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Volumn 34, Issue 11, 2012, Pages 973-981

Chaperone discovery

Author keywords

Chaperone discovery; Hsp110; Hsp60; Hsp70; Hsp90; Protein folding

Indexed keywords

BETA GALACTOSIDASE; BETA LACTAMASE; BOVINE SERUM ALBUMIN; CHAPERONE; CHLORAMPHENICOL ACETYLTRANSFERASE; DSBA PROTEIN; FUNGAL PROTEIN; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 31; HEAT SHOCK PROTEIN 33; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MITOCHONDRIAL PROTEIN; OUTER MEMBRANE PROTEIN A; OUTER MEMBRANE PROTEIN F; PROTEIN DNAK; PROTEIN HDEA; PROTEIN SURA; PROTEINASE; RIBULOSEBISPHOSPHATE CARBOXYLASE; S PHASE KINASE ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84867463459     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.201200059     Document Type: Review
Times cited : (18)

References (102)
  • 2
    • 38449092312 scopus 로고    scopus 로고
    • Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
    • de Marco A. 2007. Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat Protoc 2: 2632- 9.
    • (2007) Nat Protoc , vol.2 , pp. 2632-2639
    • de Marco, A.1
  • 3
    • 34347374452 scopus 로고    scopus 로고
    • Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E coli
    • de Marco A, Deuerling E, Mogk A, Tomoyasu T, et al. 2007. Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E coli. BMC Biotechnol 7: 32.
    • (2007) BMC Biotechnol , vol.7 , pp. 32
    • de Marco, A.1    Deuerling, E.2    Mogk, A.3    Tomoyasu, T.4
  • 4
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. 2011. Molecular chaperones in protein folding and proteostasis. Nature 475: 324- 32.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 5
    • 62149096127 scopus 로고    scopus 로고
    • Use of folding modulators to improve heterologous protein production in Escherichia coli
    • Kolaj O, Spada S, Robin S, Wall JG. 2009. Use of folding modulators to improve heterologous protein production in Escherichia coli. Microb Cell Fact 8: 9.
    • (2009) Microb Cell Fact , vol.8 , pp. 9
    • Kolaj, O.1    Spada, S.2    Robin, S.3    Wall, J.G.4
  • 6
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
    • Feder ME, Hofmann GE. 1999. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol 61: 243- 82.
    • (1999) Annu Rev Physiol , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 8
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D. 2002. Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 59: 1640- 8.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 9
    • 0000012053 scopus 로고
    • Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous
    • Bardwell JC, Craig EA. 1984. Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc Natl Acad Sci USA 81: 848- 52.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 848-852
    • Bardwell, J.C.1    Craig, E.A.2
  • 10
    • 0023392855 scopus 로고
    • r 83,000 heat shock protein has a homolog in Escherichia coli
    • r 83, 000 heat shock protein has a homolog in Escherichia coli. Proc Natl Acad Sci USA 84: 5177- 81.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5177-5181
    • Bardwell, J.C.A.1    Craig, E.A.2
  • 13
    • 0043104253 scopus 로고
    • The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system
    • Zylicz M, LeBowitz JH, McMacken R, Georgopoulos C. 1983. The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc Natl Acad Sci USA 80: 6431- 5.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6431-6435
    • Zylicz, M.1    LeBowitz, J.H.2    McMacken, R.3    Georgopoulos, C.4
  • 14
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch WJ, Feramisco JR. 1984. Nuclear and nucleolar localization of the 72, 000-dalton heat shock protein in heat-shocked mammalian cells. J Biol Chem 259: 4501- 13.
    • (1984) J Biol Chem , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 15
    • 0022327491 scopus 로고
    • Involvement of ATP in the nuclear and nucleolar functions of the 70kd heat shock protein
    • Lewis MJ, Pelham HR. 1985. Involvement of ATP in the nuclear and nucleolar functions of the 70kd heat shock protein. EMBO J 4: 3137- 43.
    • (1985) EMBO J , vol.4 , pp. 3137-3143
    • Lewis, M.J.1    Pelham, H.R.2
  • 16
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose-regulated proteins
    • Pelham HR. 1986. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46: 959- 61.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.1
  • 18
    • 0018791259 scopus 로고
    • Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly
    • Hohn T, Hohn B, Engel A, Wurtz M, et al. 1979. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. J Mol Biol 129: 359- 73.
    • (1979) J Mol Biol , vol.129 , pp. 359-373
    • Hohn, T.1    Hohn, B.2    Engel, A.3    Wurtz, M.4
  • 19
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts
    • Barraclough R, Ellis RJ. 1980. Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim Biophys Acta 608: 19- 31.
    • (1980) Biochim Biophys Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 20
    • 0023900525 scopus 로고
    • Homologous plant and bacterial proteins chaperone oligomeric protein assembly
    • Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, et al. 1988. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333: 330- 4.
    • (1988) Nature , vol.333 , pp. 330-334
    • Hemmingsen, S.M.1    Woolford, C.2    van der Vies, S.M.3    Tilly, K.4
  • 21
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J. 1987. Proteins as molecular chaperones. Nature 328: 378- 9.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 22
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP
    • Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH. 1989. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342: 884- 9.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 23
    • 0024972083 scopus 로고
    • Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng MY, Hartl FU, Martin J, Pollock RA, et al. 1989. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337: 620- 5.
    • (1989) Nature , vol.337 , pp. 620-625
    • Cheng, M.Y.1    Hartl, F.U.2    Martin, J.3    Pollock, R.A.4
  • 24
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann J, Horwich AL, Neupert W, Hartl FU. 1989. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341: 125- 30.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.U.4
  • 25
    • 29344458115 scopus 로고    scopus 로고
    • Chaperone-like features of bovine serum albumin: a comparison with alpha-crystallin
    • Marini I, Moschini R, Del Corso A, Mura U. 2005. Chaperone-like features of bovine serum albumin: a comparison with alpha-crystallin. Cell Mol Life Sci 62: 3092- 9.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 3092-3099
    • Marini, I.1    Moschini, R.2    Del Corso, A.3    Mura, U.4
  • 26
    • 82955223952 scopus 로고    scopus 로고
    • Protein aggregation: opposing effects of chaperones and crowding
    • Wyttenbach A, O'Connor V, eds; New York, USA: Springer
    • Ellis RJ. 2011. Protein aggregation: opposing effects of chaperones and crowding In Wyttenbach A, O'Connor V, eds; Folding for the Synapse. New York, USA: Springer. p. 9- 34.
    • (2011) Folding for the Synapse , pp. 9-34
    • Ellis, R.J.1
  • 27
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. 2006. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271- 94.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 29
    • 77950600645 scopus 로고    scopus 로고
    • Mechanisms of the Hsp70 chaperone system
    • Young JC. 2010. Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol 88: 291- 300.
    • (2010) Biochem Cell Biol , vol.88 , pp. 291-300
    • Young, J.C.1
  • 30
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: towards a characterization of the heat-shock protein 70 family
    • Rassow J, vonAhsen O, Bomer U, Pfanner N. 1997. Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol 7: 129- 33.
    • (1997) Trends Cell Biol , vol.7 , pp. 129-133
    • Rassow, J.1    vonAhsen, O.2    Bomer, U.3    Pfanner, N.4
  • 31
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis
    • Voos W, Rottgers K. 2002. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592: 51- 62.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 51-62
    • Voos, W.1    Rottgers, K.2
  • 32
    • 0024894102 scopus 로고
    • Expression of members of the Saccharomyces cerevisiae Hsp70 multigene family
    • Werner-Washburne M, Craig EA. 1989. Expression of members of the Saccharomyces cerevisiae Hsp70 multigene family. Genome 31: 684- 9.
    • (1989) Genome , vol.31 , pp. 684-689
    • Werner-Washburne, M.1    Craig, E.A.2
  • 33
    • 15444360108 scopus 로고    scopus 로고
    • Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae
    • Lussier M, White AM, Sheraton J, diPaolo T, et al. 1997. Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics 147: 435- 50.
    • (1997) Genetics , vol.147 , pp. 435-450
    • Lussier, M.1    White, A.M.2    Sheraton, J.3    Dipaolo, T.4
  • 34
  • 35
    • 0023387587 scopus 로고
    • Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form
    • Crooke E, Wickner W. 1987. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc Natl Acad Sci USA 84: 5216- 20.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5216-5220
    • Crooke, E.1    Wickner, W.2
  • 36
    • 0024295389 scopus 로고
    • ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle
    • Crooke E, Guthrie B, Lecker S, Lill R, et al. 1988. ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle. Cell 54: 1003- 11.
    • (1988) Cell , vol.54 , pp. 1003-1011
    • Crooke, E.1    Guthrie, B.2    Lecker, S.3    Lill, R.4
  • 37
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp T, Hauser S, Lutcke H, Bukau B. 1996. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci USA 93: 4437- 41.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lutcke, H.3    Bukau, B.4
  • 38
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides
    • Valent QA, Kendall DA, High S, Kusters R, et al. 1995. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J 14: 5494- 505.
    • (1995) EMBO J , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4
  • 39
    • 57649242773 scopus 로고    scopus 로고
    • Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp
    • Jarchow S, Luck C, Gorg A, Skerra A. 2008. Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp. Proteomics 8: 4987- 94.
    • (2008) Proteomics , vol.8 , pp. 4987-4994
    • Jarchow, S.1    Luck, C.2    Gorg, A.3    Skerra, A.4
  • 40
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen R, Henning U. 1996. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol 19: 1287- 94.
    • (1996) Mol Microbiol , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 41
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama S, Tajima T, Tokuda H. 1995. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J 14: 3365- 72.
    • (1995) EMBO J , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 42
    • 0034653760 scopus 로고    scopus 로고
    • Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli
    • Kitagawa M, Matsumura Y, Tsuchido T. 2000. Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli. FEMS Microbiol Lett 184: 165- 71.
    • (2000) FEMS Microbiol Lett , vol.184 , pp. 165-171
    • Kitagawa, M.1    Matsumura, Y.2    Tsuchido, T.3
  • 43
    • 0026784986 scopus 로고
    • Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
    • Allen SP, Polazzi JO, Gierse JK, Easton AM. 1992. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J Bacteriol 174: 6938- 47.
    • (1992) J Bacteriol , vol.174 , pp. 6938-6947
    • Allen, S.P.1    Polazzi, J.O.2    Gierse, J.K.3    Easton, A.M.4
  • 44
    • 0039870135 scopus 로고    scopus 로고
    • IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock
    • Laskowska E, Wawrzynow A, Taylor A. 1996. IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock. Biochimie 78: 117- 22.
    • (1996) Biochimie , vol.78 , pp. 117-122
    • Laskowska, E.1    Wawrzynow, A.2    Taylor, A.3
  • 45
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U, Muse W, Eser M, Bardwell JC. 1999. Chaperone activity with a redox switch. Cell 96: 341- 52.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 46
    • 1242297805 scopus 로고    scopus 로고
    • Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions
    • Mujacic M, Bader MW, Baneyx F. 2004. Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions. Mol Microbiol 51: 849- 59.
    • (2004) Mol Microbiol , vol.51 , pp. 849-859
    • Mujacic, M.1    Bader, M.W.2    Baneyx, F.3
  • 47
    • 0037195791 scopus 로고    scopus 로고
    • Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures
    • Sastry MS, Korotkov K, Brodsky Y, Baneyx F. 2002. Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures. J Biol Chem 277: 46026- 34.
    • (2002) J Biol Chem , vol.277 , pp. 46026-46034
    • Sastry, M.S.1    Korotkov, K.2    Brodsky, Y.3    Baneyx, F.4
  • 48
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Tormo A, Almiron M, Kolter R. 1990. surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339- 47.
    • (1990) J Bacteriol , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almiron, M.2    Kolter, R.3
  • 49
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar SW, Kolter R. 1996. SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770- 3.
    • (1996) J Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 50
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas D, Betton JM, Raina S. 1996. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol 21: 871- 84.
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 51
    • 0029839533 scopus 로고    scopus 로고
    • Identification of sigma S-dependent genes associated with the stationary-phase acid-resistance phenotype of Shigella flexneri
    • Waterman SR, Small PL. 1996. Identification of sigma S-dependent genes associated with the stationary-phase acid-resistance phenotype of Shigella flexneri. Mol Microbiol 21: 925- 40.
    • (1996) Mol Microbiol , vol.21 , pp. 925-940
    • Waterman, S.R.1    Small, P.L.2
  • 52
    • 22844435320 scopus 로고    scopus 로고
    • Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation
    • Hong W, Jiao W, Hu J, Zhang J, et al. 2005. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem 280: 27029- 34.
    • (2005) J Biol Chem , vol.280 , pp. 27029-27034
    • Hong, W.1    Jiao, W.2    Hu, J.3    Zhang, J.4
  • 53
    • 65249182171 scopus 로고    scopus 로고
    • Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding
    • Tapley TL, Korner JL, Barge MT, Hupfeld J, et al. 2009. Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc Natl Acad Sci USA 106: 5557- 62.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5557-5562
    • Tapley, T.L.1    Korner, J.L.2    Barge, M.T.3    Hupfeld, J.4
  • 54
    • 0036889029 scopus 로고    scopus 로고
    • Gene expression profiling of the pH response in Escherichia coli
    • Tucker DL, Tucker N, Conway T. 2002. Gene expression profiling of the pH response in Escherichia coli. J Bacteriol 184: 6551- 8.
    • (2002) J Bacteriol , vol.184 , pp. 6551-6558
    • Tucker, D.L.1    Tucker, N.2    Conway, T.3
  • 55
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C, Beil A, Ehrmann M. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97: 339- 47.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 56
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer T, Sawa J, Schafer E, Saibil HR, et al. 2008. Structural basis for the regulated protease and chaperone function of DegP. Nature 453: 885- 90.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4
  • 57
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: life on the verge of death
    • Richter K, Haslbeck M, Buchner J. 2010. The heat shock response: life on the verge of death. Mol Cell 40: 253- 66.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 58
    • 77956006894 scopus 로고    scopus 로고
    • Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function
    • Welker S, Rudolph B, Frenzel E, Hagn F, et al. 2010. Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol Cell 39: 507- 20.
    • (2010) Mol Cell , vol.39 , pp. 507-520
    • Welker, S.1    Rudolph, B.2    Frenzel, E.3    Hagn, F.4
  • 60
    • 0034651793 scopus 로고    scopus 로고
    • Structure of Hsp15 reveals a novel RNA-binding motif
    • Staker BL, Korber P, Bardwell JCA, Saper MA. 2000. Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J 19: 749- 57.
    • (2000) EMBO J , vol.19 , pp. 749-757
    • Staker, B.L.1    Korber, P.2    Bardwell, J.C.A.3    Saper, M.A.4
  • 62
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the Hsp90 chaperone
    • Zhao RM, Davey M, Hsu YC, Kaplanek P, et al. 2005. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the Hsp90 chaperone. Cell 120: 715- 27.
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.M.1    Davey, M.2    Hsu, Y.C.3    Kaplanek, P.4
  • 63
    • 23644442058 scopus 로고    scopus 로고
    • Colony filtration blot: a new screening method for soluble protein expression in Escherichia coli
    • Cornvik T, Dahlroth SL, Magnusdottir A, Herman MD, et al. 2005. Colony filtration blot: a new screening method for soluble protein expression in Escherichia coli. Nat Methods 2: 507- 9.
    • (2005) Nat Methods , vol.2 , pp. 507-509
    • Cornvik, T.1    Dahlroth, S.L.2    Magnusdottir, A.3    Herman, M.D.4
  • 64
    • 33847624936 scopus 로고    scopus 로고
    • Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Boudet J, Guilligay D, Mas PJ, et al. 2007. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat Struct Mol Biol 14: 229- 33.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 229-233
    • Tarendeau, F.1    Boudet, J.2    Guilligay, D.3    Mas, P.J.4
  • 65
    • 58449090154 scopus 로고    scopus 로고
    • Expression of Helicobacter pylori CagA domains by library-based construct screening
    • Angelini A, Tosi T, Mas P, Acajjaoui S, et al. 2009. Expression of Helicobacter pylori CagA domains by library-based construct screening. FEBS J 276: 816- 24.
    • (2009) FEBS J , vol.276 , pp. 816-824
    • Angelini, A.1    Tosi, T.2    Mas, P.3    Acajjaoui, S.4
  • 66
    • 33644874198 scopus 로고    scopus 로고
    • Combinatorial library approaches for improving soluble protein expression in Escherichia coli
    • Hart DJ, Tarendeau F. 2006. Combinatorial library approaches for improving soluble protein expression in Escherichia coli. Acta Crystallogr D 62: 19- 26.
    • (2006) Acta Crystallogr D , vol.62 , pp. 19-26
    • Hart, D.J.1    Tarendeau, F.2
  • 68
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley WC, Stidham RD, Smith NM, Hunt JF, et al. 2001. Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat Biotechnol 19: 131- 6.
    • (2001) Nat Biotechnol , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4
  • 71
    • 35748932042 scopus 로고    scopus 로고
    • An activity-independent selection system of thermostable protein variants
    • Chautard H, Blas-Galindo E, Menguy T, Grand'Moursel L, et al. 2007. An activity-independent selection system of thermostable protein variants. Nat Methods 4: 919- 21.
    • (2007) Nat Methods , vol.4 , pp. 919-921
    • Chautard, H.1    Blas-Galindo, E.2    Menguy, T.3    Grand'Moursel, L.4
  • 72
    • 33646113145 scopus 로고    scopus 로고
    • Improving protein solubility: the use of the Escherichia coli dihydrofolate reductase gene as a fusion reporter
    • Liu JW, Boucher Y, Stokes HW, Ollis DL. 2006. Improving protein solubility: the use of the Escherichia coli dihydrofolate reductase gene as a fusion reporter. Protein Expres Purif 47: 258- 63.
    • (2006) Protein Expres Purif , vol.47 , pp. 258-263
    • Liu, J.W.1    Boucher, Y.2    Stokes, H.W.3    Ollis, D.L.4
  • 73
    • 44349116166 scopus 로고    scopus 로고
    • Identification of soluble protein fragments by gene fragmentation and genetic selection
    • Dyson MR, Perera RL, Shadbolt SP, Biderman L, et al. 2008. Identification of soluble protein fragments by gene fragmentation and genetic selection. Nucleic Acids Res 36: e51.
    • (2008) Nucleic Acids Res , vol.36
    • Dyson, M.R.1    Perera, R.L.2    Shadbolt, S.P.3    Biderman, L.4
  • 74
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber V, Martinez CA, Arnold FH. 2001. Libraries of hybrid proteins from distantly related sequences. Nat Biotechnol 19: 456- 60.
    • (2001) Nat Biotechnol , vol.19 , pp. 456-460
    • Sieber, V.1    Martinez, C.A.2    Arnold, F.H.3
  • 76
    • 0037304389 scopus 로고    scopus 로고
    • Genetic screens and directed evolution for protein solubility
    • Waldo GS. 2003. Genetic screens and directed evolution for protein solubility. Curr Opin Chem Biol 7: 33- 8.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 33-38
    • Waldo, G.S.1
  • 77
    • 0034816151 scopus 로고    scopus 로고
    • Random PCR-based screening for soluble domains using green fluorescent protein
    • Kawasaki M, Inagaki F. 2001. Random PCR-based screening for soluble domains using green fluorescent protein. Biochem Bioph Res Co 280: 842- 4.
    • (2001) Biochem Bioph Res Co , vol.280 , pp. 842-844
    • Kawasaki, M.1    Inagaki, F.2
  • 78
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous S, Terwilliger TC, Waldo GS. 2005. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat Biotechnol 23: 102- 7.
    • (2005) Nat Biotechnol , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 80
    • 0037436408 scopus 로고    scopus 로고
    • FRET-based in vivo screening for protein folding and increased protein stability
    • Philipps B, Hennecke J, Glockshuber R. 2003. FRET-based in vivo screening for protein folding and increased protein stability. J Mol Biol 327: 239- 49.
    • (2003) J Mol Biol , vol.327 , pp. 239-249
    • Philipps, B.1    Hennecke, J.2    Glockshuber, R.3
  • 81
    • 79952363991 scopus 로고    scopus 로고
    • Genetic selection designed to stabilize proteins uncovers a chaperone called Spy
    • Quan S, Koldewey P, Tapley T, Kirsch N, et al. 2011. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol 18: 262- 9.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 262-269
    • Quan, S.1    Koldewey, P.2    Tapley, T.3    Kirsch, N.4
  • 82
    • 26444492138 scopus 로고    scopus 로고
    • Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis
    • Cabantous S, Pedelacq JD, Mark BL, Naranjo C, et al. 2005. Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis. J Struct Funct Genomics 6: 113- 9.
    • (2005) J Struct Funct Genomics , vol.6 , pp. 113-119
    • Cabantous, S.1    Pedelacq, J.D.2    Mark, B.L.3    Naranjo, C.4
  • 83
    • 78650530108 scopus 로고    scopus 로고
    • In vivo protein stabilization based on fragment complementation and a split GFP system
    • Lindman S, Hernandez-Garcia A, Szczepankiewicz O, Frohm B, et al. 2010. In vivo protein stabilization based on fragment complementation and a split GFP system. Proc Natl Acad Sci USA 107: 19826- 31.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19826-19831
    • Lindman, S.1    Hernandez-Garcia, A.2    Szczepankiewicz, O.3    Frohm, B.4
  • 84
    • 33750449952 scopus 로고    scopus 로고
    • A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide
    • Kim W, Kim Y, Min J, Kim DJ, et al. 2006. A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. ACS Chem Biol 1: 461- 9.
    • (2006) ACS Chem Biol , vol.1 , pp. 461-469
    • Kim, W.1    Kim, Y.2    Min, J.3    Kim, D.J.4
  • 85
    • 78649692108 scopus 로고    scopus 로고
    • Novel fluorescence-assisted whole-cell assay for engineering and characterization of proteases and their substrates
    • Kostallas G, Samuelson P. 2010. Novel fluorescence-assisted whole-cell assay for engineering and characterization of proteases and their substrates. Appl Environ Microbiol 76: 7500- 8.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 7500-7508
    • Kostallas, G.1    Samuelson, P.2
  • 86
    • 0025940629 scopus 로고
    • The 2-hybrid system - a method to identify and clone genes for proteins that interact with a protein of interest
    • Chien CT, Bartel PL, Sternglanz R, Fields S. 1991. The 2-hybrid system - a method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci USA 88: 9578- 82.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 87
    • 33846276121 scopus 로고    scopus 로고
    • Exploiting elements of transcriptional machinery to enhance protein stability
    • Barakat NH, Barakat NH, Carmody LJ, Love JJ. 2007. Exploiting elements of transcriptional machinery to enhance protein stability. J Mol Biol 366: 103- 16.
    • (2007) J Mol Biol , vol.366 , pp. 103-116
    • Barakat, N.H.1    Barakat, N.H.2    Carmody, L.J.3    Love, J.J.4
  • 88
    • 77956578906 scopus 로고    scopus 로고
    • Combined use of experimental and computational screens to characterize protein stability
    • Barakat NH, Barakat NH, Love JJ. 2010. Combined use of experimental and computational screens to characterize protein stability. Protein Eng Des Sel 23: 799- 807.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 799-807
    • Barakat, N.H.1    Barakat, N.H.2    Love, J.J.3
  • 89
    • 33644536727 scopus 로고    scopus 로고
    • Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway
    • Fisher AC, Kim W, DeLisa MP. 2006. Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway. Protein Sci 15: 449- 58.
    • (2006) Protein Sci , vol.15 , pp. 449-458
    • Fisher, A.C.1    Kim, W.2    DeLisa, M.P.3
  • 90
    • 73149084215 scopus 로고    scopus 로고
    • Mining mammalian genomes for folding competent proteins using Tat-dependent genetic selection in Escherichia coli
    • Lim HK, Mansell TJ, Linderman SW, Fisher AC, et al. 2009. Mining mammalian genomes for folding competent proteins using Tat-dependent genetic selection in Escherichia coli. Protein Sci 18: 2537- 49.
    • (2009) Protein Sci , vol.18 , pp. 2537-2549
    • Lim, H.K.1    Mansell, T.J.2    Linderman, S.W.3    Fisher, A.C.4
  • 91
    • 78650143172 scopus 로고    scopus 로고
    • Sorting things out through endoplasmic reticulum quality control
    • Tamura T, Sunryd JC, Hebert DN. 2010. Sorting things out through endoplasmic reticulum quality control. Mol Membr Biol 27: 412- 27.
    • (2010) Mol Membr Biol , vol.27 , pp. 412-427
    • Tamura, T.1    Sunryd, J.C.2    Hebert, D.N.3
  • 92
    • 77249117783 scopus 로고    scopus 로고
    • A versatile selection system for folding competent proteins using genetic complementation in a eukaryotic host
    • Lyngso C, Kjaerulff S, Muller S, Bratt T, et al. 2010. A versatile selection system for folding competent proteins using genetic complementation in a eukaryotic host. Protein Sci 19: 579- 92.
    • (2010) Protein Sci , vol.19 , pp. 579-592
    • Lyngso, C.1    Kjaerulff, S.2    Muller, S.3    Bratt, T.4
  • 93
    • 63449128473 scopus 로고    scopus 로고
    • Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum
    • Jonikas MC, Collins SR, Denic V, Oh E, et al. 2009. Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323: 1693- 7.
    • (2009) Science , vol.323 , pp. 1693-1697
    • Jonikas, M.C.1    Collins, S.R.2    Denic, V.3    Oh, E.4
  • 94
    • 34249880371 scopus 로고    scopus 로고
    • An online monitoring system based on a synthetic sigma32-dependent tandem promoter for visualization of insoluble proteins in the cytoplasm of Escherichia coli
    • Kraft M, Knupfer U, Wenderoth R, Pietschmann P, et al. 2007. An online monitoring system based on a synthetic sigma32-dependent tandem promoter for visualization of insoluble proteins in the cytoplasm of Escherichia coli. Appl Microbiol Biotechnol 75: 397- 406.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 397-406
    • Kraft, M.1    Knupfer, U.2    Wenderoth, R.3    Pietschmann, P.4
  • 95
    • 34648827854 scopus 로고    scopus 로고
    • A dual expression platform to optimize the soluble production of heterologous proteins in the periplasm of Escherichia coli
    • Kraft M, Knupfer U, Wenderoth R, Kacholdt A, et al. 2007. A dual expression platform to optimize the soluble production of heterologous proteins in the periplasm of Escherichia coli. Appl Microbiol Biotechnol 76: 1413- 22.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 1413-1422
    • Kraft, M.1    Knupfer, U.2    Wenderoth, R.3    Kacholdt, A.4
  • 96
    • 0036213467 scopus 로고    scopus 로고
    • Gene expression response to misfolded protein as a screen for soluble recombinant protein
    • Lesley SA, Graziano J, Cho CY, Knuth MW, et al. 2002. Gene expression response to misfolded protein as a screen for soluble recombinant protein. Protein Eng 15: 153- 60.
    • (2002) Protein Eng , vol.15 , pp. 153-160
    • Lesley, S.A.1    Graziano, J.2    Cho, C.Y.3    Knuth, M.W.4
  • 97
    • 84857148223 scopus 로고    scopus 로고
    • Chemical chaperones assist intracellular folding to buffer mutational variations
    • Bandyopadhyay A, Saxena K, Kasturia N, Dalal V, et al. 2012. Chemical chaperones assist intracellular folding to buffer mutational variations. Nat Chem Biol 8: 238- 45.
    • (2012) Nat Chem Biol , vol.8 , pp. 238-245
    • Bandyopadhyay, A.1    Saxena, K.2    Kasturia, N.3    Dalal, V.4
  • 98
    • 77955870526 scopus 로고    scopus 로고
    • A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila
    • Zhang S, Binari R, Zhou R, Perrimon N. 2010. A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila. Genetics 184: 1165- 79.
    • (2010) Genetics , vol.184 , pp. 1165-1179
    • Zhang, S.1    Binari, R.2    Zhou, R.3    Perrimon, N.4
  • 99
    • 59249098430 scopus 로고    scopus 로고
    • An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
    • Wang J, Farr GW, Hall DH, Li F, et al. 2009. An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. PLoS Genet 5: e1000350.
    • (2009) PLoS Genet , vol.5
    • Wang, J.1    Farr, G.W.2    Hall, D.H.3    Li, F.4
  • 100
    • 0037184939 scopus 로고    scopus 로고
    • Directed evolution of substrate-optimized GroEL/S chaperonins
    • Wang JD, Herman C, Tipton KA, Gross CA, et al. 2002. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell 111: 1027- 39.
    • (2002) Cell , vol.111 , pp. 1027-1039
    • Wang, J.D.1    Herman, C.2    Tipton, K.A.3    Gross, C.A.4
  • 101
    • 77953083350 scopus 로고    scopus 로고
    • Directed evolution of the DnaK chaperone: mutations in the lid domain result in enhanced chaperone activity
    • Aponte RA, Zimmermann S, Reinstein J. 2010. Directed evolution of the DnaK chaperone: mutations in the lid domain result in enhanced chaperone activity. J Mol Biol 399: 154- 67.
    • (2010) J Mol Biol , vol.399 , pp. 154-167
    • Aponte, R.A.1    Zimmermann, S.2    Reinstein, J.3
  • 102
    • 0031004715 scopus 로고    scopus 로고
    • Chaperone properties of the bacterial periplasmic substrate-binding proteins
    • Richarme G, Caldas TD. 1997. Chaperone properties of the bacterial periplasmic substrate-binding proteins. J Biol Chem 272: 15607- 12.
    • (1997) J Biol Chem , vol.272 , pp. 15607-15612
    • Richarme, G.1    Caldas, T.D.2


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