Discovery & Development, 12(2), 284–295.
    • (2009) Current Opinion in Drug Discovery & Development , vol.12 , Issue.2 , pp. 284-295
    • Schmidt, S.R.1
  • 36
    • 0036878154 scopus 로고    scopus 로고
    • An analysis of protein domain linkers: their classification and role in protein folding [J]
    • COI: 1:CAS:528:DC%2BD3sXitlCntLw%3D
    • George, R. A., & Heringa, J. (2002). An analysis of protein domain linkers: their classification and role in protein folding [J]. Protein Engineering, 15(11), 871–879.
    • (2002) Protein Engineering , vol.15 , Issue.11 , pp. 871-879
    • George, R.A.1    Heringa, J.2
  • 37
    • 0014381393 scopus 로고
    • Conformation of polypeptides and proteins [J]
    • COI: 1:CAS:528:DyaE3cXhtFOmsL8%3D
    • Ramachandran, G. T., & Sasisekharan, V. (1968). Conformation of polypeptides and proteins [J]. Advances in Protein Chemistry, 23, 283–437.
    • (1968) Advances in Protein Chemistry , vol.23 , pp. 283-437
    • Ramachandran, G.T.1    Sasisekharan, V.2
  • 38
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of single-chain proteins by linker length and composition mutagenesis [J]
    • COI: 1:CAS:528:DyaK1cXjtlKgsrY%3D
    • Robinson, C. R., & Sauer, R. T. (1998). Optimizing the stability of single-chain proteins by linker length and composition mutagenesis [J]. Proceedings of the National Academy of Sciences, 95(11), 5929–5934.
    • (1998) Proceedings of the National Academy of Sciences , vol.95 , Issue.11 , pp. 5929-5934
    • Robinson, C.R.1    Sauer, R.T.2
  • 39
    • 44649144487 scopus 로고    scopus 로고
    • Bifunctional enhancement of a β-glucanase-xylanase fusion enzyme by optimization of peptide linkers [J]
    • COI: 1:CAS:528:DC%2BD1cXmsFKgurY%3D
    • Lu, P., & Feng, M.-G. (2008). Bifunctional enhancement of a β-glucanase-xylanase fusion enzyme by optimization of peptide linkers [J]. Applied Microbiology and Biotechnology, 79(4), 579–587.
    • (2008) Applied Microbiology and Biotechnology , vol.79 , Issue.4 , pp. 579-587
    • Lu, P.1    Feng, M.-G.2
  • 40
    • 0022929888 scopus 로고
    • 1H-NMR study of mobility and conformational constraints within the proline-rich N-terminal of the LC1 alkali light chain of skeletal myosin [J]
    • COI: 1:CAS:528:DyaL28XlvVKisLo%3D
    • BHANDARI, D. G., LEVINE, B. A., TRAYER, I. P., et al. (1986). 1H-NMR study of mobility and conformational constraints within the proline-rich N-terminal of the LC1 alkali light chain of skeletal myosin [J]. European Journal of Biochemistry, 160(2), 349–356.
    • (1986) European Journal of Biochemistry , vol.160 , Issue.2 , pp. 349-356
    • Bhandari, D.G.1    Levine, B.A.2    Trayer, I.P.3
  • 41
    • 84947787900 scopus 로고    scopus 로고
    • SynLinker: an integrated system for designing linkers and synthetic fusion proteins [J]
    • COI: 1:CAS:528:DC%2BC28Xht1CitL7N
    • Liu, C., Chin, J. X., & Lee, D. Y. (2015). SynLinker: an integrated system for designing linkers and synthetic fusion proteins [J]. Bioinformatics, 31(22), 3700–3702.
    • (2015) Bioinformatics , vol.31 , Issue.22 , pp. 3700-3702
    • Liu, C.1    Chin, J.X.2    Lee, D.Y.3
  • 42
    • 0034039320 scopus 로고    scopus 로고
    • LINKER: a program to generate linker sequences for fusion proteins [J]
    • COI: 1:CAS:528:DC%2BD3cXntFamsb0%3D
    • Crasto, C. J., & Feng, J.-a. (2000). LINKER: a program to generate linker sequences for fusion proteins [J]. Protein Engineering, 13(5), 309–312.
    • (2000) Protein Engineering , vol.13 , Issue.5 , pp. 309-312
    • Crasto, C.J.1    Feng, J.-A.2
  • 43
    • 3242885821 scopus 로고    scopus 로고
    • LINKER: a web server to generate peptide sequences with extended conformation [J]
    • COI: 1:CAS:528:DC%2BD2cXlvFKms7g%3D
    • Xue, F., Gu, Z., & Feng, J.-a. (2004). LINKER: a web server to generate peptide sequences with extended conformation [J]. Nucleic Acids Research, 32(suppl 2), W562–W565.
    • (2004) Nucleic Acids Research , vol.32 , pp. W562-W565
    • Xue, F.1    Gu, Z.2    Feng, J.-A.3
  • 44
    • 84874365109 scopus 로고    scopus 로고
    • New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis [J]
    • COI: 1:CAS:528:DC%2BC3sXks1Wgtb4%3D
    • Hinc, K., Iwanicki, A., & Obuchowski, M. (2013). New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis [J]. Microbial Cell Factories, 12(1), 22.
    • (2013) Microbial Cell Factories , vol.12 , Issue.1 , pp. 22
    • Hinc, K.1    Iwanicki, A.2    Obuchowski, M.3
  • 45
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins [J]
    • COI: 1:CAS:528:DyaK2cXpvFGguw%3D%3D
    • Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins [J]. Biochemical Journal, 297(Pt 2), 249.
    • (1994) Biochemical Journal , vol.297 , pp. 249
    • Williamson, M.P.1
  • 46
    • 84890319993 scopus 로고    scopus 로고
    • Strategies for stabilization of enzymes in organic solvents [J]
    • COI: 1:CAS:528:DC%2BC3sXhs1Sqs7nL
    • Stepankova, V., Bidmanova, S., Koudelakova, T., et al. (2013). Strategies for stabilization of enzymes in organic solvents [J]. ACS Catalysis, 3(12), 2823–2836.
    • (2013) ACS Catalysis , vol.3 , Issue.12 , pp. 2823-2836
    • Stepankova, V.1    Bidmanova, S.2    Koudelakova, T.3
  • 47
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents [J]
    • COI: 1:CAS:528:DC%2BD3MXlvFWiuw%3D%3D
    • Klibanov, A. M. (2001). Improving enzymes by using them in organic solvents [J]. Nature, 409, 241–246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 48
    • 0024293979 scopus 로고
    • Single-chain antigen-binding proteins [J]
    • COI: 1:CAS:528:DyaL1MXit12ktLo%3D
    • Bird, R. E., Hardman, K. D., Jacobson, J. W., et al. (1988). Single-chain antigen-binding proteins [J]. Science, 242(4877), 423–426.
    • (1988) Science , vol.242 , Issue.4877 , pp. 423-426
    • Bird, R.E.1    Hardman, K.D.2    Jacobson, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.