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TP53 — TXN

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: TXN — TP53 Seemann et al., Oncogene 2005*
• IRef Bind_translation Interaction: TXN — TP53 (coimmunoprecipitation) Seemann et al., Oncogene 2005*
• IRef Biogrid Interaction: TP53 — TXN (direct interaction, pull down) Stoner et al., Biochemistry 2009*
• IRef Intact Interaction: Complex of 88 proteins (association, tandem affinity purification) Agrawal et al., Cell cycle (Georgetown, Tex.) 2010

Text-mined interactions from Literome

Ueno et al., J Biol Chem 1999 (Colonic Neoplasms) : Here, we have investigated the role of TRX in the regulation of p53 activity ... Electrophoretic mobility shift assay showed that TRX augmented the DNA binding activity of p53 and also further potentiated Ref-1 enhanced p53 activity ... The p53 dependent p21 transactivation induced by CDDP was inhibited by mTRX overexpression, suggesting that TRX dependent redox regulation is physiologically involved in p53 regulation ... Hence, TRX dependent redox regulation of p53 activity indicates coupling of the oxidative stress response and p53 dependent repair mechanism
Matsutani et al., Clin Cancer Res 2001 (Breast Neoplasms) : We reported previously that thioredoxin (TRX) regulates the DNA binding activities of ER and p53 in vitro
Chowdhury et al., J Gen Virol 2003 : Both HTLV-I Tax and the proteasome-specific inhibitor MG132 inhibited p53 mediated TRX protein degradation
Seemann et al., Oncogene 2005 (Breast Neoplasms) : In yeasts deficient for thioredoxin (Trx) reductase ( TRR ), p53 accumulates in an inactive, oxidized form, suggesting a role for TRR-Trx in controlling p53
Ravi et al., J Biol Chem 2005 : Additionally Trx increased p53-DNA binding and expression in response to anthracyclines
Hadj Amor et al., FEMS Yeast Res 2008 : Using differential display and Northern blot analysis, we demonstrated that human wt p53 expression in yeast leads to gene repression of thioredoxin ( TRX1/2 ), a highly conserved multifunctional antioxidative and antiapoptotic protein family
Stoner et al., Biochemistry 2009 : To investigate the role of thioredoxin in controlling p53 activity, the level of reporter gene transactivation by p53 was determined in yeast lacking the TRX1 and TRX2 genes encoding cytosolic thioredoxin ... Subsequent analyses showed that thioredoxin deletion suppressed the inhibitory effect of thioredoxin reductase deletion, suggesting that accumulation of oxidized thioredoxin in mutant yeast was necessary for p53 inhibition