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anti-Human BARD1 Antibodies:
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Human Polyclonal BARD1 Primary Antibody for IP, PLA - ABIN151785
Hu, Ghosh, Amleh, Yue, Lu, Katz, Li: Modulation of aromatase expression by BRCA1: a possible link to tissue-specific tumor suppression. in Oncogene 2005
Show all 13 Pubmed References
Human Polyclonal BARD1 Primary Antibody for IF (p), IHC (p) - ABIN706496
Liu, Ao, Jia, Bai, Xu, Hu, Jiang, Chen, Wu: FOXK2 transcription factor suppresses ER?-positive breast cancer cell growth through down-regulating the stability of ER? via mechanism involving BRCA1/BARD1. in Scientific reports 2015
identification of genetic variants of BRCA1-BARD1 in patients with cancer that exhibit poor protection of nascent strands but retain homologous recombination proficiency, thus defining domains of BRCA1-BARD1 that are required for fork protection and associated with cancer development
these data reveal that the OLA1-BARD1 interaction is important for the regulation of centrosome number. Regulation of centrosome number by BRCA1/BARD1 together with OLA1 is important for the genome integrity to prevent tumor development.
Data indicate that breast cancer 1 protein (BRCA1)-BRCA1 associated RING domain 1 (BARD1) monitors the replicative state of the genome.
Study reports that USP15 affects cancer cell response to PARP inhibitors by regulating homologous recombination repair. USP15 is recruited to DNA double-strand breaks (DSBs) by MDC1. USP15 deubiquitinates BARD1 BRCT domain, and promotes BARD1-HP1gamma interaction, resulting in BRCA1/BARD1 retention at DSBs. Cancer-associated USP15 mutations, with decreased USP15-BARD1 interaction, increases PARP inhibitor sensitivity.
Authors provide evidence of the roles of the polyadenylation factor cleavage stimulation factor 50 (CstF-50) and the ubiquitin (Ub) escort factor p97 as cofactors of BRCA1/BARD1 E3 Ub ligase, facilitating chromatin remodeling during the DNA damage response (DDR).
BARD1 was significantly up-regulated in HCC tumor tissues and that BARD1 up-regulation was significantly associated with a lower HCC patient survival rate and advanced stage.
In human neuroblastoma cells, attenuating full-length BARD1 increased proliferation and invasion capacity.
Study shows that tamoxifen-resistant breast cancer cells are resistant to DNA-damaging chemo- and radiotherapy because of upregulated BARD1 and BRCA1, which is caused by activated PI3K/AKT pathway.
The results reveal new information for the manner in which full-length BRCA1 engages its binding partner, BARD1, under oxidative stress conditions.
BARD1 RING domain is critical to BRCA1/BARD1 binding to nucleosomes and hence to ubiquitylation of histone H2A and also critical to transcriptional repression of BRCA1-regulated genes active in estrogen metabolism.
BARD1delta binds more efficiently than BARD1 to telomere binding proteins and causes their depletion from telomeres, leading to telomere and chromosomal instability and tumor cell cycle arrest.
BRCA1-BARD1 mutants with weakened RAD51 interactions show compromised DNA joint formation and impaired mediation of homologous recombination and DNA repair in cells; results identify a late role of BRCA1-BARD1 in homologous recombination, an attribute of the tumour suppressor complex that could be targeted in cancer therapy
variants in BARD1 were associated with moderate risks of breast cancer.
NPM1 downregulation by P-STAT5 is mediated by impairing the BRCA1-BARD1 ubiquitin ligase, which controls the stability of NPM1. In turn, decreased NPM1 levels led to suppression of p53 expression, resulting in enhanced cell survival.
In MCF-7 cells BARD1 variants do vary considerably their cellular distribution and in their ability to influence apoptotic response to cisplatin.
substitutions that create a structurally intact BRCA1/BARD1 heterodimer that is inactive in vitro with all E2 enzymes. Other substitutions in BRCA1 or BARD1 RING domains result in hyperactivity, revealing that both proteins have evolved attenuated activity. Loss of attenuation results in decreased product specificity, providing a rationale for why nature has tuned BRCA1 activity.
Findings suggest that the study of AtROW1 in plant may provide a model for elucidating the functional mechanism of BARD1 in mammals.
BRCA1-BARD1 ligase activity and subsequent SMARCAD1-dependent chromatin remodeling are critical regulators of DNA repair in cancer cells.
Results suggest that BRCA1-associated RING domain protein 1 (BARD1) rs7585356 G>A polymorphism may be associated with nephroblastoma risk.
BARD1 rs6435862 T>G and rs3768716 A>G single nucleotide polymorphisms contribute to increased susceptibility to neuroblastoma, especially for children at age >/=12 months in a Southern Chinese population.
Bard1(S563F/S563F) and Bard1(K607A/K607A) mice, unlike Brca1(S1598F/S1598F) mice, are not tumor prone, indicating that homology-directed repair alone is sufficient to suppress tumor formation in the absence of stalled fork protection
Suggest BARD1 as a driver of proliferation and of pulmonary fibrosis pathogenesis.
identification of BARD1 as mediator between proapoptotic stress and p53-dependent apoptosis
the developmental functions of Brca1 and Bard1 are mediated by the Brca1/Bard1 heterodimer.
Data show that expression of truncated mouse or human BARD1 peptides capable of interacting with Brca1 results in a homologous-repair deficiency.
the ankyrin and BRCT motifs of BARD1 are each essential for both chromosome stability and homology-directed DNA repair.
The remarkable similarities between the mammary carcinomas of Bard1-, Brca1-, and Bard1/Brca1-mutant mice indicate that the tumor suppressor activities of both genes are mediated through the BRCA1/BARD1 heterodimer.
This gene encodes a protein which interacts with the N-terminal region of BRCA1. In addition to its ability to bind BRCA1 in vivo and in vitro, it shares homology with the 2 most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes. This protein also contains 3 tandem ankyrin repeats. The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. This protein may be the target of oncogenic mutations in breast or ovarian cancer.
BRCA1 associated RING domain 1
, BRCA1-associated RING domain protein 1-like
, BRCA1 associated RING domain 1 isoform alfa
, BRCA1 associated RING domain 1 isoform beta
, BRCA1 associated RING domain 1 isoform delta
, BRCA1 associated RING domain 1 isoform epsilon
, BRCA1 associated RING domain 1 isoform eta
, BRCA1 associated RING domain 1 isoform gamma
, BRCA1 associated RING domain 1 isoform phi
, BRCA1-associated RING domain gene 1
, BRCA1-associated RING domain protein 1