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dc.contributor.authorCantor, Sharon B.
dc.contributor.authorBell, Daphne W.
dc.contributor.authorGanesan, Shridar
dc.contributor.authorKass, Elizabeth M.
dc.contributor.authorDrapkin, Ronny
dc.contributor.authorGrossman, Steven R.
dc.contributor.authorWahrer, Doke C. R.
dc.contributor.authorSgroi, Dennis C.
dc.contributor.authorLane, William S.
dc.contributor.authorHaber, Daniel A.
dc.contributor.authorLivingston, David M.
dc.date2022-08-11T08:08:02.000
dc.date.accessioned2022-08-23T15:40:01Z
dc.date.available2022-08-23T15:40:01Z
dc.date.issued2001-04-13
dc.date.submitted2008-12-10
dc.identifier.citationCell. 2001 Apr 6;105(1):149-60.
dc.identifier.issn0092-8674 (Print)
dc.identifier.pmid11301010
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26307
dc.description.abstractBRCA1 interacts in vivo with a novel protein, BACH1, a member of the DEAH helicase family. BACH1 binds directly to the BRCT repeats of BRCA1. A BACH1 derivative, bearing a mutation in a residue that was essential for catalytic function in other helicases, interfered with normal double-strand break repair in a manner that was dependent on its BRCA1 binding function. Thus, BACH1/BRCA1 complex formation contributes to a key BRCA1 activity. In addition, germline BACH1 mutations affecting the helicase domain were detected in two early-onset breast cancer patients and not in 200 matched controls. Thus, it is conceivable that, like BRCA1, BACH1 is a target of germline cancer-inducing mutations.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=11301010&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/S0092-8674(01)00304-X
dc.subjectAdult
dc.subjectAmino Acid Motifs
dc.subjectBRCA1 Protein
dc.subjectBinding Sites
dc.subjectBoston
dc.subjectBreast Neoplasms
dc.subjectCell Line
dc.subjectChromosomes, Human, Pair 17
dc.subjectDNA Helicases
dc.subjectDNA Repair
dc.subject*DNA-Binding Proteins
dc.subjectFemale
dc.subjectGenetic Predisposition to Disease
dc.subjectGenetic Screening
dc.subjectHumans
dc.subjectMolecular Sequence Data
dc.subjectMutagenesis, Site-Directed
dc.subjectProtein Binding
dc.subjectProtein Structure, Tertiary
dc.subjectRNA Helicases
dc.subjectRecombinant Fusion Proteins
dc.subjectSequence Homology, Amino Acid
dc.subjectSpectrometry, Mass, Electrospray Ionization
dc.subjectTransfection
dc.subjectCancer Biology
dc.subjectNeoplasms
dc.titleBACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function
dc.typeJournal Article
dc.source.journaltitleCell
dc.source.volume105
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cancerbiology_pp/6
dc.identifier.contextkey679284
html.description.abstract<p>BRCA1 interacts in vivo with a novel protein, BACH1, a member of the DEAH helicase family. BACH1 binds directly to the BRCT repeats of BRCA1. A BACH1 derivative, bearing a mutation in a residue that was essential for catalytic function in other helicases, interfered with normal double-strand break repair in a manner that was dependent on its BRCA1 binding function. Thus, BACH1/BRCA1 complex formation contributes to a key BRCA1 activity. In addition, germline BACH1 mutations affecting the helicase domain were detected in two early-onset breast cancer patients and not in 200 matched controls. Thus, it is conceivable that, like BRCA1, BACH1 is a target of germline cancer-inducing mutations.</p>
dc.identifier.submissionpathcancerbiology_pp/6
dc.contributor.departmentDepartment of Medicine, Division of Hematology/Oncology
dc.contributor.departmentDepartment of Cancer Biology
dc.source.pages149-60


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