Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm

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Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm is …
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scholarly articleQ13442814

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P819ADS bibcode1999PNAS...9613703B
P356DOI10.1073/PNAS.96.24.13703
P3181OpenCitations bibliographic resource ID4726008
P932PMC publication ID24128
P698PubMed publication ID10570136
P5875ResearchGate publication ID12731376

P2093author name stringJ Beckwith
F Aslund
G Georgiou
P H Bessette
P2860cites workIn vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA)Q72102596
Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded proteinQ73425938
Disulfide bond catalysts in Escherichia coliQ74420339
The genetics of disulfide bond metabolismQ77936221
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coliQ78177288
Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterizationQ24676777
Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoterQ27860697
RsrA, an anti-sigma factor regulated by redox changeQ28504098
The thioredoxin superfamily: redundancy, specificity, and gray-area genomicsQ33537167
Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio choleraeQ33613621
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxinsQ33889552
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzymeQ33937247
A signal sequence is not required for protein export in prlA mutants of Escherichia coliQ34044995
Determinants of membrane protein topologyQ34372343
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Q34444511
Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibriaQ34743720
An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteinsQ34756523
Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulationQ35970767
Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide statusQ37199804
A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae RdQ37273291
Expression of active human tissue-type plasminogen activator in Escherichia coli.Q39479612
Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductasesQ42027032
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasmQ42271387
A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio choleraeQ42599846
Synthesis and secretion of a fibrinolytically active tissue-type plasminogen activator variant in Escherichia coliQ44466285
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.Q46203577
Why is DsbA such an oxidizing disulfide catalyst?Q48068494
Identification of a protein required for disulfide bond formation in vivoQ48201805
Production of enzymatically active rat protein disulfide isomerase in Escherichia coliQ49168113
The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.Q54563918
Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.Q54588808
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.Q54613834
Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.Q54646876
A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonucleaseQ54679075
Secretion of active kringle-2-serine protease in Escherichia coli.Q54707269
Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity.Q54773032
P433issue24
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
cytoplasmQ79899
protein foldingQ847556
P304page(s)13703-8
P577publication date1999-11-23
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleEfficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
P478volume96

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