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Volumn 11, Issue 10, 2016, Pages

Novel hydrophobin fusion tags for plant-produced fusion proteins

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; HYDROPHOBIN; HYDROPHOBIN II; HYDROPHOBIN III; HYDROPHOBIN IV; HYDROPHOBIN V; HYDROPHOBIN VI; PROTEIN HYD3; PROTEIN HYD4; PROTEIN HYD5; SURFACTANT; UNCLASSIFIED DRUG; FUNGAL PROTEIN;

EID: 84992144077     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0164032     Document Type: Article
Times cited : (14)

References (26)
  • 1
    • 48749113989 scopus 로고    scopus 로고
    • Structural analysis of hydrophobins
    • Oct, PMID: 17875392
    • Sunde M, Kwan AHY, Templeton MD, Beever RE, Mackay JP. Structural analysis of hydrophobins. Micron. 2008 Oct; 39(7):773-84. doi: 10.1016/j.micron.2007.08.003 PMID: 17875392
    • (2008) Micron , vol.39 , Issue.7 , pp. 773-784
    • Sunde, M.1    Kwan, A.H.Y.2    Templeton, M.D.3    Beever, R.E.4    Mackay, J.P.5
  • 4
    • 84884220390 scopus 로고    scopus 로고
    • Structure-function relationships in hydrophobins: Probing the role of charged side chains
    • Sep 15; PMID: 23835172
    • Lienemann M, Gandier J- A, Joensuu JJ, Iwanaga A, Takatsuji Y, Haruyama T, et al. Structure-function relationships in hydrophobins: probing the role of charged side chains. Appl Environ Microbiol. 2013 Sep 15; 79(18):5533-8. doi: 10.1128/AEM.01493-13 PMID: 23835172
    • (2013) Appl Environ Microbiol , vol.79 , Issue.18 , pp. 5533-5538
    • Lienemann, M.1    Gandier-J, A.2    Joensuu, J.J.3    Iwanaga, A.4    Takatsuji, Y.5    Haruyama, T.6
  • 5
    • 51049104790 scopus 로고    scopus 로고
    • Exceptional stability of food foams using class II hydrophobin HFBII
    • Mar
    • Cox AR, Aldred DL, Russell AB. Exceptional stability of food foams using class II hydrophobin HFBII. Food Hydrocoll. 2009 Mar; 23(2):366-76. doi: 10.1016/j.foodhyd.2008.03.001
    • (2009) Food Hydrocoll , vol.23 , Issue.2 , pp. 366-376
    • Cox, A.R.1    Aldred, D.L.2    Russell, A.B.3
  • 7
    • 0036708010 scopus 로고    scopus 로고
    • Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei
    • Sep, PMID: 12192081
    • Linder M, Szilvay GR, Nakari-Setälä T, Söderlund H, Penttilä M. Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei. Protein Sci. 2002 Sep; 11 (9):2257-66. doi: 10.1110/ps.0207902 PMID: 12192081
    • (2002) Protein Sci , vol.11 , Issue.9 , pp. 2257-2266
    • Linder, M.1    Szilvay, G.R.2    Nakari-Setälä, T.3    Söderlund, H.4    Penttilä, M.5
  • 8
    • 4644247411 scopus 로고    scopus 로고
    • Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systems
    • Sep 21; PMID: 15362873
    • Linder MB, Qiao M, Laumen F, Selber K, Hyytiä T, Nakari-Setälä T, et al. Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systems. Biochemistry. American Chemical Society; 2004 Sep 21; 43(37):11873-82. doi: 10.1021/bi0488202 PMID: 15362873
    • (2004) Biochemistry American Chemical Society; , vol.43 , Issue.37 , pp. 11873-11882
    • Linder, M.B.1    Qiao, M.2    Laumen, F.3    Selber, K.4    Hyytiä, T.5    Nakari-Setälä, T.6
  • 9
    • 0034888635 scopus 로고    scopus 로고
    • The Hydrophobins HFBI and HFBII from Trichoderma r eesei Showing Efficient Interactions with Nonionic Surfactants in Aqueous Two- Phase Systems
    • Jun, PMID: 11749214
    • Linder M, Selber K, Nakari-Setälä T, Qiao M, Kula M-R, Penttilä M. The Hydrophobins HFBI and HFBII from Trichoderma r eesei Showing Efficient Interactions with Nonionic Surfactants in Aqueous Two- Phase Systems. Biomacromolecules. American Chemical Society; 2001 Jun; 2(2):511-7. doi: 10.1021/bm0001493 PMID: 11749214
    • (2001) Biomacromolecules American Chemical Society; , vol.2 , Issue.2 , pp. 511-517
    • Linder, M.1    Selber, K.2    Nakari-Setälä, T.3    Qiao, M.4    Kula, M.-R.5    Penttilä, M.6
  • 10
    • 40849124046 scopus 로고    scopus 로고
    • Hydrophobin (HFBI): A potential fusion partner for one-step purification of recombinant proteins from insect cells
    • May, PMID: 18267368
    • Lahtinen T, Linder MB, Nakari-Setälä T, Oker-Blom C. Hydrophobin (HFBI): A potential fusion partner for one-step purification of recombinant proteins from insect cells. Protein Expr Purif. 2008 May; 59 (1):18-24. doi: 10.1016/j.pep.2007.12.014 PMID: 18267368
    • (2008) Protein Expr Purif , vol.59 , Issue.1 , pp. 18-24
    • Lahtinen, T.1    Linder, M.B.2    Nakari-Setälä, T.3    Oker-Blom, C.4
  • 11
    • 84855920404 scopus 로고    scopus 로고
    • Bioseparation of recombinant proteins from plant extract with hydrophobin fusion technology
    • Jan, PMID: 22160918
    • Joensuu JJ, Conley AJ, Linder MB, Menassa R. Bioseparation of recombinant proteins from plant extract with hydrophobin fusion technology. Methods Mol Biol. 2012 Jan; 824:527-34. doi: 10.1007/978-1-61779-433-9-28 PMID: 22160918
    • (2012) Methods Mol Biol , vol.824 , pp. 527-534
    • Joensuu, J.J.1    Conley, A.J.2    Linder, M.B.3    Menassa, R.4
  • 12
    • 75949109975 scopus 로고    scopus 로고
    • Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana
    • Feb 1; PMID: 20018596
    • Joensuu JJ, Conley AJ, Lienemann M, Brandle JE, Linder MB, Menassa R. Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiol. 2010 Feb 1; 152(2):622-33. doi: 10.1104/pp.109.149021 PMID: 20018596
    • (2010) Plant Physiol , vol.152 , Issue.2 , pp. 622-633
    • Joensuu, J.J.1    Conley, A.J.2    Lienemann, M.3    Brandle, J.E.4    Linder, M.B.5    Menassa, R.6
  • 13
    • 84899059237 scopus 로고    scopus 로고
    • Scale-up of hydrophobin-assisted recombinant protein production in tobacco BY-2 suspension cells
    • PMID 24341724
    • Reuter LJ, Bailey MJ, Joensuu JJ, Ritala A. Scale-up of hydrophobin-assisted recombinant protein production in tobacco BY-2 suspension cells. Plant Biotechnol J. 2014; 12(4):402-10. doi: 10.1111/pbi. 12147 PMID: 24341724
    • (2014) Plant Biotechnol J , vol.12 , Issue.4 , pp. 402-410
    • Reuter, L.J.1    Bailey, M.J.2    Joensuu, J.J.3    Ritala, A.4
  • 14
    • 0030053545 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the Trichoderma reesei hydrophobin HFBI
    • PMID: 8631337
    • Nakari-Setälä T, Aro N, Kalkkinen N, Alatalo E, Penttilä M. Genetic and biochemical characterization of the Trichoderma reesei hydrophobin HFBI. Eur J Biochem. 1996; 235:248-55. doi: 10.1111/j.1432- 1033.1996.00248.x PMID: 8631337
    • (1996) Eur J Biochem , vol.235 , pp. 248-255
    • Nakari-Setälä, T.1    Aro, N.2    Kalkkinen, N.3    Alatalo, E.4    Penttilä, M.5
  • 15
    • 84877249345 scopus 로고    scopus 로고
    • Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins
    • Jan 10;, PMID: 23663656
    • Gutiérrez SP, Saberianfar R, Kohalmi SE, Menassa R. Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins. BMC Biotechnol. BioMed Central Ltd; 2013 Jan 10; 13(1):40. doi: 10.1186/1472-6750-13-40 PMID: 23663656
    • (2013) BMC Biotechnol. BioMed Central Ltd; , vol.13 , Issue.1 , pp. 40
    • Gutiérrez, S.P.1    Saberianfar, R.2    Kohalmi, S.E.3    Menassa, R.4
  • 16
    • 84939536635 scopus 로고    scopus 로고
    • Protein body formation in leaves of Nicotiana benthamiana: A concentration-dependent mechanism influenced by the presence of fusion tags
    • Sep, PMID: 25640969
    • Saberianfar R, Joensuu JJ, Conley AJ, Menassa R. Protein body formation in leaves of Nicotiana benthamiana: a concentration-dependent mechanism influenced by the presence of fusion tags. Plant Biotechnol J. 2015 Sep; 13(7):927-37. doi: 10.1111/pbi.12329 PMID: 25640969
    • (2015) Plant Biotechnol J. , vol.13 , Issue.7 , pp. 927-937
    • Saberianfar, R.1    Joensuu, J.J.2    Conley, A.J.3    Menassa, R.4
  • 17
    • 84919884398 scopus 로고    scopus 로고
    • Hydrophobin Fusion of an Influenza Virus Hemagglutinin Allows High Transient Expression in Nicotiana benthamiana Easy Purification and Immune Response with Neutralizing Activity
    • PMID 25541987
    • Jacquet N, Navarre C, Desmecht D, Boutry M. Hydrophobin Fusion of an Influenza Virus Hemagglutinin Allows High Transient Expression in Nicotiana benthamiana, Easy Purification and Immune Response with Neutralizing Activity. PLoS One. 2014; 9(12):e115944. doi: 10.1371/journal.pone. 0115944 PMID: 25541987
    • (2014) PLoS One , vol.9 , Issue.12 , pp. e115944
    • Jacquet, N.1    Navarre, C.2    Desmecht, D.3    Boutry, M.4
  • 18
    • 84902578401 scopus 로고    scopus 로고
    • Influence of elastin-like polypeptide and hydrophobin on recombinant hemagglutinin accumulations in transgenic tobacco plants
    • Jan 10;, PMID: 24914995
    • Phan HT, Hause B, Hause G, Arcalis E, Stoger E, Maresch D, et al. Influence of elastin-like polypeptide and hydrophobin on recombinant hemagglutinin accumulations in transgenic tobacco plants. PLoS One. Public Library of Science; 2014 Jan 10; 9(6):e99347. doi: 10.1371/journal.pone.0099347 PMID: 24914995
    • (2014) PLoS One. Public Library of Science; , vol.9 , Issue.6 , pp. e99347
    • Phan, H.T.1    Hause, B.2    Hause, G.3    Arcalis, E.4    Stoger, E.5    Maresch, D.6
  • 19
    • 84902910334 scopus 로고    scopus 로고
    • Production and characterization of in planta transiently produced polygalacturanase from Aspergillus Niger and its fusions with hydrophobin or ELP tags
    • PMID: 24970673
    • Pereira EO, Kolotilin I, Conley AJ, Menassa R. Production and characterization of in planta transiently produced polygalacturanase from Aspergillus niger and its fusions with hydrophobin or ELP tags. BMC Biotechnol. 2014; 14(1):59. doi: 10.1186/1472-6750-14-59 PMID: 24970673
    • (2014) BMC Biotechnol , vol.14 , Issue.1 , pp. 59
    • Pereira, E.O.1    Kolotilin, I.2    Conley, A.J.3    Menassa, R.4
  • 20
    • 79954759457 scopus 로고    scopus 로고
    • Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants
    • May, PMID: 21338467
    • Conley AJ, Joensuu JJ, Richman A, Menassa R. Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants. Plant Biotechnol J. 2011 May; 9(4):419-33. doi: 10.1111/j.1467-7652.2011.00596.x PMID: 21338467
    • (2011) Plant Biotechnol J , vol.9 , Issue.4 , pp. 419-433
    • Conley, A.J.1    Joensuu, J.J.2    Richman, A.3    Menassa, R.4
  • 21
    • 84956698952 scopus 로고    scopus 로고
    • A plant-produced bacteriophage tailspike protein for the control of salmonella
    • Jan, PMID: 26779243
    • Miletic S, Simpson DJ, Szymanski CM, Deyholos MK, Menassa R. A Plant-Produced Bacteriophage Tailspike Protein for the Control of Salmonella. Front Plant Sci. Frontiers; 2015 Jan 8; 6:1221. doi: 10.3389/fpls.2015.01221 PMID: 26779243
    • (2015) Front Plant Sci. Frontiers , vol.8 , Issue.6 , pp. 1221
    • Miletic, S.1    Simpson, D.J.2    Szymanski, C.M.3    Deyholos, M.K.4    Menassa, R.5
  • 22
    • 0030886123 scopus 로고    scopus 로고
    • Differential expression of the vegetative and spore-bound hydrophobins of trichoderma reesei cloning and characterization of the hfb2 gene
    • Sep, PMID: 9346297
    • Nakari-Setala T, Aro N, IlmeN M, Munoz G, Kalkkinen N, Penttila M. Differential Expression of the Vegetative and Spore-Bound Hydrophobins of Trichoderma Reesei Cloning and Characterization of the Hfb2 Gene. Eur J Biochem. 1997 Sep; 248(2):415-23. doi: 10.1111/j.1432-1033.1997.00415.x PMID: 9346297
    • (1997) Eur J Biochem , vol.248 , Issue.2 , pp. 415-423
    • Nakari-Setala, T.1    Aro, N.2    IlmeN, M.3    Munoz, G.4    Kalkkinen, N.5    Penttila, M.6
  • 23
    • 3843086042 scopus 로고    scopus 로고
    • Five hydrophobin genes in Fusarium verticillioides include two required for microconidial chain formation
    • Sep, PMID: 15288021
    • Fuchs U, Czymmek KJ, Sweigard JA. Five hydrophobin genes in Fusarium verticillioides include two required for microconidial chain formation. Fungal Genet Biol. 2004 Sep; 41(9):852-64. doi: 10.1016/j. fgb.2004.04.004 PMID: 15288021
    • (2004) Fungal Genet Biol , vol.41 , Issue.9 , pp. 852-864
    • Fuchs, U.1    Czymmek, K.J.2    Sweigard, J.A.3
  • 25
    • 84879807034 scopus 로고    scopus 로고
    • Two novel class II hydrophobins from Trichoderma spp. Stimulate enzymatic hydrolysis of poly(ethylene terephthalate) when expressed as fusion proteins
    • Jul 15;, PMID: 23645195
    • Espino-Rammer L, Ribitsch D, Przylucka A, Marold A, Greimel KJ, Herrero Acero E, et al. Two novel class II hydrophobins from Trichoderma spp. stimulate enzymatic hydrolysis of poly(ethylene terephthalate) when expressed as fusion proteins. Appl Environ Microbiol. 2013 Jul 15; 79(14):4230-8. doi: 10.1128/AEM.01132-13 PMID: 23645195
    • (2013) Appl Environ Microbiol , vol.79 , Issue.14 , pp. 4230-4238
    • Espino-Rammer, L.1    Ribitsch, D.2    Przylucka, A.3    Marold, A.4    Greimel, K.J.5    Herrero Acero, E.6
  • 26
    • 0037124354 scopus 로고    scopus 로고
    • A viral protein suppresses RNA silencing and binds silencing-generated, 21- to 25-nucleotide double-stranded RNAs
    • Jun 17; PMID: 12065420
    • Silhavy D, Molná r A, Lucioli A, Szittya G, Hornyik C, Tavazza M, et al. A viral protein suppresses RNA silencing and binds silencing-generated, 21- to 25-nucleotide double-stranded RNAs. EMBO J. 2002 Jun 17; 21(12):3070-80. doi: 10.1093/emboj/cdf312 PMID: 12065420
    • (2002) EMBO J , vol.21 , Issue.12 , pp. 3070-3080
    • Silhavy, D.1    Molnár, A.2    Lucioli, A.3    Szittya, G.4    Hornyik, C.5    Tavazza, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.