Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The BARD1/BRCA1 interaction is disrupted by BRCA1 missense mutations that segregate with breast cancer susceptibility, indicating that BARD1 may be involved in mediating tumour suppression by BRCA1.
|
8944023 |
1996 |
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Somatically acquired missense mutations were observed in one breast carcinoma and one endometrial tumor; in at least one of these cases, tumor formation was accompanied by loss of the wild-type BARD1 allele, following the paradigm for known tumor suppressor genes.
|
9425226 |
1998 |
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
A tumor-associated mutation Q564H of BARD1 is defective in apoptosis induction, thus suggesting a role of BARD1 in tumor suppression by mediating the signaling from proapoptotic stress toward induction of apoptosis.
|
11779501 |
2001 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
We report that EWS and EWS-FLI1 interact via their common NH2 terminus with the COOH terminus of BARD1, a putative tumor suppressor, in vitro and in vivo.
|
12183411 |
2002 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The BRCA1 tumor suppressor and the BARD1 protein form a stable heterodimeric complex that can catalyze the formation of polyubiquitin chains.
|
15166217 |
2004 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
TIEG in combination with Bard1 discriminated between N-/bad outcome from N-/good tumors with a sensitivity and specificity of 83 and 82%, respectively.
|
15218362 |
2004 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The BARD1 gene is mutated in a subset of breast and ovarian cancers, implicating BARD1 as a potential tumor suppressor.
|
15632137 |
2005 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
One particular protein, BARD1, seems to be an important regulator of the tumour-suppressor function of BRCA1, as well as acting as a tumour suppressor itself.
|
16633366 |
2006 |
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
In breast cancer, BARD1 expression was correlated with poor differentiation and large tumor size, established factors of poor prognosis, as well as short disease-free survival.
|
16152612 |
2006 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1 (BRCA1-associated RING-domain 1) is a tumor suppressor whose protein product interacts with BRCA1, and in which rare somatic and germline mutations have been reported in breast, uterine, and endometrial cancers.
|
16333312 |
2006 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1 and BRCA1 form a stable heterodimer and dimerization, which is required for most tumor suppressor functions attributed to BRCA1.
|
17556008 |
2007 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1 is required for protein stability and tumor suppressor functions of BRCA1, which depend on the ubiquitin ligase activity of the BRCA1-BARD1 heterodimer.
|
18089818 |
2007 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The BRCA1 tumor suppressor exists as a heterodimeric complex with BARD1, and this complex is thought to mediate many of the functions ascribed to BRCA1, including its role in tumor suppression.
|
17848578 |
2007 |
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Characterization of the relative expression of BARD1 FL, BARD1delta, and BARD1 DeltaRIN using quantitative PCR analysis indicated that the mean expression levels of BARD1 FL, BARD1delta, and BARD1 DeltaRIN were significantly higher in tumors than in morphologically normal tissues and lymphocytes.
|
17497650 |
2007 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1 plays a crucial role in tumor repression, along with its heterodimeric partner BRCA1.
|
17028982 |
2007 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
We aimed to use split-GFP reassembly to examine the determinants of association for a heterodimeric four-helix bundle, and we chose the N-terminal RING domains of BARD1 and the tumor suppressor BRCA1 as our test system.
|
18493658 |
2008 |
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Gene expression analysis using DNA microarrays classified the tumor as basal-like, with very low BARD1 and ID4 expression, but high expression of BRCA1, RAD51, PARP1, CHEK1, and FANCA.
|
20842729 |
2010 |
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Consistent with its role as tumor suppressor, we further find that the expression of the full-length BARD1 protein predicts outcome in colon cancer and that loss of full-length BARD1 protein is associated with a poor prognosis (P = 0.0002).
|
21693656 |
2011 |
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Furthermore, the pattern of BARD1 isoform expression was similar in tumor and morphologically normal peri-tumor tissues, and only one novel isoform π was specifically upregulated in tumors.
|
21815143 |
2012 |
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Over the past years BARD1 (BRCA1-associated RING domain 1) has been considered as both a BRCA1 (BReast Cancer susceptibility gene 1, early onset) interactor and tumor suppressor gene mutated in breast and ovarian cancers.
|
24349422 |
2013 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
The breast and ovarian cancer-specific tumor suppressor BRCA1, along with its heterodimer partner BRCA1-associated RING domain protein (BARD1), plays important roles in DNA repair, centrosome regulation, and transcription.
|
24289923 |
2014 |
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
We found BRCA1 localized in the cytoplasm with BARD1 in 51.4 % of tumors.
|
26395808 |
2015 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BRCA1 mRNA and protein in situ expression, as well as the amount of BRCA1 ligated to BARD1 in the tumor, lacked any associations with patient outcomes, likely due to high intratumoral heterogeneity, and thus could not be used for clinical purposes.
|
26490435 |
2015 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1 is a breast cancer tumor suppressor with multiple domains and functions.
|
26022179 |
2015 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1 (BRCA1 associated RING domain protein 1), as an important animal tumor suppressor gene associated with many kinds of cancers, has been intensively studied for decades.
|
27502904 |
2016 |