|
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
PALB2, RAD51C, and BARD1 are additional tumor suppressor genes which also mediate repair of double stranded DNA breaks through the HRD pathway and are implicated in hereditary breast (PALB2; BARD1) and ovarian (RAD51C) cancer.
|
30772928 |
2019 |
|
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BARD1, a tumor suppressor, is essential for genome stability by interaction with BRCA1.
|
31258718 |
2019 |
|
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
In this paper, whole exome sequencing of over 10,000 cancer samples from 33 cancer types identified from somatic mutations and loss of heterozygosity in tumors 76 potentially cancer-associated BARD1 missense and truncation variants.
|
30925164 |
2019 |
|
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
In conclusion, we have identified two potentially causative SNPs at the BARD1 locus associated with predisposition to high-risk neuroblastoma, and have shown that full-length BARD1 may act as tumor suppressor.
|
30132831 |
2018 |
|
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
The BRCT Domains of the BRCA1 and BARD1 Tumor Suppressors Differentially Regulate Homology-Directed Repair and Stalled Fork Protection.
|
30244837 |
2018 |
|
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Similarly, circRNA_BARD1 overexpression induced by TCDD suppressed the growth and metastasis of tumor in vivo.
|
30521417 |
2018 |
|
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
During this process, BRCA1-BARD1 facilitates the nucleolytic resection of DNA ends to generate a single-stranded template for the recruitment of another tumour suppressor complex, BRCA2-PALB2, and the recombinase RAD51.
|
28976962 |
2017 |
|
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
The breast- and ovarian-cancer-specific tumor suppressor BRCA1 and its heterodimeric partner BARD1 contain RING domains that implicate them as E3 ubiquitin ligases.
|
28564596 |
2017 |
|
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
BRCA1-associated RING domain protein 1 (BARD1) is a tumor suppressor, which forms a heterodimer with BRCA1.
|
28161399 |
2017 |
|
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Emerging data suggest that BARD1 can have both tumor-suppressor gene and oncogene functions in tumor initiation and progression.
|
29292755 |
2017 |
|
Neoplasms
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Previous reports have shown that expression of BARD1δ, a deletion-bearing isoform of BARD1, correlates with tumor aggressiveness and progression.
|
28030839 |
2017 |
|
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 |
|
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |