Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein

scientific article

Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1093/EMBOJ/20.21.5853
P3181OpenCitations bibliographic resource ID1975681
P932PMC publication ID125700
P698PubMed publication ID11689426
P5875ResearchGate publication ID11664687

P50authorAnette HenriksenQ58834162
P2093author name stringF G Hansen
J R Winther
H Ostergaard
P2860cites workCircularly permuted variants of the green fluorescent proteinQ21045402
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Structural basis of spectral shifts in the yellow-emission variants of green fluorescent proteinQ27765711
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Electron avenue: pathways of disulfide bond formation and isomerizationQ33760255
Chaperone activity with a redox switchQ33852523
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxinsQ33889552
2 Thiol/disulfide exchange equilibria and disulfidebond stabilityQ34303407
Molecular and cellular aspects of thiol-disulfide exchange.Q34373608
Activation of the OxyR transcription factor by reversible disulfide bond formationQ34459806
An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteinsQ34756523
Chemical nature of the light emitter of the Aequorea green fluorescent proteinQ35920120
Wavelength mutations and posttranslational autoxidation of green fluorescent proteinQ35987741
Glutathione reductase is not required for maintenance of reduced glutathione in Escherichia coli K-12.Q36359033
pH homeostasis in Escherichia coli: measurement by 31P nuclear magnetic resonance of methylphosphonate and phosphate.Q36374847
Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transferQ37402383
A Bacterial Thioredoxin-like Protein That Is Exposed to the Periplasm Has Redox Properties Comparable with Those of Cytoplasmic ThioredoxinsQ38289494
Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coliQ38344053
Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)—a reexaminationQ39261126
The Glutathione Status of CellsQ39293102
Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structureQ41230313
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
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coliQ42843291
Direct measurement of the equilibrium between glutathione and dithiothreitol by high performance liquid chromatographyQ43531471
Evidence for redox forms of the Aequorea green fluorescent proteinQ46826000
Chromophore formation in green fluorescent proteinQ47853021
Identification of a protein required for disulfide bond formation in vivoQ48201805
An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs.Q52340732
A versatile plasmid vector system for the regulated expression of genes in Escherichia coli.Q53017400
The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.Q54563918
Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.Q54646876
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P433issue21
P407language of work or nameEnglishQ1860
P304page(s)5853-5862
P577publication date2001-11-01
P1433published inThe EMBO JournalQ1278554
P1476titleShedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein
P478volume20

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