메뉴 건너뛰기




Volumn 32, Issue 5, 2018, Pages 2658-2675

Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation

Author keywords

Chaperna; Neutralizing antibody; Protein folding; Viral infection

Indexed keywords

CHAPERONE; INFLUENZA VIRUS HEMAGGLUTININ; NEUTRALIZING ANTIBODY; RNA; TRANSFER RNA; HEMAGGLUTININ, HUMAN INFLUENZA A VIRUS; VIRUS ANTIBODY;

EID: 85047079132     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.201700747RR     Document Type: Article
Times cited : (21)

References (63)
  • 1
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick, J. P., and Hartl, F. U. (1995) The role of molecular chaperones in protein folding. FASEB J. 9, 1559-1569
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.U.2
  • 2
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and Hayer-Hartl, M. (2002)Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and Horwich, A. L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 5
    • 85003968385 scopus 로고    scopus 로고
    • RNAs as chaperones
    • Horowitz, S., and Bardwell, J. C. (2016) RNAs as chaperones. RNA Biol. 13, 1228-1231
    • (2016) RNA Biol. , vol.13 , pp. 1228-1231
    • Horowitz, S.1    Bardwell, J.C.2
  • 7
    • 84964056001 scopus 로고    scopus 로고
    • M1RNAis important for the in-cell solubility of its cognate C5 protein: Implications for RNAmediated protein folding
    • Son,A.,Choi,S. I.,Han,G.,andSeong,B.L. (2015)M1RNAis important for the in-cell solubility of its cognate C5 protein: implications for RNAmediated protein folding. RNA Biol. 12, 1198-1208
    • (2015) RNA Biol. , vol.12 , pp. 1198-1208
    • Son, A.1    Choi, S.I.2    Han, G.3    Seong, B.L.4
  • 8
    • 0029759715 scopus 로고    scopus 로고
    • Reactivation of denatured proteins by 23S ribosomal RNA: Role of domain v
    • Chattopadhyay, S., Das, B., and Dasgupta, C. (1996) Reactivation of denatured proteins by 23S ribosomal RNA: role of domain V. Proc. Natl. Acad. Sci. USA 93, 8284-8287
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8284-8287
    • Chattopadhyay, S.1    Das, B.2    Dasgupta, C.3
  • 9
    • 0030623528 scopus 로고    scopus 로고
    • Ribosomes and ribosomal RNA as chaperones for folding of proteins
    • Kudlicki, W., Coffman, A., Kramer, G., and Hardesty, B. (1997) Ribosomes and ribosomal RNA as chaperones for folding of proteins. Fold. Des. 2, 101-108
    • (1997) Fold. Des. , vol.2 , pp. 101-108
    • Kudlicki, W.1    Coffman, A.2    Kramer, G.3    Hardesty, B.4
  • 10
    • 85021454258 scopus 로고    scopus 로고
    • The folding competence of HIV-1 Tat mediated by interaction with TAR RNA
    • Kim, J. M., Choi, H. S., and Seong, B. L. (2017) The folding competence of HIV-1 Tat mediated by interaction with TAR RNA. RNA Biol. 14, 926-937
    • (2017) RNA Biol. , vol.14 , pp. 926-937
    • Kim, J.M.1    Choi, H.S.2    Seong, B.L.3
  • 13
    • 78049288264 scopus 로고    scopus 로고
    • Vaccine delivery: A matter of size, geometry, kinetics and molecular patterns
    • Bachmann, M. F., and Jennings, G. T. (2010) Vaccine delivery: a matter of size, geometry, kinetics and molecular patterns. Nat. Rev. Immunol. 10, 787-796
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 787-796
    • Bachmann, M.F.1    Jennings, G.T.2
  • 15
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa, P., and Csermely, P. (2004) The role of structural disorder in the function of RNA and protein chaperones. FASEB J. 18, 1169-1175
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 16
    • 0141518434 scopus 로고    scopus 로고
    • A peptide fromthe extension of Lys-tRNA synthetase binds to transfer RNA and DNA
    • Yiadom,K.P.,Hammamieh, R.,Ukpabi,N.,Tsang,P.,andYang,D. C. (2003) A peptide fromthe extension of Lys-tRNA synthetase binds to transfer RNA and DNA. Peptides 24, 987-998
    • (2003) Peptides , vol.24 , pp. 987-998
    • Yiadom, K.P.1    Hammamieh, R.2    Ukpabi, N.3    Tsang, P.4    Yang, D.C.5
  • 17
    • 0028988414 scopus 로고
    • Polyanion-induced alpha-helical structure of a synthetic 23-residue peptide representing the lysine-rich segment of the N-terminal extension of yeast cytoplasmic aspartyl-tRNA synthetase
    • Agou, F., Yang, Y.,Gesquière, J.C.,Waller, J. P., and Guittet, E. (1995) Polyanion-induced alpha-helical structure of a synthetic 23-residue peptide representing the lysine-rich segment of the N-terminal extension of yeast cytoplasmic aspartyl-tRNA synthetase. Biochemistry 34, 569-576
    • (1995) Biochemistry , vol.34 , pp. 569-576
    • Agou, F.1    Yang, Y.2    Gesquière, J.C.3    Waller, J.P.4    Guittet, E.5
  • 18
    • 0037127205 scopus 로고    scopus 로고
    • TheNterminal domain ofmammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain
    • Francin,M.,Kaminska,M.,Kerjan, P., andMirande,M. (2002)TheNterminal domain ofmammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain. J. Biol. Chem. 277, 1762-1769
    • (2002) J. Biol. Chem. , vol.277 , pp. 1762-1769
    • Francin, M.1    Kaminska, M.2    Kerjan, P.3    Mirande, M.4
  • 21
    • 84964588070 scopus 로고    scopus 로고
    • The 2016 Vaccine Development Pipeline: A special issue from the World Health Organization Product Development for Vaccine Advisory Committee (PDVAC)
    • Giersing, B. K., Modjarrad, K., Kaslow, D. C., Okwo-Bele, J. M., and Moorthy, V. S. (2016) The 2016 Vaccine Development Pipeline: a special issue from the World Health Organization Product Development for Vaccine Advisory Committee (PDVAC). Vaccine 34, 2863-2864
    • (2016) Vaccine , vol.34 , pp. 2863-2864
    • Giersing, B.K.1    Modjarrad, K.2    Kaslow, D.C.3    Okwo-Bele, J.M.4    Moorthy, V.S.5
  • 22
    • 84888123350 scopus 로고    scopus 로고
    • High-yield soluble expression of recombinant influenza virus antigens fromEscherichia coli and their potential uses in diagnosis
    • Jang, Y. H., Cho, S. H., Son, A., Lee, Y. H., Lee, J., Lee, K. H., and Seong, B. L. (2014) High-yield soluble expression of recombinant influenza virus antigens fromEscherichia coli and their potential uses in diagnosis. J. Virol. Methods 196, 56-64
    • (2014) J. Virol. Methods , vol.196 , pp. 56-64
    • Jang, Y.H.1    Cho, S.H.2    Son, A.3    Lee, Y.H.4    Lee, J.5    Lee, K.H.6    Seong, B.L.7
  • 23
    • 33947728505 scopus 로고    scopus 로고
    • N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers
    • Kim,C.W.,Han,K.S.,Ryu,K. S.,Kim,B.H.,Kim,K.H.,Choi,S. I.,and Seong, B. L. (2007) N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers. Protein Sci. 16, 635-643
    • (2007) Protein Sci. , vol.16 , pp. 635-643
    • Kim, C.W.1    Han, K.S.2    Ryu, K.S.3    Kim, B.H.4    Kim, K.H.5    Choi, S.I.6    Seong, B.L.7
  • 24
    • 85019427531 scopus 로고    scopus 로고
    • Comparativeproteinstructuremodeling using MODELLER
    • Webb,B., andSali,A. (2016)Comparativeproteinstructuremodeling using MODELLER. Curr. Protoc. Protein Sci. 86, 2.9.1-2.9.37
    • (2016) Curr. Protoc. Protein Sci. , vol.86 , pp. 291-2937
    • Webb, B.1    Sali, A.2
  • 27
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: An FFT-based protein docking program with pairwise potentials
    • Kozakov, D., Brenke, R., Comeau, S. R., and Vajda, S. (2006) PIPER: an FFT-based protein docking program with pairwise potentials. Proteins 65, 392-406
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4
  • 28
    • 0032571132 scopus 로고    scopus 로고
    • Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli
    • Sachdev, D., and Chirgwin, J. M. (1998) Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli. Biochem. Biophys. Res. Commun. 244, 933-937
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 933-937
    • Sachdev, D.1    Chirgwin, J.M.2
  • 29
    • 84925411269 scopus 로고    scopus 로고
    • Positional effects of fusion partners on the yield and solubility of MBP fusion proteins
    • Raran-Kurussi, S., Keefe, K., and Waugh, D. S. (2015) Positional effects of fusion partners on the yield and solubility of MBP fusion proteins. Protein Expr. Purif. 110, 159-164
    • (2015) Protein Expr. Purif. , vol.110 , pp. 159-164
    • Raran-Kurussi, S.1    Keefe, K.2    Waugh, D.S.3
  • 30
    • 34247516876 scopus 로고    scopus 로고
    • The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
    • Vera, A., González-Montalbán, N., Arís, A., and Villaverde, A. (2007) The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol. Bioeng. 96, 1101-1106
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 1101-1106
    • Vera, A.1    González-Montalbán, N.2    Arís, A.3    Villaverde, A.4
  • 31
    • 0037449762 scopus 로고    scopus 로고
    • Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase
    • Francin, M., and Mirande, M. (2003) Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase. J. Biol. Chem. 278, 1472-1479
    • (2003) J. Biol. Chem. , vol.278 , pp. 1472-1479
    • Francin, M.1    Mirande, M.2
  • 32
    • 84868091682 scopus 로고    scopus 로고
    • Cell-free production of trimeric influenza hemagglutinin head domain proteins as vaccine antigens
    • Welsh, J. P., Lu, Y., He, X. S., Greenberg, H. B., and Swartz, J. R. (2012) Cell-free production of trimeric influenza hemagglutinin head domain proteins as vaccine antigens. Biotechnol. Bioeng. 109, 2962-2969
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 2962-2969
    • Welsh, J.P.1    Lu, Y.2    He, X.S.3    Greenberg, H.B.4    Swartz, J.R.5
  • 34
    • 77955411860 scopus 로고    scopus 로고
    • Properly folded bacterially expressed H1N1 hemagglutinin globular head and ectodomain vaccines protect ferrets against H1N1 pandemic influenza virus
    • Khurana, S., Verma, S., Verma, N., Crevar, C. J., Carter, D. M., Manischewitz, J., King, L. R., Ross, T. M., and Golding, H. (2010) Properly folded bacterially expressed H1N1 hemagglutinin globular head and ectodomain vaccines protect ferrets against H1N1 pandemic influenza virus. PLoS One 5, e11548
    • (2010) PLoS One , vol.5 , pp. e11548
    • Khurana, S.1    Verma, S.2    Verma, N.3    Crevar, C.J.4    Carter, D.M.5    Manischewitz, J.6    King, L.R.7    Ross, T.M.8    Golding, H.9
  • 35
    • 32544449619 scopus 로고    scopus 로고
    • Characterization of live influenza vaccine donor strain derived from cold-adaptation of X-31 virus
    • Lee, K.H., Seo, S. U., Song, J. M., Lee,C.M., Kim, H. A., and Seong, B. L. (2006) Characterization of live influenza vaccine donor strain derived from cold-adaptation of X-31 virus. Vaccine 24, 1966-1974
    • (2006) Vaccine , vol.24 , pp. 1966-1974
    • Lee, K.H.1    Seo, S.U.2    Song, J.M.3    Lee, C.M.4    Kim, H.A.5    Seong, B.L.6
  • 36
    • 84959150699 scopus 로고    scopus 로고
    • Genetic analysis of attenuation markers of cold-adapted X-31 influenza live vaccine donor strain
    • Jang, Y. H., Jung, E. J., Lee, K. H., Byun, Y. H., Yang, S. W., and Seong, B. L. (2016) Genetic analysis of attenuation markers of cold-adapted X-31 influenza live vaccine donor strain. Vaccine 34, 1343-1349
    • (2016) Vaccine , vol.34 , pp. 1343-1349
    • Jang, Y.H.1    Jung, E.J.2    Lee, K.H.3    Byun, Y.H.4    Yang, S.W.5    Seong, B.L.6
  • 37
    • 62549125006 scopus 로고    scopus 로고
    • RNA-mediated chaperone type for de novo protein folding
    • Choi, S. I.,Ryu,K., and Seong,B. L. (2009)RNA-mediated chaperone type for de novo protein folding. RNA Biol. 6, 21-24
    • (2009) RNA Biol. , vol.6 , pp. 21-24
    • Choi, S.I.1    Ryu, K.2    Seong, B.L.3
  • 38
    • 0029163563 scopus 로고
    • RNAchaperones andtheRNAfoldingproblem
    • Herschlag,D. (1995)RNAchaperones andtheRNAfoldingproblem. J. Biol. Chem. 270, 20871-20874
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 41
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley, D. C., Wilson, I. A., and Skehel, J. J. (1981) Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289, 373-378
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 43
    • 78651396311 scopus 로고    scopus 로고
    • Bacterial HA1 vaccine against pandemic H5N1 influenza virus: Evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets
    • Khurana, S., Verma, S., Verma, N., Crevar, C. J., Carter, D. M., Manischewitz, J., King, L. R., Ross, T. M., and Golding, H. (2011) Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets. J. Virol. 85, 1246-1256
    • (2011) J. Virol. , vol.85 , pp. 1246-1256
    • Khurana, S.1    Verma, S.2    Verma, N.3    Crevar, C.J.4    Carter, D.M.5    Manischewitz, J.6    King, L.R.7    Ross, T.M.8    Golding, H.9
  • 45
    • 34250017377 scopus 로고    scopus 로고
    • Structure and function of RbcX, an assembly chaperone for hexadecameric rubisco
    • Saschenbrecker, S., Bracher, A., Rao, K. V., Rao, B. V.,Hartl, F. U., and Hayer-Hartl, M. (2007) Structure and function of RbcX, an assembly chaperone for hexadecameric rubisco. Cell 129, 1189-1200
    • (2007) Cell , vol.129 , pp. 1189-1200
    • Saschenbrecker, S.1    Bracher, A.2    Rao, K.V.3    Rao, B.V.4    Hartl, F.U.5    Hayer-Hartl, M.6
  • 46
    • 84856006671 scopus 로고    scopus 로고
    • Influence of physiological state of Escherichia coli cells on the expression of soluble protein-recombinant analog of glycoprotein G of herpes simplex virus of type 2
    • Korshun, L. N., Moǐsa, L. N., Ganova, L. A., Vudmaska, M. I., Kovtoniuk,G. V.,Kiseleva, E. K., and Spivak,NIa. (2011) [Influence of physiological state of Escherichia coli cells on the expression of soluble protein-recombinant analog of glycoprotein G of herpes simplex virus of type 2]. Mikrobiol. Z. 73, 36-46
    • (2011) Mikrobiol. Z. , vol.73 , pp. 36-46
    • Korshun, L.N.1    Moǐsa, L.N.2    Ganova, L.A.3    Vudmaska, M.I.4    Kovtoniuk, G.V.5    Kiseleva, E.K.6    Spivak, N.I.7
  • 47
    • 0031456444 scopus 로고    scopus 로고
    • Aminoacyl-tRNAsynthetases
    • Cusack, S. (1997)Aminoacyl-tRNAsynthetases. Curr.Opin. Struct. Biol. 7, 881-889
    • (1997) Curr.Opin. Struct. Biol. , vol.7 , pp. 881-889
    • Cusack, S.1
  • 48
    • 0022972506 scopus 로고
    • Cytotoxic T lymphocytes recognize influenza haemagglutinin that lacks a signal sequence
    • Townsend, A. R., Bastin, J., Gould, K., and Brownlee, G. G. (1986) Cytotoxic T lymphocytes recognize influenza haemagglutinin that lacks a signal sequence. Nature 324, 575-577
    • (1986) Nature , vol.324 , pp. 575-577
    • Townsend, A.R.1    Bastin, J.2    Gould, K.3    Brownlee, G.G.4
  • 49
    • 0026014942 scopus 로고
    • Characterization of two distinct major histocompatibility complex class i Kk-restricted T-cell epitopes within the influenza A/PR/8/34 virus hemagglutinin
    • Gould, K. G., Scotney, H., and Brownlee, G. G. (1991) Characterization of two distinct major histocompatibility complex class I Kk-restricted T-cell epitopes within the influenza A/PR/8/34 virus hemagglutinin. J. Virol. 65, 5401-5409
    • (1991) J. Virol. , vol.65 , pp. 5401-5409
    • Gould, K.G.1    Scotney, H.2    Brownlee, G.G.3
  • 50
    • 0023525835 scopus 로고
    • Mouse H-2k-restricted cytotoxic T cells recognize antigenic determinants in both the HA1 and HA2 subunits of the influenza A/PR/8/34 hemagglutinin
    • Gould, K. G., Scotney,H., Townsend, A. R., Bastin, J., and Brownlee, G. G. (1987) Mouse H-2k-restricted cytotoxic T cells recognize antigenic determinants in both the HA1 and HA2 subunits of the influenza A/PR/8/34 hemagglutinin. J. Exp. Med. 166, 693-701
    • (1987) J. Exp. Med. , vol.166 , pp. 693-701
    • Gould, K.G.1    Scotney, H.2    Townsend, A.R.3    Bastin, J.4    Brownlee, G.G.5
  • 51
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark, E. D. B. (1998) Refolding of recombinant proteins. Curr. Opin. Biotechnol. 9, 157-163
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 157-163
    • Clark, E.D.B.1
  • 52
    • 84921676353 scopus 로고    scopus 로고
    • Rapid production of synthetic influenza vaccines
    • Dormitzer, P. R. (2015) Rapid production of synthetic influenza vaccines. Curr. Top. Microbiol. Immunol. 386, 237-273
    • (2015) Curr. Top. Microbiol. Immunol. , vol.386 , pp. 237-273
    • Dormitzer, P.R.1
  • 53
    • 84897552314 scopus 로고    scopus 로고
    • Pandemic preparedness and response-lessons from the H1N1 influenza of 2009
    • Fineberg, H. V. (2014) Pandemic preparedness and response-lessons from the H1N1 influenza of 2009. N. Engl. J. Med. 370, 1335-1342
    • (2014) N. Engl. J. Med. , vol.370 , pp. 1335-1342
    • Fineberg, H.V.1
  • 54
    • 77953964469 scopus 로고    scopus 로고
    • The production of hemagglutininbased virus-like particles in plants: A rapid, efficient and safe response to pandemic influenza
    • D'Aoust,M. A., Couture, M. M., Charland, N., Trépanier, S., Landry, N.,Ors, F., and Vézina, L. P. (2010) The production of hemagglutininbased virus-like particles in plants: a rapid, efficient and safe response to pandemic influenza. Plant Biotechnol. J. 8, 607-619
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 607-619
    • D'Aoust, M.A.1    Couture, M.M.2    Charland, N.3    Trépanier, S.4    Landry, N.5    Ors, F.6    Vézina, L.P.7
  • 57
    • 0031793228 scopus 로고    scopus 로고
    • An isoleucine zipper peptide forms a native-like triple stranded coiled coil in solution
    • Suzuki, K., Hiroaki, H., Kohda, D., and Tanaka, T. (1998) An isoleucine zipper peptide forms a native-like triple stranded coiled coil in solution. Protein Eng. 11, 1051-1055
    • (1998) Protein Eng. , vol.11 , pp. 1051-1055
    • Suzuki, K.1    Hiroaki, H.2    Kohda, D.3    Tanaka, T.4
  • 58
    • 1642363339 scopus 로고    scopus 로고
    • Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin
    • Güthe, S., Kapinos, L., Möglich, A., Meier, S., Grzesiek, S., and Kiefhaber, T. (2004) Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin. J. Mol. Biol. 337, 905-915
    • (2004) J. Mol. Biol. , vol.337 , pp. 905-915
    • Güthe, S.1    Kapinos, L.2    Möglich, A.3    Meier, S.4    Grzesiek, S.5    Kiefhaber, T.6
  • 59
    • 84866403056 scopus 로고    scopus 로고
    • Sweeping away protein aggregation with entropic bristles: Intrinsically disordered protein fusions enhance soluble expression
    • Santner, A. A., Croy,C.H., Vasanwala, F.H.,Uversky, V.N., Van, Y. Y., and Dunker, A. K. (2012) Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression. Biochemistry 51, 7250-7262
    • (2012) Biochemistry , vol.51 , pp. 7250-7262
    • Santner, A.A.1    Croy, C.H.2    Vasanwala, F.H.3    Uversky, V.N.4    Van, Y.Y.5    Dunker, A.K.6
  • 60
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coliHsp70DnaK: IsDnaKaholdase or anunfoldase?
    • Slepenkov, S. V., and Witt, S. N. (2002) The unfolding story of the Escherichia coliHsp70DnaK: isDnaKaholdase or anunfoldase? Mol. Microbiol. 45, 1197-1206
    • (2002) Mol. Microbiol. , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 61
    • 84943450201 scopus 로고    scopus 로고
    • Impact of holdase chaperones Skp and SurA on the folding of b-barrel outermembrane proteins.Nat
    • Thoma, J., Burmann, B.M.,Hiller, S., andMüller,D. J. (2015) Impact of holdase chaperones Skp and SurA on the folding of b-barrel outermembrane proteins.Nat. Struct. Mol. Biol. 22, 795-802
    • (2015) Struct. Mol. Biol. , vol.22 , pp. 795-802
    • Thoma, J.1    Burmann, B.M.2    Hiller, S.3    Müller, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.