about
Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressorThe LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activityMultifunctional transcription factor TFII-I is an activator of BRCA1 functionBRCA1 interacts with FHL2 and enhances FHL2 transactivation functionIdentification of DBC1 as a transcriptional repressor for BRCA1Roles of BRCA1 in centrosome duplicationHighlight: BRCA1 and BRCA2 proteins in breast cancerBRCA1 is a negative modulator of the PRC2 complexStructure of an XRCC1 BRCT domain: a new protein-protein interaction moduleCollaboration of signal transducer and activator of transcription 1 (STAT1) and BRCA1 in differential regulation of IFN-gamma target genesThe BRCA2 gene product functionally interacts with p53 and RAD51The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2CBP/p300 interact with and function as transcriptional coactivators of BRCA1BRCA1-associated growth arrest is RB-dependentBRCA1 is a component of the RNA polymerase II holoenzymeBRCA1 regulates p53-dependent gene expressionIncreased cell survival by inhibition of BRCA1 using an antisense approach in an estrogen responsive ovarian carcinoma cell lineCaretaker Brca1: keeping the genome in the straight and narrow.Role of BRCA gene dysfunction in breast and ovarian cancer predisposition.EMSY links breast cancer gene 2 to the 'Royal Family'A guide for functional analysis of BRCA1 variants of uncertain significanceBRCA1, a 'complex' protein involved in the maintenance of genomic stabilityStructural consequences of a cancer-causing BRCA1-BRCT missense mutationAn hGCN5/TRRAP histone acetyltransferase complex co-activates BRCA1 transactivation function through histone modificationRole of direct interaction in BRCA1 inhibition of estrogen receptor activityBRCA1 associates with processive RNA polymerase IIA novel tricomplex of BRCA1, Nmi, and c-Myc inhibits c-Myc-induced human telomerase reverse transcriptase gene (hTERT) promoter activity in breast cancerBARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear exportAdenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1c-Fos oncogene regulator Elk-1 interacts with BRCA1 splice variants BRCA1a/1b and enhances BRCA1a/1b-mediated growth suppression in breast cancer cellsEnhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 proteinIs there more to BARD1 than BRCA1?The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activityBRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transitionThe C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repressionThe second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoterNFBD1/MDC1 associates with p53 and regulates its function at the crossroad between cell survival and death in response to DNA damageBRCA1 and Oxidative StressProbing structure-function relationships in missense variants in the carboxy-terminal region of BRCA1Tumorigenesis and a DNA repair defect in mice with a truncating Brca2 mutation
P2860
Q22253893-25D245A3-3A7B-4882-A706-E5880538E273Q24292058-2B295F74-48B6-4208-928B-F9A9A92414A5Q24297413-E2CB8770-772B-4289-921E-349A08E8ECF1Q24297493-EFFB4710-7749-44F1-AB40-3F7E96BC7F9AQ24299659-37977C08-07C8-49C4-B866-88E852190D06Q24306201-5C0FAEE1-57C2-45D9-9E6C-EA0D176CD303Q24307401-F2814C63-24CD-46D2-BB24-4837467146DAQ24339430-5705D061-5D5B-4B26-8D5F-FCDDEEAFA385Q24533379-6506D592-FB9F-470E-A26D-A851477A3793Q24643507-35F4CCBB-BCF8-4874-B7E3-7A5BA1859478Q24650406-FFDA1881-43C8-4DC2-827F-03BEB8612911Q24657679-BCADADC8-296B-4B3A-9E63-B49D76B37671Q24673965-4B379931-898A-4C97-AB1B-811751693430Q24675010-4E9248FF-FA86-4EB3-82FC-89AD4193ADA7Q24675704-8D0197D0-B3EA-417A-97C5-2AD7CBD97A38Q24685083-9AEAD0B4-0117-41A1-97CC-D8F5EE0EA841Q24791221-BDCAD624-B9AB-4DB0-A3EF-8553D700A22CQ24793132-C1A12875-3C65-4FE6-89EF-B6A53BAB792BQ24800677-3204341C-EA41-4A83-B601-A33A4CC81C34Q24806435-B85089B0-4DBD-4AF7-B3F6-29A3EC7919D4Q26829268-7F2749E3-3F74-495C-B715-B0CD50D6801FQ26853262-3193883C-85A0-4A73-A562-3FBFD1AEEBCEQ27639943-C6E0287A-0AC4-486E-A30E-1AA942A04152Q28115512-55E28170-7456-4426-853D-97A0541DCFA0Q28204456-809F4D8C-5E67-4446-85B2-E79B7D8E05C6Q28204666-B34343C9-0FD4-444B-9B26-BB5E5F270191Q28210555-C38D357B-F443-4527-96E3-1F7934CBCD32Q28211710-43890BFC-4D45-42D6-BDC2-E25E2EE32052Q28212223-98916835-F867-447D-870C-FEE60325E4A0Q28213710-8BE62AAD-AD5A-475F-B2E7-BBF8C31E7850Q28214794-6177A6C1-2676-4EEB-B693-D925479196ACQ28236135-2D73088B-35AE-48F2-BFC6-7DFD3F0E7FF6Q28246541-8D21543D-904B-46C7-8FDC-9DA86CB63E5BQ28247388-99DC8B55-ABDF-47B0-AA67-A8F2BFF3BB10Q28282486-BDF82BA5-A392-4831-AD22-85D00CC0FC23Q28295923-7A3AACB2-5E41-433D-8F30-FD5E9F52B999Q28304255-745476C4-26B6-45B8-89A9-6A05C20830F7Q28388921-F54F0277-6FF6-4F52-BC28-BA3A7E9D033EQ28539000-A835625F-94C4-4F55-B7FC-1322A95537D2Q28586360-B0C7B121-7C04-4030-B102-59A3ED60AF02
P2860
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в серпні 1996
@uk
name
Transcriptional activation by BRCA1
@en
Transcriptional activation by BRCA1
@nl
type
label
Transcriptional activation by BRCA1
@en
Transcriptional activation by BRCA1
@nl
prefLabel
Transcriptional activation by BRCA1
@en
Transcriptional activation by BRCA1
@nl
P356
P1433
P1476
Transcriptional activation by BRCA1
@en
P2093
P2888
P304
P356
10.1038/382678A0
P407
P577
1996-08-01T00:00:00Z
P6179
1002606918