Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli.
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[1] George Georgiou,et al. Construction and Characterization of a Set of E. coli Strains Deficient in All Known Loci Affecting the Proteolytic Stability of Secreted Recombinant Proteins , 1994, Bio/Technology.
[2] J. King,et al. Amino acid substitutions influencing intracellular protein folding pathways , 1992, FEBS letters.
[3] D. N. Collier. Expression of Escherichia coli SecB in Bacillus subtilis facilitates secretion of the SecB-dependent maltose-binding protein of E. coli , 1994, Journal of bacteriology.
[4] P. Model,et al. Role of an Escherichia coli stress-response operon in stationary-phase survival. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[5] W. Dower,et al. Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors , 1994, Journal of bacteriology.
[6] F. Blattner,et al. Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. , 1993, Gene.
[7] D. Belin,et al. A pathway for disulfide bond formation in vivo. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[8] L. Randall,et al. High selectivity with low specificity: how SecB has solved the paradox of chaperone binding. , 1995, Trends in biochemical sciences.
[9] W. A. Bridger,et al. Folding and assembly of the Escherichia coli succinyl-CoA synthetase heterotetramer without participation of molecular chaperones. , 1992, Biochemistry.
[10] F. Neidhardt,et al. Stress response of Escherichia coli to elevated hydrostatic pressure , 1993, Journal of bacteriology.
[11] A. Robins,et al. Secretion of eukaryotic growth hormones in Escherichia coli is influenced by the sequence of the mature proteins. , 1994, Gene.
[12] R. Wetzel,et al. Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1 beta point mutant modified in a surface loop. , 1993, Protein engineering.
[13] P. Blum,et al. Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli , 1992, Journal of bacteriology.
[14] M. Inouye,et al. The cold‐shock response — a hot topic , 1994, Molecular microbiology.
[15] B. Seaton,et al. A gene encoding a DnaK/hsp70 homolog in Escherichia coli. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[16] G. Fischer,et al. Peptidyl-prolyl cis/trans isomerases and their effectors , 1994 .
[17] H. Burtscher,et al. Expression of human placental alkaline phosphatase in Escherichia coli. , 1994, Protein expression and purification.
[18] B Demple,et al. Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene , 1992, Journal of bacteriology.
[19] A. Plückthun,et al. Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). , 1995, Gene.
[20] P O Olins,et al. Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli. , 1992, The Journal of biological chemistry.
[21] T. Nyström,et al. Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest , 1994, Molecular microbiology.
[22] G. Lorimer,et al. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli , 1989, Nature.
[23] J. Ghuysen,et al. Engineering and overexpression of periplasmic forms of the penicillin-binding protein 3 of Escherichia coli. , 1994, The Biochemical journal.
[24] J. Pogliano,et al. SecD and SecF facilitate protein export in Escherichia coli. , 1994, The EMBO journal.
[25] E. Söderlind,et al. Intra- and extracellular expression of an scFv antibody fragment in E. coli: effect of bacterial strains and pathway engineering using GroES/L chaperonins. , 1994, BioTechniques.
[26] A. Plückthun,et al. Correctly folded T-cell receptor fragments in the periplasm of Escherichia coli. Influence of folding catalysts. , 1994, Journal of molecular biology.
[27] Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[28] C. Walsh,et al. Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. , 1993, The Journal of biological chemistry.
[29] G. Reinhart,et al. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore , 1994, Cell.
[30] P. Blum,et al. DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies , 1992, Bio/Technology.
[31] F. Jacob-Dubuisson,et al. PapD and superfamily of periplasmic immunoglobulin-like pilus chaperones. , 1993, Advances in protein chemistry.
[32] B. Dobberstein. On the beaten pathway , 1994, Nature.
[33] Zbyszek Otwinowski,et al. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å , 1994, Nature.
[34] R. Hockney. Recent developments in heterologous protein production in Escherichia coli. , 1994, Trends in biotechnology.
[35] J. Barbero,et al. DnaK/DnaJ supplementation improves the periplasmic production of human granulocyte-colony stimulating factor in Escherichia coli. , 1995, Biochemical and biophysical research communications.
[36] D. Belin,et al. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. , 1993, Science.
[37] Y. Fujita,et al. SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. , 1993, The EMBO journal.
[38] R. Wetzel,et al. Inclusion body formation by interleukin‐1β depends on the thermal sensitivity of a folding intermediate , 1994, FEBS letters.
[39] G. Dale,et al. Increased solubility of trimethoprim-resistant type S1 DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES. , 1994, Protein engineering.
[40] R. Jaenicke,et al. Response of bacteria and fungi to high‐pressure stress as investigated by two‐dimensional polyacrylamide gel electrophoresis , 1994, Electrophoresis.
[41] G. Georgiou,et al. The folding of bovine pancreatic trypsin inhibitor in the Escherichia coli periplasm. , 1994, The Journal of biological chemistry.
[42] M. Kleerebezem,et al. Expression of the pspA gene stimulates efficient protein export in Escherichia coli , 1993, Molecular microbiology.
[43] G von Heijne,et al. Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane , 1994, FEBS letters.
[44] T. Mizuno,et al. A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli , 1995, Journal of bacteriology.
[45] E. Reinherz,et al. Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2. , 1993, Structure.
[46] W. B. Snyder,et al. Enhanced export of beta-galactosidase fusion proteins in prlF mutants is Lon dependent , 1992, Journal of bacteriology.
[47] P. Caspers,et al. Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli. , 1994, Cellular and molecular biology.
[48] T. Mizuno,et al. An analogue of the DnaJ molecular chaperone whose expression is controlled by σS during the stationary phase and phosphate starvation in Escherichia coli , 1994, Molecular microbiology.
[49] R. Glockshuber,et al. In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA). , 1993, The Journal of biological chemistry.
[50] H. Mori,et al. Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli , 1994, Journal of bacteriology.
[51] I. Holland,et al. Protein secretion pathways in Escherichia coli , 1994 .
[52] A. Plückthun,et al. The Effect of Folding Catalysts on the In Vivo Folding Process of Different Antibody Fragments Expressed in Escherichia coli , 1993, Bio/Technology.
[53] H. Gilbert. Protein chaperones and protein folding. , 1994, Current opinion in biotechnology.
[54] A. Plückthun,et al. Engineered turns of a recombinant antibody improve its in vivo folding. , 1995, Protein engineering.
[55] J. Gierse,et al. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli , 1992, Journal of bacteriology.
[56] J E Bailey,et al. Co‐overexpression of prlF Increases Cell Viability and Enzyme Yields in Recombinant Escherichia coli Expressing Bacillus stearothermophilus α‐Amylase , 1995, Biotechnology progress.
[57] A. Plückthun,et al. Protein folding in the periplasm of Escherichia coli , 1994, Molecular microbiology.
[58] J. Barbero,et al. Increasing the Efficiency of Protein Export in Escherichia coli , 1994, Bio/Technology.
[59] F. Hartl,et al. Molecular chaperones in cellular protein folding. , 1994, Nature.
[60] D. Y. Thomas,et al. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. , 1994, Trends in biochemical sciences.
[61] C. Georgopoulos,et al. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. , 1994, The EMBO journal.
[62] H. Crooke,et al. The biogenesis of c‐type cytochromes in Escherichia coli requires a membrane‐bound protein, DipZ, with a protein disulphide isomerase‐like domain , 1995, Molecular microbiology.
[63] D. Kern,et al. Reassessment of the putative chaperone function of prolyl‐cis/trans‐isomerases , 1994, FEBS letters.
[64] Phage Tailspike Protein: A fishy tale of protein folding , 1994, Current Biology.
[65] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.
[66] L. Alksne,et al. A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli , 1995, Journal of bacteriology.
[67] J. King,et al. Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. , 1993, The Journal of biological chemistry.
[68] R. Schekman. Translocation gets a push , 1994, Cell.
[69] W. Wickner,et al. SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation. , 1994, The EMBO journal.
[70] G. Dale,et al. Improving protein solubility through rationally designed amino acid replacements: solubilization of the trimethoprim-resistant type S1 dihydrofolate reductase. , 1994, Protein engineering.
[71] J. Bardwell,et al. Building bridges: disulphide bond formation in the cell , 1994, Molecular microbiology.
[72] T. Silhavy,et al. Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli , 1990, Nature.