| Identifier | HPI031734 |
| Interaction | HBx <==> p53 |
| Role & State | RS:0000080,suppressor; RS:0000068,activator; RS:0000074,inhibitor; RS:0000002,activity; |
| Interaction Type | IT:0000198,modify; IT:0000026,interact; IT:0000114,activation; IT:0000068,transcription; IT:0000274,interfere; IT:0000295,affect; IT:0000076,inhibition; IT:0000176,suppress; IT:0000290,form; IT:0000271,express; IT:0000080,effect; IT:0000099,formation; IT:0000078,regulation; IT:0000294,stimulate; IT:0000174,repress; IT:0000059,binding; IT:0000075,transduction; IT:0000227,bind; |
| Biological Process | BP:0031497,chromatin assembly; BP:0006915,apoptosis; BP:0051301,cell division; BP:0051235,sequestering; BP:0051726,tumor suppression; BP:0016446,mutation; BP:0006281,DNA repair; BP:0032502,development; BP:0007165,signal transduction; |
| Biological Function | BF:0002039,p53 binding; |
| Subcelluar Location | SCL:0000785,chromatin; SCL:0000006,cytoplasm; |
| Detection Method | --- |
| Reference | 10074921_11, Thus, our data indicate that HBx may interfere with the NER pathway through both p53-dependent and p53-independent mechanisms.
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| Reference | 10842185_4, In this study, we have examined the ability of HBx to modify p53 regulation of the HCC tumor marker gene, alpha-fetoprotein (AFP).
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| Reference | 10842185_5, By utilizing in vitro chromatin assembly of DNA templates prior to transcription analysis, we have demonstrated that HBx functionally disrupts p53-mediated repression of AFP transcription through protein-protein interaction.
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| Reference | 11278765_3, Herein we report that HBx represses two components of the transcription-repair factor TFIIH, XPB (p89), and XPD (p80), both in p53-proficient and p53-deficient liver cells.
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| Reference | 11325602_2, The X protein of hepatitis B virus (HBx) is a multifunctional protein that can interact with p53 but can also influence a variety of signal transduction pathways within the cell.
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| Reference | 11821950_2, Using a transgenic mouse model, we have recently shown that HBx stimulates the apoptotic turnover of hepatocytes, independently of p53.
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| Reference | 12839924_11, This constitutes the first report to demonstrate that HBx has an effect on the p53-mediated transcription of PTEN, which, in turn, is associated with tumor suppression.
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| Reference | 15450428_1, The hepatitis B virus X protein (HBx) is implicated in liver cancer development, and this presumably involves its ability to bind and functionally inactivate the p53 tumour suppressor.
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| Reference | 15450428_10, The data demonstrate that HBx expression can reduce the efficiency of TCNER in addition to GNER in human cells via p53-independent as well as p53-dependent pathways.
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| Reference | 16055925_7, The binding of HBx to p53 modulated (but did not inhibit) the transcriptional activation function of p53.
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| Reference | 16953033_7, In that process, HBx will suppress p53 function, which will lead to ineffective liver cell division and resulting in HCC.
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| Reference | 18601905_6, The abrogation of apoptosis is completely reversed by specific COX-2 inhibition, suggesting that HBx blocks p53-induced apoptosis via activation of COX-2/PGE(2) pathway.
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| Reference | 8521383_3, We and others have recently demonstrated that the hepatitis B virus oncoprotein, HBx, can form a complex with p53 and inhibit its DNA consensus sequence binding and transcriptional transactivator activity.
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| Reference | 8521383_7, Alternatively, HBx could affect p53 binding to the TFIIH transcription-nucleotide excision repair complex as HBx binds to the COOH terminus of p53 and inhibits its binding to XPB or XPD.
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| Reference | 8871869_8, Further, HBx may enhance HBV related carcinogenesis by inactivation of the tumour suppressor gene product p53.
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| Reference | 8903370_13, These data show that HBx has a weak tumorigenicity in murine hepatocytes and that the addition of mutation of p53 at codon 249 to HBx expression does not increase tumorigenicity in AML12 cells.
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| Reference | 8903370_5, Because mutations of the p53 gene, in particular at codon 249, have been implicated in HCC development in geographical areas with high incidence of the tumor, we also studied the putative cooperative role in transformation between HBx and mutated p53 by cotransfecting HBx with a murine p53 mutant equivalent to human ser249 (ser246p53).
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| Reference | 8903370_7, The toxic effect of HBx on colony formation was abolished by cotransfection with 246p53, suggesting that the inhibitory effect requires functionally intact p53.
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| Reference | 9405677_4, Using a microinjection technique, we show that this same C-terminal region of HBx is necessary for sequestering p53 in the cytoplasm and abrogating p53-mediated apoptosis.
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| Reference | 9837906_6, We demonstrate that HBx expression affects DNA repair in a p53-dependent manner.
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