{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,19]],"date-time":"2026-02-19T03:54:34Z","timestamp":1771473274294,"version":"3.50.1"},"reference-count":2,"publisher":"BMJ","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Mol Path"],"published-print":{"date-parts":[[1998,10]]},"DOI":"10.1136\/mp.51.5.237","type":"journal-article","created":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T19:10:34Z","timestamp":1230750634000},"page":"237-247","source":"Crossref","is-referenced-by-count":52,"title":["BRCA1 and BRCA2 proteins: roles in health and disease."],"prefix":"10.1136","volume":"51","author":[{"given":"J A","family":"Duncan","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J R","family":"Reeves","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T G","family":"Cooke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"239","published-online":{"date-parts":[[1998,10,1]]},"reference":[{"key":"ref_1","article-title":"The protein kinase(s) and protein phosphatase(s) could therefore perform the important task of regulating BRCA1 activity. Already suggested for this role have been CDK2\u2212cyclin D or CDK2\u2212cyclin A complexes,35 both of which have been shown to be capable of phosphorylating BRCA1 in vitro. Given the recognised association of hyperphosphorylated BRCA1 and its localisation to nuclear dots, it is interesting to note that exposure of cells to DNA damaging agents causes promotion of hyperphosphorylation yet leads to the elimination of the punctate nuclear staining pattern normally seen for BRCA1. This suggests that hyperphosphorylation itself is not the localising signal for congregation to nuclear foci.46","unstructured":"The protein kinase(s) and protein phosphatase(s) could therefore perform the important task of regulating BRCA1 activity. Already suggested for this role have been CDK2\u2212cyclin D or CDK2\u2212cyclin A complexes,35 both of which have been shown to be capable of phosphorylating BRCA1 in vitro. Given the recognised association of hyperphosphorylated BRCA1 and its localisation to nuclear dots, it is interesting to note that exposure of cells to DNA damaging agents causes promotion of hyperphosphorylation yet leads to the elimination of the punctate nuclear staining pattern normally seen for BRCA1. This suggests that hyperphosphorylation itself is not the localising signal for congregation to nuclear foci.46"},{"key":"ref_2","article-title":"BRCA2 mRNA expression has been shown to be regulated with the cell cycle and associated with proliferation in both normal and tumour derived breast epithelial cells.50 53 Similar to that seen with BRCA1, cells arrested in G0 or early G1 contained little BRCA2 mRNA. Once released into the proliferating phase however, BRCA2 mRNA concentrations rise, reaching a maximum in late G1 and S phases.50 53 54 In association with this, the BRCA2 protein has also been shown to be induced in late G1\/early S phase, before DNA synthesis, implying that this rise is not simply secondary to the increase in proliferation.34 This coincides with the time of maximum cellular growth and diVerentiation.50","unstructured":"BRCA2 mRNA expression has been shown to be regulated with the cell cycle and associated with proliferation in both normal and tumour derived breast epithelial cells.50 53 Similar to that seen with BRCA1, cells arrested in G0 or early G1 contained little BRCA2 mRNA. Once released into the proliferating phase however, BRCA2 mRNA concentrations rise, reaching a maximum in late G1 and S phases.50 53 54 In association with this, the BRCA2 protein has also been shown to be induced in late G1\/early S phase, before DNA synthesis, implying that this rise is not simply secondary to the increase in proliferation.34 This coincides with the time of maximum cellular growth and diVerentiation.50"}],"container-title":["Molecular Pathology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1136\/mp.51.5.237","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,8,24]],"date-time":"2025-08-24T17:52:07Z","timestamp":1756057927000},"score":1,"resource":{"primary":{"URL":"https:\/\/mp.bmj.com\/lookup\/doi\/10.1136\/mp.51.5.237"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,10]]},"references-count":2,"journal-issue":{"issue":"5","published-online":{"date-parts":[[1998,10,1]]},"published-print":{"date-parts":[[1998,10]]}},"alternative-id":["10.1136\/mp.51.5.237"],"URL":"https:\/\/doi.org\/10.1136\/mp.51.5.237","relation":{},"ISSN":["1366-8714","1472-4154"],"issn-type":[{"value":"1366-8714","type":"print"},{"value":"1472-4154","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,10]]}}}