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- W2018335923 abstract "Thioredoxin, a ubiquitous and evolutionarily conserved protein, modulates the structure and activity of proteins involved in a spectrum of processes, such as gene expression, apoptosis, and the oxidative stress response. Here, we present a comprehensive analysis of the thioredoxin-linked Escherichia coli proteome by using tandem affinity purification and nanospray microcapillary tandem mass spectrometry. We have identified a total of 80 proteins associated with thioredoxin, implicating the involvement of thioredoxin in at least 26 distinct cellular processes that include transcription regulation, cell division, energy transduction, and several biosynthetic pathways. We also found a number of proteins associated with thioredoxin that either participate directly (SodA, HPI, and AhpC) or have key regulatory functions (Fur and AcnB) in the detoxification of the cell. Transcription factors NusG, OmpR, and RcsB, not considered to be under redox control, are also associated with thioredoxin." @default.
- W2018335923 created "2016-06-24" @default.
- W2018335923 creator A5035609517 @default.
- W2018335923 creator A5043016878 @default.
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- W2018335923 date "2004-03-02" @default.
- W2018335923 modified "2023-10-16" @default.
- W2018335923 title "Proteomic analysis of thioredoxin-targeted proteins in <i>Escherichia coli</i>" @default.
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- W2018335923 doi "https://doi.org/10.1073/pnas.0308701101" @default.
- W2018335923 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/374317" @default.
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