Chaperone discovery
dc.contributor.author | Quan, Shu | en_US |
dc.contributor.author | Bardwell, James C. A. | en_US |
dc.date.accessioned | 2012-11-07T17:04:32Z | |
dc.date.available | 2014-01-07T14:51:07Z | en_US |
dc.date.issued | 2012-11 | en_US |
dc.identifier.citation | Quan, Shu; Bardwell, James C. A. (2012). "Chaperone discovery." BioEssays 34(11): 973-981. <http://hdl.handle.net/2027.42/94250> | en_US |
dc.identifier.issn | 0265-9247 | en_US |
dc.identifier.issn | 1521-1878 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/94250 | |
dc.description.abstract | Molecular chaperones assist de novo protein folding and facilitate the refolding of stress‐denatured proteins. The molecular chaperone concept was coined nearly 35 years ago, and since then, tremendous strides have been made in understanding how these factors support protein folding. Here, we focus on how various chaperone proteins were first identified to play roles in protein folding. Examples are used to illustrate traditional routes of chaperone discovery and point out their advantages and limitations. Recent advances, including the development of folding biosensors and promising methods for the stabilization of proteins in vivo, provide new routes for chaperone discovery. With new methods of chaperone discovery, the question as to whether we have discovered all the chaperones that exist is very pertinent: there may well be important new surprises on the horizon. The image depicts one method of monitoring protein folding, namely the coupling of protein folding to the host stress response. This review cover is the past, present, and future of chaperone discovery. | en_US |
dc.publisher | WILEY‐VCH Verlag | en_US |
dc.subject.other | Hsp110 | en_US |
dc.subject.other | Protein Folding | en_US |
dc.subject.other | Chaperone Discovery | en_US |
dc.subject.other | Hsp60 | en_US |
dc.subject.other | Hsp70 | en_US |
dc.subject.other | Hsp90 | en_US |
dc.title | Chaperone discovery | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Molecular, Cellular, and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, USA. | en_US |
dc.contributor.affiliationum | Department of Molecular, Cellular, and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.identifier.pmid | 22968800 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/94250/1/973_ftp.pdf | |
dc.identifier.doi | 10.1002/bies.201200059 | en_US |
dc.identifier.source | BioEssays | en_US |
dc.identifier.citedreference | Kawasaki M, Inagaki F. 2001. Random PCR‐based screening for soluble domains using green fluorescent protein. Biochem Bioph Res Co 280: 842 – 4. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Cabantous S, Rogers Y, Terwilliger TC, Waldo GS. 2008. New molecular reporters for rapid protein folding assays. PLoS ONE 3: e2387. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Barakat NH, Barakat NH, Carmody LJ, Love JJ. 2007. Exploiting elements of transcriptional machinery to enhance protein stability. J Mol Biol 366: 103 – 16. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Tamura T, Sunryd JC, Hebert DN. 2010. Sorting things out through endoplasmic reticulum quality control. Mol Membr Biol 27: 412 – 27. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Wang JD, Herman C, Tipton KA, Gross CA, et al. 2002. Directed evolution of substrate‐optimized GroEL/S chaperonins. Cell 111: 1027 – 39. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Richarme G, Caldas TD. 1997. Chaperone properties of the bacterial periplasmic substrate‐binding proteins. J Biol Chem 272: 15607 – 12. | en_US |
dc.identifier.citedreference | Chen B, Retzlaff M, Roos T, Frydman J. 2011. Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol 3: a004374. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Hartl FU, Bracher A, Hayer‐Hartl M. 2011. Molecular chaperones in protein folding and proteostasis. Nature 475: 324 – 32. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Feder ME, Hofmann GE. 1999. Heat‐shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol 61: 243 – 82. | en_US |
dc.identifier.citedreference | Vabulas RM, Raychaudhuri S, Hayer‐Hartl M, Hartl FU. 2010. Protein folding in the cytoplasm and the heat shock response. Cold Spring Harb Perspect Biol 2: a004390. | en_US |
dc.identifier.citedreference | Picard D. 2002. Heat‐shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 59: 1640 – 8. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Bardwell JCA, Craig EA. 1987. Eukaryotic M r 83,000 heat shock protein has a homolog in Escherichia coli. Proc Natl Acad Sci USA 84: 5177 – 81. | en_US |
dc.identifier.citedreference | Cowing DW, Bardwell JCA, Craig EA, Woolford C, et al. 1985. Consensus sequence for Escherichia coli heat‐shock gene promoters. Proc Natl Acad Sci USA 82: 2679 – 83. | en_US |
dc.identifier.citedreference | Lindquist S, Craig EA. 1988. The heat‐shock proteins. Annu Rev Genet 22: 631 – 77. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Lewis MJ, Pelham HR. 1985. Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein. EMBO J 4: 3137 – 43. | en_US |
dc.identifier.citedreference | Pelham HR. 1986. Speculations on the functions of the major heat shock and glucose‐regulated proteins. Cell 46: 959 – 61. | en_US |
dc.identifier.citedreference | Georgopoulos CP, Hendrix RW, Casjens SR, Kaiser AD. 1973. Host participation in bacteriophage lambda head assembly. J Mol Biol 76: 45 – 60. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Ellis J. 1987. Proteins as molecular chaperones. Nature 328: 378 – 9. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Pearl LH, Prodromou C. 2006. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271 – 94. | en_US |
dc.identifier.citedreference | Yebenes H, Mesa P, Munoz IG, Montoya G, et al. 2011. Chaperonins: two rings for folding. Trends Biochem Sci 36: 424 – 32. | en_US |
dc.identifier.citedreference | Young JC. 2010. Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol 88: 291 – 300. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Voos W, Rottgers K. 2002. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592: 51 – 62. | en_US |
dc.identifier.citedreference | Werner‐Washburne M, Craig EA. 1989. Expression of members of the Saccharomyces cerevisiae Hsp70 multigene family. Genome 31: 684 – 9. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Maier T, Ferbitz L, Deuerling E, Ban N. 2005. A cradle for new proteins: trigger factor at the ribosome. Curr Opin Struct Biol 15: 204 – 12. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Jakob U, Muse W, Eser M, Bardwell JC. 1999. Chaperone activity with a redox switch. Cell 96: 341 – 52. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Tormo A, Almiron M, Kolter R. 1990. surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339 – 47. | en_US |
dc.identifier.citedreference | Lazar SW, Kolter R. 1996. SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770 – 3. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Tucker DL, Tucker N, Conway T. 2002. Gene expression profiling of the pH response in Escherichia coli. J Bacteriol 184: 6551 – 8. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Richter K, Haslbeck M, Buchner J. 2010. The heat shock response: life on the verge of death. Mol Cell 40: 253 – 66. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Korber P, Zander T, Herschlag D, Bardwell JCA. 1999. A new heat shock protein that binds nucleic acids. J Biol Chem 274: 249 – 56. | en_US |
dc.identifier.citedreference | Staker BL, Korber P, Bardwell JCA, Saper MA. 2000. Structure of Hsp15 reveals a novel RNA‐binding motif. EMBO J 19: 749 – 57. | en_US |
dc.identifier.citedreference | Korber P, Stahl JM, Nierhaus KH, Bardwell JC. 2000. Hsp15: a ribosome‐associated heat shock protein. EMBO J 19: 741 – 8. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Hart DJ, Tarendeau F. 2006. Combinatorial library approaches for improving soluble protein expression in Escherichia coli. Acta Crystallogr D 62: 19 – 26. | en_US |
dc.identifier.citedreference | Waldo GS, Standish BM, Berendzen J, Terwilliger TC. 1999. Rapid protein‐folding assay using green fluorescent protein. Nat Biotechnol 17: 691 – 5. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Maxwell KL, Mittermaier AK, Forman‐Kay JD, Davidson AR. 1999. A simple in vivo assay for increased protein solubility. Protein Sci 8: 1908 – 11. | en_US |
dc.identifier.citedreference | Foit L, Morgan GJ, Kern MJ, Steimer LR, et al. 2009. Optimizing protein stability in vivo. Mol Cell 36: 861 – 71. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | 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. | en_US |
dc.identifier.citedreference | Sieber V, Martinez CA, Arnold FH. 2001. Libraries of hybrid proteins from distantly related sequences. Nat Biotechnol 19: 456 – 60. | en_US |
dc.identifier.citedreference | Pedelacq JD, Piltch E, Liong EC, Berendzen J, et al. 2002. Engineering soluble proteins for structural genomics. Nat Biotechnol 20: 927 – 32. | en_US |
dc.identifier.citedreference | Waldo GS. 2003. Genetic screens and directed evolution for protein solubility. Curr Opin Chem Biol 7: 33 – 8. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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