Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins

scientific article published in September 2001

Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/AEM.67.9.3994-4000.2001
P932PMC publication ID93120
P698PubMed publication ID11525996
P5875ResearchGate publication ID11819928

P2093author name stringWinter J
Rudolph R
Schwarz E
Schäffner J
P2860cites workEfficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasmQ24644906
The Hsp70 and Hsp60 chaperone machinesQ29547601
The effect of molecular chaperones on in vivo and in vitro folding processesQ30425820
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.Q33885969
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxinsQ33889552
Secretion cloning vectors in Escherichia coliQ33940005
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingQ34242618
Protein folding in the bacterial periplasmQ35621918
Cellular location affects protein stability in Escherichia coliQ36287012
Expression of active human tissue-type plasminogen activator in Escherichia coli.Q39479612
Leaderless polypeptides efficiently extracted from whole cells by osmotic shockQ39846925
Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphataseQ40054982
Building bridges: disulphide bond formation in the cellQ40576198
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.Q40874220
In vitro folding of inclusion body proteins.Q40949126
Small heat shock proteins are molecular chaperones.Q42812560
High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene productQ43689663
Selection for signal sequence mutations that enhance production of secreted human proinsulin by Escherichia coliQ43890901
Molecular cloning, sequencing and expression in Escherichia coli of the 25-kDa growth-related protein of Ehrlich ascites tumor and its homology to mammalian stress proteinsQ44454104
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.Q46203577
The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.Q46522433
High-level production and long-term storage of engineered antibodies in transgenic tobacco seedsQ47787657
Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.Q52524766
Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties.Q54559625
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.Q54613834
Biochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022Q54686711
Purification and properties of the dnaJ replication protein of Escherichia coliQ69892745
Molecular basis of fibrinolysis, as relevant for thrombolytic therapyQ70943347
A simple, sensitive spectrophotometric assay for extrinsic (tissue-type) plasminogen activator applicable to measurements in plasmaQ71845661
In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA)Q72102596
Effect of modification of connecting peptide of proinsulin on its exportQ72273946
Inhibition of aggregation side reactions during in vitro protein foldingQ73043260
In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbGQ74602402
Advances in refolding of proteins produced in E. coliQ77576594
The genetics of disulfide bond metabolismQ77936221
P433issue9
P407language of work or nameEnglishQ1860
P921main subjectmolecular chaperonesQ422496
P304page(s)3994-4000
P577publication date2001-09-01
P1433published inApplied and Environmental MicrobiologyQ4781593
P1476titleCosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins
P478volume67

Reverse relations

cites work (P2860)
Q40409120Ability of Lactococcus lactis to export viral capsid antigens: a crucial step for development of live vaccines
Q28080871Cellular disulfide bond formation in bioactive peptides and proteins
Q41844834Effect of culture medium, host strain and oxygen transfer on recombinant Fab antibody fragment yield and leakage to medium in shaken E. coli cultures.
Q33690400Expression of active recombinant human tissue-type plasminogen activator by using in vivo polyhydroxybutyrate granule display
Q42048325Optimal conditions for the expression of a single-chain antibody (scFv) gene in Pichia pastoris
Q39120553Optimizing antibody expression: The nuts and bolts
Q92702314QbD Based Media Development for the Production of Fab Fragments in E. coli
Q33893399Reducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli
Q30377057Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.
Q24792799Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins
Q37256734Structural and Functional Characterization of Recombinant Interleukin-10 from Indian Major Carp Labeo rohita.
Q40833107Studies of single-chain antibody expression in quiescent Escherichia coli
Q44525552The N-terminal stem region of bovine and human beta1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies
Q40718297Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli
Q37097393Use of folding modulators to improve heterologous protein production in Escherichia coli.

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