(Q27730283)

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Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B

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Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B (English)

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solution structure

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J Qin

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author name string

G M Clore

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W M Kennedy

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J R Huth

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A M Gronenborn

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15 March 1995

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289-97

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3

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Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62

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Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-kappa B in vitro

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Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro

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Redox regulation of fos and jun DNA-binding activity in vitro

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Enzymatic reduction-oxidation of protein disulfides by thioredoxin

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Enzymatic reduction of disulfide bonds in fibrin-ogen by the thioredoxin system. I. Identification of reduced bonds and studies on reoxidation process

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Thioredoxin and glutathione in cultured fibroblasts from human cases with 5-oxoprolinuria and cystinosis

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Epstein-Barr virus-containing B-cell line produces an interleukin 1 that it uses as a growth factor

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Transcription of IL-2 receptor gene is stimulated by ATL-derived factor produced by HTLV-I(+) T cell lines.

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Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotropic virus type I- and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2

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A genetic tool used to identify thioredoxin as a mediator of a growth inhibitory signal

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HTLV-1 transactivator induces interleukin-2 receptor expression through an NF-kappa B-like factor.

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NF-kappa B: a pleiotropic mediator of inducible and tissue-specific gene control

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Structure of NF-kappa B p50 homodimer bound to a kappa B site

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Structure of the NF-kappa B p50 homodimer bound to DNA

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Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.

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The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin

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Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione

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The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.

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