BRCA1: Wikis


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From Wikipedia, the free encyclopedia

Breast cancer 1, early onset

PDB rendering based on 1jm7.
Available structures
1jm7, 1jnx, 1n5o, 1oqa, 1t15, 1t29, 1t2u, 1t2v, 1y98
External IDs OMIM113705 MGI104537 HomoloGene5276 GeneCards: BRCA1 Gene
RNA expression pattern
PBB GE BRCA1 204531 s at.png
PBB GE BRCA1 211851 x at.png
More reference expression data
Species Human Mouse
Entrez 672 12189
Ensembl ENSG00000012048 ENSMUSG00000017146
UniProt P38398 Q3UMS5
RefSeq (mRNA) NM_007294 NM_009764
RefSeq (protein) NP_009225 NP_033894
Location (UCSC) Chr 17:
38.45 - 38.53 Mb
Chr 11:
101.31 - 101.37 Mb
PubMed search [1] [2]
Location of the BRCA1 gene on chromosome 17.

BRCA1 (breast cancer 1, early onset) is a human tumor suppressor gene, which produces a protein, called breast cancer type 1 susceptibility protein. It is found in the cells of breast and other tissue, where it helps repair damaged DNA, and destroy the cell when DNA can't be repaired. If BRCA1 itself is damaged, the damaged DNA can let the cell duplicate without control, and turn into a cancer.[1][2]

The protein encoded by the BRCA1 gene combines with other tumor suppressors, DNA damage sensors, and signal transducers to form a large multi-subunit protein complex known as the BRCA1-associated genome surveillance complex (BASC).[3] The BRCA1 protein associates with RNA polymerase II, and through the C-terminal domain, also interacts with histone deacetylase complexes. This protein thus plays a role in transcription, DNA repair of double-stranded breaks[2] ubiquitination, transcriptional regulation as well as other functions.[4]


Gene location

The human BRCA1 gene is located on the long (q) arm of chromosome 17 at band 21, from base pair 38,449,840 to base pair 38,530,994 (map). BRCA1 orthologs [5] have been identified in most mammals for which complete genome data are available.

Protein structure

The BRCA1 protein (breast cancer type 1 susceptibility protein also known as RING finger protein 53) contains the following domains:[6]

This protein also contains nuclear localization signal and nuclear export signal motifs.[7]

Function and mechanism

BRCA1 repairs double-strand breaks in DNA. The strands of the DNA double helix are continually breaking from damage. Sometimes one strand is broken, and sometimes both strands are broken simultaneously. BRCA1 is part of a protein complex that repairs DNA when both strands are broken. When both strands are broken, it's difficult for the repair mechanism to "know" how to replace the correct DNA sequence, and there are multiple ways to attempt the repair. The double-stranded repair mechanism that BRCA1 participates in is homologous recombination, in which the repair proteins utilize homologous intact sequence from a sister chromatid, homologous chromosome, or from the same chromosome (depending on cell cyle phase) as a template.[8] This DNA repair takes place with the DNA in the cell nucleus, wrapped around the histone. Several proteins, including BRCA1, arrive at the histone-DNA complex for this repair.

In the nucleus of many types of normal cells, the BRCA1 protein interacts with RAD51 during repair of DNA double-strand breaks.[9] These breaks can be caused by natural radiation or other exposures, but also occur when chromosomes exchange genetic material (homologous recombination, e.g. "crossing over" during meiosis). The BRCA2 protein, which has a function similar to that of BRCA1, also interacts with the RAD51 protein. By influencing DNA damage repair, these three proteins play a role in maintaining the stability of the human genome.

BRCA1 directly binds to DNA, with higher affinity for branched DNA structures. This ability to bind to DNA contributes to its ability to inhibit the nuclease activity of the MRN complex as well as the nuclease activity of Mre11 alone.[10] This may explain a role for BRCA1 to promote higher fidelity DNA repair by non-homologous end joining (NHEJ).[11] BRCA1 also colocalizes with γ-H2AX (histone H2AX phosphorylated on serine-139) in DNA double-strand break repair foci, indicating it may play a role in recruiting repair factors.[4][12]



BRCA1 was shown to co-purify with the human RNA Polymerase II holoenzyme in HeLa extracts, implying it is a component of the holoenzyme.[13] Later research, however, contradicted this assumption, instead showing that the predominant complex including BRCA1 in HeLa cells is a 2 megadalton complex containing SWI/SNF.[14] SWI/SNF is a chromatin remodeling complex. Artificial tethering of BRCA1 to chromatin was shown to decondense heterochromatin, though the SWI/SNF interacting domain was not necessary for this role.[12] BRCA1 interacts with the NELF-B (COBRA1) subunit of the NELF complex.[12]

Other roles

Research suggests that both the BRCA1 and BRCA2 proteins regulate the activity of other genes and play a critical role in embryo development. The BRCA1 protein probably interacts with many other proteins, including tumor suppressors and regulators of the cell division cycle.

Mutations and cancer risk

Certain variations of the BRCA1 gene lead to an increased risk for breast cancer. Researchers have identified hundreds of mutations in the BRCA1 gene, many of which are associated with an increased risk of cancer. Women who have an abnormal BRCA1 or BRCA2 gene have up to an 85% risk of developing breast cancer by age 70; increased risk of developing ovarian cancer is about 55% for women with BRCA1 mutations and about 25% for women with BRCA2 mutations.[15]

These mutations can be changes in one or a small number of DNA base pairs (the building blocks of DNA). Those mutations can be identified with PCR and DNA sequencing.

In some cases, large segments of DNA are rearranged. Those large segments, also called large rearrangements, can be a deletion or a duplication of one or several exons in the gene. Classical methods for mutations detection(sequencing) are unable to reveal those mutations.[16] Other methods are proposed: Q-PCR,[17] Multiplex Ligation-dependent Probe Amplification (MLPA),[18] and Quantitative Multiplex PCR of Shorts Fluorescents Fragments (QMPSF).[19] New methods have been recently proposed: heteroduplex analysis (HDA) by multi-capillary electrophoresis or also dedicated oligonucleotides array based on comparative genomic hybridization (array-CGH).[20]

The participation of BRCA1 in the development of breast cancer has been proposed in several studies where hypermethylation of its promoter. Some results suggest that hypermethylation could be considered as an inactivating mechanism for BRCA1 expression, which has been reported in some cancers.[21]

A mutated BRCA1 gene usually makes a protein that does not function properly because it is abnormally short. Researchers believe that the defective BRCA1 protein is unable to help fix mutations that occur in other genes. These defects accumulate and may allow cells to grow and divide uncontrollably to form a tumor.

In addition to breast cancer, mutations in the BRCA1 gene also increase the risk on ovarian, fallopian tube and prostate cancers. Moreover, precancerous lesions (dysplasia) within the Fallopian tube have been linked to BRCA1 gene mutations. Pathogenic mutations anywhere in a model pathway containing BRCA1 and BRCA2 greatly increase risks for a subset of leukemias and lymphomas.[2]

Germ line mutations and founder effect

All germ line BRCA1 mutations identified to date have been inherited, suggesting the possibility of a large “founder” effect in which a certain mutation is common to a well-defined population group and can theoretically be traced back to a common ancestor. Given the complexity of mutation screening for BRCA1, these common mutations may simplify the methods required for mutation screening in certain populations. Analysis of mutations that occur with high frequency also permits the study of their clinical expression[22]. Examples of manifestations of a founder effect are seen among Ashkenazi Jews. Three mutations in BRCA1 have been reported to account for the majority of Ashkenazi Jewish patients with inherited BRCA1-related breast and/or ovarian cancer: 185delAG, 188del11 and 5382insC in the BRCA1 gene [23] [24]. In fact, it has been shown that if a Jewish woman does not carry a BRCA1 185delAG, BRCA1 5382insC founder mutation, it is highly unlikely that a different BRCA1 mutation will be found [25]. Additional examples of founder mutations in BRCA1 are given in Table 1 [mainly derived from [22]]. Reference for mutation nomenclature: [den Dunnen and Antonarakis, 2000] [26].

Population or subgroup BRCA1 mutation(s) Reference(s)
African-Americans 943ins10, M1775R [27]
Ashkenazi Jewish 185delAG, 188del11, 5382insC [23] [24]
Austrians 2795delA, C61G, 5382insC, Q1806stop [28]
Belgians 2804delAA, IVS5+3A>G [29] [30]
Dutch Exon 2 deletion, exon 13 deletion, 2804delAA [31] [29] [32]
Finns 3745delT, IVS11-2A>G [33] [34]
French 3600del11, G1710X [35]
French Canadians C4446T [36]
Germans 5382insC [37]
Greeks 5382insC [38]
Hungarians 300T>G, 5382insC, 185delAG [39]
Italians 5083del19 [40]
Japanese L63X, Q934X [41]
Native North Americans 1510insG, 1506A>G [42]
Northern Irish 2800delAA [43]
Norwegians 816delGT, 1135insA, 1675delA, 3347delAG [44] [45]
Pakistanis 2080insA, 3889delAG, 4184del4, 4284delAG, IVS14-1A>G [46]
Polish 300T>G, 5382insC, C61G, 4153delA [47] [48]
Russians 5382insC, 4153delA [49]
Scottish 2800delAA [50] [43]
South Afrikaners E881X [51]
Spanish R71G [52] [53]
Swedish Q563X, 3171ins5, 1201del11, 2594delC [27] [54]


BRCA1 together with BRCA2 are patented in the United States by Myriad Genetics.[55] This US patent has been challenged by the American Civil Liberties Union.[56]


BRCA1 has been shown to interact with

Browser View

View a graphical representation of all GenBank isoforms at the UCSC Genome Browser

UCSC Gene details page

See also


  1. ^ "Breast and Ovarian Cancer Genetic Screening". Palo Alto Medical Foundation. Retrieved 2008-10-11. 
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  3. ^ a b c d e f g Wang, Y; Cortez D, Yazdi P, Neff N, Elledge S J, Qin J (Apr. 2000). "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures". Genes Dev. 14 (8): 927–39. PMID 10783165.  [Free full text]
  4. ^ a b Starita, L.M.; Parvin, J.D. (2003). "The multiple nuclear functions of BRCA1: transcription, ubiquitination and DNA repair". Current Opinion in Cell Biology 15 (3): 345–350. doi:10.1016/S0955-0674(03)00042-5. PMID 12787778. 
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  8. ^ Kimball's Biologh Pages
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  10. ^ Paull, T.T.; Cortez, D.; Bowers, B.; Elledge, S.J.; Gellert, M. (2001). "Direct DNA binding by Brca1". Proceedings of the National Academy of Sciences 98: 6086–6091. doi:10.1073/pnas.111125998. PMID 11353843. 
  11. ^ Durant, S.T.; Nickoloff, J.A. (2005). "Good timing in the cell cycle for precise DNA repair by BRCA1". Cell Cycle 4 (9): 1216–22. Retrieved 2008-05-05. 
  12. ^ a b c Ye, Q.; Hu, Y.F.; Zhong, H.; Nye, A.C.; Belmont, A.S.; Li, R. (2001). "BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations". The Journal of Cell Biology 155 (6): 911–922. doi:10.1083/jcb.200108049. PMID 11739404. 
  13. ^ Scully, R.; Anderson, S.F.; Chao, D.M.; Wei, W.; Ye, L.; Young, R.A.; Livingston, D.M.; Parvin, J.D. (1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proceedings of the National Academy of Sciences 94 (11): 5605. doi:10.1073/pnas.94.11.5605. PMID 9159119. 
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  15. ^ > Cancer Risk and Abnormal Breast Cancer Genes Page last modified on: August 7, 2008
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  25. ^ Narod, SA; Foulkes, WD. (2004). "BRCA1 and BRCA2: 1994 and beyond". Nature Reviews on Cancer 4: 665 – 676. PMID 15343273. 
  26. ^ den Dunnen, JT; Antonarakis, SE. (2000). "Mutation nomenclature extensions and suggestions to describe complex mutations: a discussion.". Human Mutation 15: 7 – 12. PMID 10612815. 
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  28. ^ Wagner, TM; Moslinger, RA; Muhr, D; Langbauer, G; Hirtenlehner, K; Concin, H; Doeller, W; Haid, A; Lang, AH; Mayer, P; Ropp, E; Kubista, E; Amirimani, B; Helbich, T; Becherer, A; Scheiner, O; Breiteneder, H; Borg, A; Devilee, P; Oefner, P; Zielinski, C. (1998). "BRCA1-related breast cancer in Austrian breast and ovarian cancer families: specific BRCA1 mutations and pathological characteristics". International Journal of Cancer 77: 354 – 360. PMID 9663595. 
  29. ^ a b Peelen, T; van Vliet, M; Petrij-Bosch, A; Mieremet, R; Szabo, C; van den Ouweland, AM; Hogervorst, F; Brohet, R; Ligtenberg, MJ; Teugels, E; van der Luijt, RB; van der Hout, AH; Gille, JJ; Pals, G; Jedema, I; Olmer, R; van Leeuwen, I; Newman, B; Plandsoen, M; van der Est, M; Brink, G; Hageman, S; Arts, PJ; Bakker, MM; Devilee, P. (1997). "A high proportion of novel mutations in BRCA1 with strong founder effects among Dutch and Belgian hereditary breast and ovarian cancer families". American Journal of Human Genetics 60: 1041 – 1049. PMID 9150151. 
  30. ^ Claes, K; Machackova, E; De Vos, M; Poppe, B; De Paepe, A; Messiaen, L. (1999). "Mutation analysis of the BRCA1 and BRCA2 genes in the Belgian patient population and identification of a Belgian founder mutation BRCA1 IVS5 + 3A > G". Disease Markers 15: 69 – 73. PMID 10595255. 
  31. ^ Petrij-Bosch, A; Peelen, T; van Vliet, M; van Eijk, R; Olmer, R; Drusedau, M; Hogervorst, FB; Hageman, S; Arts, PJ; Ligtenberg, MJ; Meijers-Heijboer, H; Klijn, JG; Vasen, HF; Cornelisse, CJ; van Bakker, E; van Ommen, GJ; Devilee, P. (1997). "BRCA1 genomic deletions are major founder mutations in Dutch breast cancer patients". Nature Genetics 17: 341 – 345. PMID 9354803. 
  32. ^ Verhoog, LC; van den Ouweland, AM; Berns, E; van Veghel-Plandsoen, MM; van Staveren, IL; Wagner, A; Bartels, CC; Tilanus-Linthorst, MM; Devilee, P; Seynaeve, C; Halley, DJ; Niermeijer, MF; Klijn, JG; Meijers-Heijboer, H. (2001). "Large regional differences in the frequency of distinct BRCA1/BRCA2 mutations in 517 Dutch breast and/or ovarian cancer families". European Journal of Cancer 37: 2082 – 2090. PMID 11597388. 
  33. ^ Huusko, P; Pääkkönen, K; Launonen, V; Poyhonen, M; Blanco, G; Kauppila, A; Puistola, U; Kiviniemi, H; Kujala, M; Leisti, J; Winqvist, R. (1998). "Evidence of founder mutations in Finnish BRCA1 and BRCA2 families". American Journal of Human Genetics 62: 1544 – 1548. PMID 9585608. 
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  35. ^ Muller, D; Bonaiti-Pelie, C; Abecassis, J; Stoppa-Lyonnet, D; Fricker, JP. (2004). "BRCA1 testing in breast and/or ovarian cancer families from northeastern France identifies two common mutations with a founder effect". Familial Cancer 3: 15 – 20. PMID 15131401. 
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  37. ^ Backe, J; Hofferbert, S; Skawran, B; Dork, T; Stuhrmann, M; Karstens, JH; Untch, M; Meindl, A; Burgemeister, R; Chang-Claude, J; Weber, BH. (1999). "Frequency of BRCA1 mutation 5382insC in German breast cancer patients". Gynecologic Oncology 72: 402 – 406. PMID 10053113. 
  38. ^ Ladopoulou, A; Kroupis, C; Konstantopoulou, I; Ioannidou-Mouzaka, L; Schofield, AC; Pantazidis, A; Armaou, S; Tsiagas, I; Lianidou, E; Efstathiou, E; Tsionou, C; Panopoulos, C; Mihalatos, M; Nasioulas, G; Skarlos, D; Haites, NE; Fountzilas, G; Pandis, N; Yannoukakos, D. (2002). "Germ line BRCA1 and BRCA2 mutations in Greek breast/ovarian cancer families: 5382insC is the most frequent mutation observed". Cancer Letters 185: 61 – 70. PMID 12142080. 
  39. ^ Van Der Looij, M; Szabo, C; Besznyak, I; Liszka, G; Csokay, B; Pulay, T; Toth, J; Devilee, P; King, MC; Olah, E. (2000). "Prevalence of founder BRCA1 and BRCA2 mutations among breast and ovarian cancer patients in Hungary". International Journal of Cancer 86: 737 – 740. PMID 10797299. 
  40. ^ Baudi, F; Quaresima, B; Grandinetti, C; Cuda, G; Faniello, C; Tassone, P; Barbieri, V; Bisegna, R; Ricevuto, E; Conforti, S; Viel, A; Marchetti, P; Ficorella, C; Radice, P; Costanzo, F; Venuta, S. (2001). "Evidence of a founder mutation of BRCA1 in a highly homogeneous population from southern Italy with breast/ovarian cancer". Human Mutation 18: 163 – 164. PMID 11462242. 
  41. ^ Sekine, M; Nagata, H; Tsuji, S; Hirai, Y; Fujimoto, S; Hatae, M; Kobayashi, I; Fujii, T; Nagata, I; Ushijima, K; Obata, K; Suzuki, M; Yoshinaga, M; Umesaki, N; Satoh, S; Enomoto, T; Motoyama, S; Tanaka K; Japanese Familial Ovarian Cancer Study Group. (2001). "Mutational analysis of BRCA1 and BRCA2 and clinicopathologic analysis of ovarian cancer in 82 ovarian cancer families: two common founder mutations of BRCA1 in Japanese population". Clinical Cancer Research 7: 3144 – 3150. PMID 11595708. 
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  44. ^ Borg, A; Dørum, A; Heimdal, K; Maehle, L; Hovig, E; Møller, P. (1999). "BRCA1 1675delA and 1135insA account for one third of Norwegian familial breast-ovarian cancer and are associated with later disease onset than less frequent mutations". Disease Markers 15: 79 – 84. PMID 10595257. 
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  47. ^ Górski, B; Byrski, T; Huzarski, T; Jakubowska, A; Menkiszak, J; Gronwald, J; Pluzanska, A; Bebenek, M; Fischer-Maliszewska, L; Grzybowska, E; Narod, SA; Lubinski, J. (2000). "Founder mutations in the BRCA1 gene in Polish families with breast-ovarian cancer". American Journal of Human Genetics 66: 1963 – 1968. PMID 10788334. 
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  50. ^ Liede, A; Cohen, B; Black, DM; Davidson, RH; Renwick, A; Hoodfar, E; Olopade, OI; Micek, M; Anderson, V; De Mey, R; Fordyce, A; Warner, E; Dann, JL; King, MC; Weber, B; Narod, SA; Steel, CM. (2000). "Evidence of a founder BRCA1 mutation in Scotland". British Journal of Cancer 82: 705 – 711. PMID 10682686. 
  51. ^ Reeves, MD; Yawitch, TM; van der Merwe, NC; van den Berg, HJ; Dreyer, G; van Rensburg, EJ. (2004). "BRCA1 mutations in South African breast and/or ovarian cancer families: evidence of a novel founder mutation in Afrikaner families". International Journal of Cancer 110: 677 – 682. PMID 15146556. 
  52. ^ Vega, A; Campos, B; Bressac-De-Paillerets, B; Bond, PM; Janin, N; Douglas, FS; Domenech, M; Baena, M; Pericay, C; Alonso, C; Carracedo, A; Baiget, M; Diez, O. (2001). "The R71G BRCA1 is a founder Spanish mutation and leads to aberrant splicing of the transcript.". Human Mutation 17: 520 – 521. PMID 11385711. 
  53. ^ Campos, B; Diez, O; Odefrey, F; Domenech, M; Moncoutier, V; Martinez-Ferrandis, JI; Osorio, A; Balmana, J; Barroso, A; Armengod, ME; Benitez, J; Alonso, C; Stoppa-Lyonnet, D; Goldgar, D; Baiget, M. (2003). "Haplotype analysis of the BRCA2 9254delATCAT recurrent mutation in breast/ovarian cancer families from Spain". Human Mutation 21: 452. PMID 12655574. 
  54. ^ Bergman, A; Einbeigi, Z; Olofsson, U; Taib, Z; Wallgren, A; Karlsson, P; Wahlstrom, J; Martinsson, T; Nordling, M. (2001). "The western Swedish BRCA1 founder mutation 3171ins5; a 3.7 cM conserved haplotype of today is a reminiscence of a 1500-year-old mutation". European Journal of Human Genetics 9: 787 – 793. PMID 11781691. 
  55. ^ US patent 5747282, Skolnick HS, Goldgar DE, Miki Y, Swenson J, Kamb A, Harshman KD, Shattuck-Eidens DM, Tavtigian SV, Wiseman RW, Futreal PA, "7Q-linked breast and ovarian cancer susceptibility gene", granted 1998-05-05 , assigned to Myraid Genetics, Inc., The United States of America as represented by the Secretary of Health and Human Services, and University of Utah Research Foundation,. 
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Further reading

  • Cui JQ, Wang H, Reddy ES, Rao VN (1998). "Differential transcriptional activation by the N-terminal region of BRCA1 splice variants BRCA1a and BRCA1b". Oncology reports 5 (3): 585–9. PMID 9538156. 
  • Wang H, Shao N, Ding QM, Cui J, Reddy ES, Rao VN (July 1997). "BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases". Oncogene 15 (2): 143–57. doi:10.1038/sj.onc.1201252. PMID 9244350. 
  • Cui JQ, Wang H, Reddy ES, Rao VN (1998). "Differential transcriptional activation by the N-terminal region of BRCA1 splice variants BRCA1a and BRCA1b". Oncology reports 5 (3): 585–9. PMID 9538156. 
  • Cui JQ, Shao N, Chai Y, Wang H, Reddy ES, Rao VN (1998). "BRCA1 splice variants BRCA1a and BRCA1b associate with CBP co-activator". Oncology reports 5 (3): 591–5. PMID 9538157. 
  • Zou JP, Hirose Y, Siddique H, Rao VN, Reddy ES (1999). "Structure and expression of variant BRCA2a lacking the transactivation domain". Oncology reports 6 (2): 437–40. PMID 10023017. 
  • Antoniou A, Pharoah PD, Narod S, Risch HA, Eyfjord JE, Hopper JL, Loman N, Olsson H, Johannsson O, Borg A, Pasini B, Radice P, Manoukian S, Eccles DM, Tang N, Olah E, Anton-Culver H, Warner E, Lubinski J, Gronwald J, Gorski B, Tulinius H, Thorlacius S, Eerola H, Nevanlinna H, Syrjakoski K, Kallioniemi OP, Thompson D, Evans C, Peto J, Lalloo F, Evans DG, Easton DF (2003). "Average risks of breast and ovarian cancer associated with BRCA1 or BRCA2 mutations detected in case Series unselected for family history: a combined analysis of 22 studies". Am J Hum Genet 72 (5): 1117–30. doi:10.1086/375033. PMID 12677558. 
  • Barnett GL, Friedrich CA (2004). "Recent developments in ovarian cancer genetics". Curr Opin Obstet Gynecol 16 (1): 79–85. doi:10.1097/00001703-200402000-00014. PMID 15128012. 
  • Botuyan MV, Nomine Y, Xu Y, Juranic N, Macura S, Chen J, Mer G (2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure 12 (7): 1137–1146. doi:10.1016/j.str.2004.06.002. PMID 15242590. 
  • Daniel DC (2002). "Highlight: BRCA1 and BRCA2 proteins in breast cancer". Microsc Res Tech 59 (1): 68–83. doi:10.1002/jemt.10178. PMID 12242698. 
  • Ding SL, Sheu LF, Yu JC, Yang TL, Chen BF, Leu FJ, Shen CY (2004). "Abnormality of the DNA double-strand-break checkpoint/repair genes, ATM, BRCA1 and TP53, in breast cancer is related to tumour grade". Br J Cancer 90 (10): 1995–2001. doi:10.1038/sj.bjc.6601804. PMID 15138484. 
  • Foulkes WD, Metcalfe K, Sun P, Hanna WM, Lynch HT, Ghadirian P, Tung N, Olopade OI, Weber BL, McLennan J, Olivotto IA, Begin LR, Narod SA (2004). "Estrogen receptor status in BRCA1- and BRCA2-related breast cancer: the influence of age, grade, and histological type". Clin Cancer Res 10 (6): 2029–34. doi:10.1158/1078-0432.CCR-03-1061. PMID 15041722. 
  • Hall JM, Lee MK, Newman B, Morrow JE, Anderson LA, Huey B, King MC (1990). "Linkage of early-onset familial breast cancer to chromosome 17q21". Science 250 (4988): 1684–89. doi:10.1126/science.2270482. PMID 2270482. 
  • Liede A, Karlan BY, Narod SA (2004). "Cancer risks for male carriers of germline mutations in BRCA1 or BRCA2: a review of the literature". J Clin Oncol 22 (4): 735–42. doi:10.1200/JCO.2004.05.055. PMID 14966099. 
  • Metcalfe K, Lynch HT, Ghadirian P, Tung N, Olivotto I, Warner E, Olopade OI, Eisen A, Weber B, McLennan J, Sun P, Foulkes WD, Narod SA (2004). "Contralateral breast cancer in BRCA1 and BRCA2 mutation carriers". J Clin Oncol 22 (12): 2328–35. doi:10.1200/JCO.2004.04.033. PMID 15197194. 
  • Parthasarathy, Shobita (2007). Building Genetic Medicine: Breast Cancer, Technology, and the Comparative Politics of Health Care. The MIT Press. ISBN 978-0-262-016242-5. 
  • Powell SN, Kachnic LA (2003). "Roles of BRCA1 and BRCA2 in homologous recombination, DNA replication fidelity and the cellular response to ionizing radiation". Oncogene 22 (37): 5784–91. doi:10.1038/sj.onc.1206678. PMID 12947386. 
  • Scully R, Puget N (2002). "BRCA1 and BRCA2 in hereditary breast cancer". Biochimie 84 (1): 95–102. doi:10.1016/S0300-9084(01)01359-1. PMID 11900881. 
  • Tutt A, Ashworth A (2002). "The relationship between the roles of BRCA genes in DNA repair and cancer predisposition". Trends Mol Med 8 (12): 571–6. doi:10.1016/S1471-4914(02)02434-6. PMID 12470990. 
  • Venkitaraman AR (2002). "Cancer susceptibility and the functions of BRCA1 and BRCA2". Cell 108 (2): 171–82. doi:10.1016/S0092-8674(02)00615-3. PMID 11832208. 
  • Zweemer RP, van Diest PJ, Verheijen RH, Ryan A, Gille JJ, Sijmons RH, Jacobs IJ, Menko FH, Kenemans P (2000). "Molecular evidence linking primary cancer of the fallopian tube to BRCA1 germline mutations". Gynecol oncol 76 (1): 45. doi:10.1006/gyno.1999.5623. PMID 10620440. 
  • Piek JM, van Diest PJ, Zweemer RP, Jansen JW, Poort-Keesom RJ, Menko FH, Gille JJ, Jongsma AP, Pals G, Kenemans P, Verheijen RH (2001). "Dysplastic changes in prophylactically removed Fallopian tubes of women predisposed to developing ovarian cancer". J Pathol. 195 (4): 451. doi:10.1002/path.1000. PMID 11745677. 

External links


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