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Gene Information

Gene symbol: BARD1

Gene name: BRCA1 associated RING domain 1

HGNC ID: 952

Related Genes

# Gene Symbol Number of hits
1 BRCA1 1 hits
2 BRCA2 1 hits
3 MYC 1 hits
4 NR1I2 1 hits
5 PCNA 1 hits
6 RAD18 1 hits
7 RAD51 1 hits
8 RBBP8 1 hits
9 TAC1 1 hits
10 TP53 1 hits

Related Sentences

# PMID Sentence
1 8944023 This BRCA1-associated RING domain (BARD1) protein contains an N-terminal RING motif, three tandem ankyrin repeats, and a C-terminal sequence with significant homology to the phylogenetically conserved BRCT domains that lie near the C terminus of BRCA1.
2 8944023 This BRCA1-associated RING domain (BARD1) protein contains an N-terminal RING motif, three tandem ankyrin repeats, and a C-terminal sequence with significant homology to the phylogenetically conserved BRCT domains that lie near the C terminus of BRCA1.
3 8944023 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.
4 8944023 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.
5 9267023 BARD1 and Rad51, two proteins associated with the BRCA1 dots, behaved similarly.
6 9267023 BARD1 and Rad51, two proteins associated with the BRCA1 dots, behaved similarly.
7 9267023 The S phase BRCA1 phosphorylation response to DNA damage occurred in cells lacking, respectively, two DNA damage-sensing protein kinases, DNA-PK and Atm, implying that neither plays a prime role in this process.
8 9267023 The S phase BRCA1 phosphorylation response to DNA damage occurred in cells lacking, respectively, two DNA damage-sensing protein kinases, DNA-PK and Atm, implying that neither plays a prime role in this process.
9 9267023 Finally, after BRCA1 dot dispersal, BRCA1, BARD1, and Rad51 accumulated, focally, on PCNA+ replication structures, implying an interaction of BRCA1/BARD1/Rad51 containing complexes with damaged, replicating DNA.
10 9267023 Finally, after BRCA1 dot dispersal, BRCA1, BARD1, and Rad51 accumulated, focally, on PCNA+ replication structures, implying an interaction of BRCA1/BARD1/Rad51 containing complexes with damaged, replicating DNA.
11 9425226 Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers.
12 9425226 Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers.
13 9425226 Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers.
14 9425226 The protein encoded by BRCA1 interacts in vivo with the BRCA1-associated RING domain (BARD1) protein.
15 9425226 The protein encoded by BRCA1 interacts in vivo with the BRCA1-associated RING domain (BARD1) protein.
16 9425226 The protein encoded by BRCA1 interacts in vivo with the BRCA1-associated RING domain (BARD1) protein.
17 9425226 Accordingly, BARD1 is likely to be a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers.
18 9425226 Accordingly, BARD1 is likely to be a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers.
19 9425226 Accordingly, BARD1 is likely to be a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers.
20 9645467 In Saccharomyces cerevisiae PRR is controlled by the RAD61RAD18 pathway which involves POL30 gene encoding proliferating cell nuclear antigen (PCNA), and in human cells PCNA is known to be closely associated with the newly replicated chromatin where PRR probably takes place.
21 9645467 In Saccharomyces cerevisiae PRR is controlled by the RAD61RAD18 pathway which involves POL30 gene encoding proliferating cell nuclear antigen (PCNA), and in human cells PCNA is known to be closely associated with the newly replicated chromatin where PRR probably takes place.
22 9645467 In Saccharomyces cerevisiae PRR is controlled by the RAD61RAD18 pathway which involves POL30 gene encoding proliferating cell nuclear antigen (PCNA), and in human cells PCNA is known to be closely associated with the newly replicated chromatin where PRR probably takes place.
23 9645467 In Saccharomyces cerevisiae PRR is controlled by the RAD61RAD18 pathway which involves POL30 gene encoding proliferating cell nuclear antigen (PCNA), and in human cells PCNA is known to be closely associated with the newly replicated chromatin where PRR probably takes place.
24 9645467 In UV-irradiated human cells distinct PCNA foci may be detected in some cells which accumulate phosphorylated breast cancer susceptibility protein BRCA1 and another protein BARD1.
25 9645467 In UV-irradiated human cells distinct PCNA foci may be detected in some cells which accumulate phosphorylated breast cancer susceptibility protein BRCA1 and another protein BARD1.
26 9645467 In UV-irradiated human cells distinct PCNA foci may be detected in some cells which accumulate phosphorylated breast cancer susceptibility protein BRCA1 and another protein BARD1.
27 9645467 In UV-irradiated human cells distinct PCNA foci may be detected in some cells which accumulate phosphorylated breast cancer susceptibility protein BRCA1 and another protein BARD1.
28 9645467 In this study we found that the known inhibitor of protein kinases staurosporine supresses PRR in NER-deficient cells which is consistent with the view that BRCA1 and PCNA are required for PRR.
29 9645467 In this study we found that the known inhibitor of protein kinases staurosporine supresses PRR in NER-deficient cells which is consistent with the view that BRCA1 and PCNA are required for PRR.
30 9645467 In this study we found that the known inhibitor of protein kinases staurosporine supresses PRR in NER-deficient cells which is consistent with the view that BRCA1 and PCNA are required for PRR.
31 9645467 In this study we found that the known inhibitor of protein kinases staurosporine supresses PRR in NER-deficient cells which is consistent with the view that BRCA1 and PCNA are required for PRR.
32 9645467 Since RAD18 protein is not essential for normal DNA replication and directly controls PRR in yeast, we analysed whether this protein as well as its human homologs (HR18A and HR18B) have common domains with BRCA1 and BARD1.
33 9645467 Since RAD18 protein is not essential for normal DNA replication and directly controls PRR in yeast, we analysed whether this protein as well as its human homologs (HR18A and HR18B) have common domains with BRCA1 and BARD1.
34 9645467 Since RAD18 protein is not essential for normal DNA replication and directly controls PRR in yeast, we analysed whether this protein as well as its human homologs (HR18A and HR18B) have common domains with BRCA1 and BARD1.
35 9645467 Since RAD18 protein is not essential for normal DNA replication and directly controls PRR in yeast, we analysed whether this protein as well as its human homologs (HR18A and HR18B) have common domains with BRCA1 and BARD1.
36 9645467 It is found that HR18A has a subregion of homology to BARD1 and HR18A-to BRCA1.
37 9645467 It is found that HR18A has a subregion of homology to BARD1 and HR18A-to BRCA1.
38 9645467 It is found that HR18A has a subregion of homology to BARD1 and HR18A-to BRCA1.
39 9645467 It is found that HR18A has a subregion of homology to BARD1 and HR18A-to BRCA1.
40 9645467 Taken together the results indicate that BRCA1 and BARD1 may be involved in PRR in human cells.
41 9645467 Taken together the results indicate that BRCA1 and BARD1 may be involved in PRR in human cells.
42 9645467 Taken together the results indicate that BRCA1 and BARD1 may be involved in PRR in human cells.
43 9645467 Taken together the results indicate that BRCA1 and BARD1 may be involved in PRR in human cells.
44 9798686 Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
45 9798686 Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
46 9798686 Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
47 9798686 Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
48 9798686 Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
49 9798686 Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
50 9798686 During S phase of the cell cycle, BRCA1 polypeptides are found in discrete nuclear bodies ('BRCA1 nuclear dots') together with HsRad51, a human homolog of the E. coli recA protein, and BARD1, a protein that interacts with BRCA1 to form a stable heterodimer.
51 9798686 During S phase of the cell cycle, BRCA1 polypeptides are found in discrete nuclear bodies ('BRCA1 nuclear dots') together with HsRad51, a human homolog of the E. coli recA protein, and BARD1, a protein that interacts with BRCA1 to form a stable heterodimer.
52 9798686 During S phase of the cell cycle, BRCA1 polypeptides are found in discrete nuclear bodies ('BRCA1 nuclear dots') together with HsRad51, a human homolog of the E. coli recA protein, and BARD1, a protein that interacts with BRCA1 to form a stable heterodimer.
53 9798686 During S phase of the cell cycle, BRCA1 polypeptides are found in discrete nuclear bodies ('BRCA1 nuclear dots') together with HsRad51, a human homolog of the E. coli recA protein, and BARD1, a protein that interacts with BRCA1 to form a stable heterodimer.
54 9798686 During S phase of the cell cycle, BRCA1 polypeptides are found in discrete nuclear bodies ('BRCA1 nuclear dots') together with HsRad51, a human homolog of the E. coli recA protein, and BARD1, a protein that interacts with BRCA1 to form a stable heterodimer.
55 9798686 During S phase of the cell cycle, BRCA1 polypeptides are found in discrete nuclear bodies ('BRCA1 nuclear dots') together with HsRad51, a human homolog of the E. coli recA protein, and BARD1, a protein that interacts with BRCA1 to form a stable heterodimer.
56 9798686 BARD1 is structurally similar to BRCA1 in that both molecules harbor an amino-terminal RING domain and two carboxy-terminal BRCT domains.
57 9798686 BARD1 is structurally similar to BRCA1 in that both molecules harbor an amino-terminal RING domain and two carboxy-terminal BRCT domains.
58 9798686 BARD1 is structurally similar to BRCA1 in that both molecules harbor an amino-terminal RING domain and two carboxy-terminal BRCT domains.
59 9798686 BARD1 is structurally similar to BRCA1 in that both molecules harbor an amino-terminal RING domain and two carboxy-terminal BRCT domains.
60 9798686 BARD1 is structurally similar to BRCA1 in that both molecules harbor an amino-terminal RING domain and two carboxy-terminal BRCT domains.
61 9798686 BARD1 is structurally similar to BRCA1 in that both molecules harbor an amino-terminal RING domain and two carboxy-terminal BRCT domains.
62 9798686 However, the remaining sequences of BARD1 display a markedly lower degree of phylogenetic conservation, comparable to those reported for BRCA1 and BRCA2.
63 9798686 However, the remaining sequences of BARD1 display a markedly lower degree of phylogenetic conservation, comparable to those reported for BRCA1 and BRCA2.
64 9798686 However, the remaining sequences of BARD1 display a markedly lower degree of phylogenetic conservation, comparable to those reported for BRCA1 and BRCA2.
65 9798686 However, the remaining sequences of BARD1 display a markedly lower degree of phylogenetic conservation, comparable to those reported for BRCA1 and BRCA2.
66 9798686 However, the remaining sequences of BARD1 display a markedly lower degree of phylogenetic conservation, comparable to those reported for BRCA1 and BRCA2.
67 9798686 However, the remaining sequences of BARD1 display a markedly lower degree of phylogenetic conservation, comparable to those reported for BRCA1 and BRCA2.
68 9798686 Moreover, murine Bard1 retains the ability to associate in vivo with BRCA1, and its expression pattern in adult mice mirrors that of Brca1, with elevated levels of RNA transcripts found in the testes and spleen.
69 9798686 Moreover, murine Bard1 retains the ability to associate in vivo with BRCA1, and its expression pattern in adult mice mirrors that of Brca1, with elevated levels of RNA transcripts found in the testes and spleen.
70 9798686 Moreover, murine Bard1 retains the ability to associate in vivo with BRCA1, and its expression pattern in adult mice mirrors that of Brca1, with elevated levels of RNA transcripts found in the testes and spleen.
71 9798686 Moreover, murine Bard1 retains the ability to associate in vivo with BRCA1, and its expression pattern in adult mice mirrors that of Brca1, with elevated levels of RNA transcripts found in the testes and spleen.
72 9798686 Moreover, murine Bard1 retains the ability to associate in vivo with BRCA1, and its expression pattern in adult mice mirrors that of Brca1, with elevated levels of RNA transcripts found in the testes and spleen.
73 9798686 Moreover, murine Bard1 retains the ability to associate in vivo with BRCA1, and its expression pattern in adult mice mirrors that of Brca1, with elevated levels of RNA transcripts found in the testes and spleen.
74 9798686 These data suggest that BRCA1 and BARD1 have co-evolved to participate in a common pathway of tumor suppression.
75 9798686 These data suggest that BRCA1 and BARD1 have co-evolved to participate in a common pathway of tumor suppression.
76 9798686 These data suggest that BRCA1 and BARD1 have co-evolved to participate in a common pathway of tumor suppression.
77 9798686 These data suggest that BRCA1 and BARD1 have co-evolved to participate in a common pathway of tumor suppression.
78 9798686 These data suggest that BRCA1 and BARD1 have co-evolved to participate in a common pathway of tumor suppression.
79 9798686 These data suggest that BRCA1 and BARD1 have co-evolved to participate in a common pathway of tumor suppression.
80 9832560 BRCA1-associated RING domain (BARD1) was identified as a protein interacting with the breast cancer gene product BRCA1.
81 9832560 BRCA1-associated RING domain (BARD1) was identified as a protein interacting with the breast cancer gene product BRCA1.
82 9832560 BRCA1-associated RING domain (BARD1) was identified as a protein interacting with the breast cancer gene product BRCA1.
83 9832560 BRCA1-associated RING domain (BARD1) was identified as a protein interacting with the breast cancer gene product BRCA1.
84 9832560 BRCA1-associated RING domain (BARD1) was identified as a protein interacting with the breast cancer gene product BRCA1.
85 9832560 The identification of tumorigenic missense mutations within BRCA1 that impair the formation of BARD1-BRCA1 complexes, and of BARD1 mutations in breast carcinomas, sustain the view that BARD1 is involved in BRCA1-mediated tumor suppression.
86 9832560 The identification of tumorigenic missense mutations within BRCA1 that impair the formation of BARD1-BRCA1 complexes, and of BARD1 mutations in breast carcinomas, sustain the view that BARD1 is involved in BRCA1-mediated tumor suppression.
87 9832560 The identification of tumorigenic missense mutations within BRCA1 that impair the formation of BARD1-BRCA1 complexes, and of BARD1 mutations in breast carcinomas, sustain the view that BARD1 is involved in BRCA1-mediated tumor suppression.
88 9832560 The identification of tumorigenic missense mutations within BRCA1 that impair the formation of BARD1-BRCA1 complexes, and of BARD1 mutations in breast carcinomas, sustain the view that BARD1 is involved in BRCA1-mediated tumor suppression.
89 9832560 The identification of tumorigenic missense mutations within BRCA1 that impair the formation of BARD1-BRCA1 complexes, and of BARD1 mutations in breast carcinomas, sustain the view that BARD1 is involved in BRCA1-mediated tumor suppression.
90 9832560 We have cloned the murine Bard1 gene and determined that its expression in different tissues correlates with the expression profile of Brca1.
91 9832560 We have cloned the murine Bard1 gene and determined that its expression in different tissues correlates with the expression profile of Brca1.
92 9832560 We have cloned the murine Bard1 gene and determined that its expression in different tissues correlates with the expression profile of Brca1.
93 9832560 We have cloned the murine Bard1 gene and determined that its expression in different tissues correlates with the expression profile of Brca1.
94 9832560 We have cloned the murine Bard1 gene and determined that its expression in different tissues correlates with the expression profile of Brca1.
95 9832560 To investigate the function of Bard1, we have reduced Bard1 gene expression in TAC-2 cells, a murine mammary epithelial cell line that retains morphogenetic properties characteristic of normal breast epithelium.
96 9832560 To investigate the function of Bard1, we have reduced Bard1 gene expression in TAC-2 cells, a murine mammary epithelial cell line that retains morphogenetic properties characteristic of normal breast epithelium.
97 9832560 To investigate the function of Bard1, we have reduced Bard1 gene expression in TAC-2 cells, a murine mammary epithelial cell line that retains morphogenetic properties characteristic of normal breast epithelium.
98 9832560 To investigate the function of Bard1, we have reduced Bard1 gene expression in TAC-2 cells, a murine mammary epithelial cell line that retains morphogenetic properties characteristic of normal breast epithelium.
99 9832560 To investigate the function of Bard1, we have reduced Bard1 gene expression in TAC-2 cells, a murine mammary epithelial cell line that retains morphogenetic properties characteristic of normal breast epithelium.
100 9832560 Partial repression of Bard1, achieved by the transfection of TAC-2 cells with plasmids constitutively expressing ribozymes or antisense RNAs, resulted in marked phenotypic changes, consisting of altered cell shape, increased cell size, high frequency of multinucleated cells, and aberrant cell cycle progression.
101 9832560 Partial repression of Bard1, achieved by the transfection of TAC-2 cells with plasmids constitutively expressing ribozymes or antisense RNAs, resulted in marked phenotypic changes, consisting of altered cell shape, increased cell size, high frequency of multinucleated cells, and aberrant cell cycle progression.
102 9832560 Partial repression of Bard1, achieved by the transfection of TAC-2 cells with plasmids constitutively expressing ribozymes or antisense RNAs, resulted in marked phenotypic changes, consisting of altered cell shape, increased cell size, high frequency of multinucleated cells, and aberrant cell cycle progression.
103 9832560 Partial repression of Bard1, achieved by the transfection of TAC-2 cells with plasmids constitutively expressing ribozymes or antisense RNAs, resulted in marked phenotypic changes, consisting of altered cell shape, increased cell size, high frequency of multinucleated cells, and aberrant cell cycle progression.
104 9832560 Partial repression of Bard1, achieved by the transfection of TAC-2 cells with plasmids constitutively expressing ribozymes or antisense RNAs, resulted in marked phenotypic changes, consisting of altered cell shape, increased cell size, high frequency of multinucleated cells, and aberrant cell cycle progression.
105 9894790 A role for BRCA1 and BRCA2 in the control of genome integrity easily fits a tumor suppressor model.
106 9894790 The studies summarized here suggest that BRCA1, BRCA2, RAD51. and BARD1 function as a biochemical complex.
107 9894790 Experimental data suggest that BRCA1 and BRCA2 function as regulators of transcription.
108 9894790 Are the DNA repair and transcriptional regulatory functions of BRCA1 and BRCA2 related?
109 9894790 BRCA1 and BRCA2 may maintain the integrity of the genome by regulating expression of genes directly involved in this process.
110 9894790 If BRCA1 and BRCA2 are ubiquitously expressed, why do mutations in BRCA1 and BRCA2 lead specifically to tumors primarily of the breast and ovary, as well as a limited number of other tissues to a lesser degree?
111 9894790 Nothing to date has been revealed that would explain how alteration of the transcriptional regulatory function and or the DNA repair function ascribed to BRCA1 and BRCA2 would result in tumor specificity as both of these functions are essential to a broad spectrum of tissues.
112 9894790 It is possible that BRCAI and BRCA2 may regulate genes expressed only in the breast and ovary.
113 9894790 Similarly, there may be unidentified BRCA1 and BRCA2 co-factors that are active only in the breast and ovary and, therefore, are critical to tumorigenesis.
114 10026184 Interaction of the ring finger domains of BRCA1 and BARD1.
115 10026184 Interaction of the ring finger domains of BRCA1 and BARD1.
116 10026184 Interaction of the ring finger domains of BRCA1 and BARD1.
117 10026184 Interaction of the ring finger domains of BRCA1 and BARD1.
118 10026184 Interaction of the ring finger domains of BRCA1 and BARD1.
119 10026184 Interaction of the ring finger domains of BRCA1 and BARD1.
120 10026184 Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions.
121 10026184 Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions.
122 10026184 Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions.
123 10026184 Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions.
124 10026184 Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions.
125 10026184 Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions.
126 10026184 To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the structural domains required for the interaction, as well as their oligomerization state, relative stability, and possible nucleic acid binding activity.
127 10026184 To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the structural domains required for the interaction, as well as their oligomerization state, relative stability, and possible nucleic acid binding activity.
128 10026184 To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the structural domains required for the interaction, as well as their oligomerization state, relative stability, and possible nucleic acid binding activity.
129 10026184 To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the structural domains required for the interaction, as well as their oligomerization state, relative stability, and possible nucleic acid binding activity.
130 10026184 To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the structural domains required for the interaction, as well as their oligomerization state, relative stability, and possible nucleic acid binding activity.
131 10026184 To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the structural domains required for the interaction, as well as their oligomerization state, relative stability, and possible nucleic acid binding activity.
132 10026184 We have found that the RING finger motifs do not themselves constitute stable structural domains but are instead part of larger domains comprising residues 1-109 of BRCA1 and residues 26-119 of BARD1.
133 10026184 We have found that the RING finger motifs do not themselves constitute stable structural domains but are instead part of larger domains comprising residues 1-109 of BRCA1 and residues 26-119 of BARD1.
134 10026184 We have found that the RING finger motifs do not themselves constitute stable structural domains but are instead part of larger domains comprising residues 1-109 of BRCA1 and residues 26-119 of BARD1.
135 10026184 We have found that the RING finger motifs do not themselves constitute stable structural domains but are instead part of larger domains comprising residues 1-109 of BRCA1 and residues 26-119 of BARD1.
136 10026184 We have found that the RING finger motifs do not themselves constitute stable structural domains but are instead part of larger domains comprising residues 1-109 of BRCA1 and residues 26-119 of BARD1.
137 10026184 We have found that the RING finger motifs do not themselves constitute stable structural domains but are instead part of larger domains comprising residues 1-109 of BRCA1 and residues 26-119 of BARD1.
138 10026184 Shorter BRCA1 RING finger constructs do not interact with BARD1 or with longer BRCA1 constructs, indicating that the heterodimeric and homodimer interactions are mediated by regions outside the canonical RING finger motif.
139 10026184 Shorter BRCA1 RING finger constructs do not interact with BARD1 or with longer BRCA1 constructs, indicating that the heterodimeric and homodimer interactions are mediated by regions outside the canonical RING finger motif.
140 10026184 Shorter BRCA1 RING finger constructs do not interact with BARD1 or with longer BRCA1 constructs, indicating that the heterodimeric and homodimer interactions are mediated by regions outside the canonical RING finger motif.
141 10026184 Shorter BRCA1 RING finger constructs do not interact with BARD1 or with longer BRCA1 constructs, indicating that the heterodimeric and homodimer interactions are mediated by regions outside the canonical RING finger motif.
142 10026184 Shorter BRCA1 RING finger constructs do not interact with BARD1 or with longer BRCA1 constructs, indicating that the heterodimeric and homodimer interactions are mediated by regions outside the canonical RING finger motif.
143 10026184 Shorter BRCA1 RING finger constructs do not interact with BARD1 or with longer BRCA1 constructs, indicating that the heterodimeric and homodimer interactions are mediated by regions outside the canonical RING finger motif.
144 10026184 We show that neither the homodimers nor the heterodimer displays affinity for nucleic acids, indicating that the proposed roles of BRCA1 and BARD1 in DNA repair and/or transcriptional activation must be mediated either by other regions of the proteins or by additional cofactors.
145 10026184 We show that neither the homodimers nor the heterodimer displays affinity for nucleic acids, indicating that the proposed roles of BRCA1 and BARD1 in DNA repair and/or transcriptional activation must be mediated either by other regions of the proteins or by additional cofactors.
146 10026184 We show that neither the homodimers nor the heterodimer displays affinity for nucleic acids, indicating that the proposed roles of BRCA1 and BARD1 in DNA repair and/or transcriptional activation must be mediated either by other regions of the proteins or by additional cofactors.
147 10026184 We show that neither the homodimers nor the heterodimer displays affinity for nucleic acids, indicating that the proposed roles of BRCA1 and BARD1 in DNA repair and/or transcriptional activation must be mediated either by other regions of the proteins or by additional cofactors.
148 10026184 We show that neither the homodimers nor the heterodimer displays affinity for nucleic acids, indicating that the proposed roles of BRCA1 and BARD1 in DNA repair and/or transcriptional activation must be mediated either by other regions of the proteins or by additional cofactors.
149 10026184 We show that neither the homodimers nor the heterodimer displays affinity for nucleic acids, indicating that the proposed roles of BRCA1 and BARD1 in DNA repair and/or transcriptional activation must be mediated either by other regions of the proteins or by additional cofactors.
150 10195418 The function of BRCA1 has been examined in gene knockout mice in which the nullizygous mice die early in utero, but this lethality can be partially rescued by a nullizygous p53 mutation.
151 10195418 Wild-type BRCA1 protein binds to a number of cellular proteins, including DNA repair protein Rad51, tumor suppressor p53, RNA polymerase II holoenzyme, RNA helicase A, CtBP-interacting protein, c-myc, BRCA1-associated RING domain protein (BARD1), BRCA2 protein, etc.