scholarly article | Q13442814 |
P2093 | author name string | J Beckwith | |
F Aslund | |||
G Georgiou | |||
P H Bessette | |||
P2860 | cites work | In 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 protein | Q73425938 | ||
Disulfide bond catalysts in Escherichia coli | Q74420339 | ||
The genetics of disulfide bond metabolism | Q77936221 | ||
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli | Q78177288 | ||
Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization | Q24676777 | ||
Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter | Q27860697 | ||
RsrA, an anti-sigma factor regulated by redox change | Q28504098 | ||
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics | Q33537167 | ||
Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae | Q33613621 | ||
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins | Q33889552 | ||
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme | Q33937247 | ||
A signal sequence is not required for protein export in prlA mutants of Escherichia coli | Q34044995 | ||
Determinants of membrane protein topology | Q34372343 | ||
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 equilibria | Q34743720 | ||
An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins | Q34756523 | ||
Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation | Q35970767 | ||
Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status | Q37199804 | ||
A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd | Q37273291 | ||
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 oxidoreductases | Q42027032 | ||
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm | Q42271387 | ||
A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae | Q42599846 | ||
Synthesis and secretion of a fibrinolytically active tissue-type plasminogen activator variant in Escherichia coli | Q44466285 | ||
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 vivo | Q48201805 | ||
Production of enzymatically active rat protein disulfide isomerase in Escherichia coli | Q49168113 | ||
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 ribonuclease | Q54679075 | ||
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 | ||
P433 | issue | 24 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
cytoplasm | Q79899 | ||
protein folding | Q847556 | ||
P304 | page(s) | 13703-8 | |
P577 | publication date | 1999-11-23 | |
P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
P1476 | title | Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm | |
P478 | volume | 96 |
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