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Journal Abstract Search
177 related items for PubMed ID: 9798686
1. Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein. Ayi TC, Tsan JT, Hwang LY, Bowcock AM, Baer R. Oncogene; 1998 Oct 22; 17(16):2143-8. PubMed ID: 9798686 [Abstract] [Full Text] [Related]
2. Identification of a RING protein that can interact in vivo with the BRCA1 gene product. Wu LC, Wang ZW, Tsan JT, Spillman MA, Phung A, Xu XL, Yang MC, Hwang LY, Bowcock AM, Baer R. Nat Genet; 1996 Dec 22; 14(4):430-40. PubMed ID: 8944023 [Abstract] [Full Text] [Related]
3. Nuclear-cytoplasmic shuttling of BARD1 contributes to its proapoptotic activity and is regulated by dimerization with BRCA1. Rodriguez JA, Schüchner S, Au WW, Fabbro M, Henderson BR. Oncogene; 2004 Mar 11; 23(10):1809-20. PubMed ID: 14647430 [Abstract] [Full Text] [Related]
4. BRCA1-dependent and independent functions of BARD1. Irminger-Finger I, Leung WC. Int J Biochem Cell Biol; 2002 Jun 11; 34(6):582-7. PubMed ID: 11943588 [Abstract] [Full Text] [Related]
5. Structure of a BRCA1-BARD1 heterodimeric RING-RING complex. Brzovic PS, Rajagopal P, Hoyt DW, King MC, Klevit RE. Nat Struct Biol; 2001 Oct 11; 8(10):833-7. PubMed ID: 11573085 [Abstract] [Full Text] [Related]
6. Structural requirements for the BARD1 tumor suppressor in chromosomal stability and homology-directed DNA repair. Laufer M, Nandula SV, Modi AP, Wang S, Jasin M, Murty VV, Ludwig T, Baer R. J Biol Chem; 2007 Nov 23; 282(47):34325-33. PubMed ID: 17848578 [Abstract] [Full Text] [Related]
8. Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1. Meza JE, Brzovic PS, King MC, Klevit RE. J Biol Chem; 1999 Feb 26; 274(9):5659-65. PubMed ID: 10026184 [Abstract] [Full Text] [Related]
11. BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity. Nishikawa H, Wu W, Koike A, Kojima R, Gomi H, Fukuda M, Ohta T. Cancer Res; 2009 Jan 01; 69(1):111-9. PubMed ID: 19117993 [Abstract] [Full Text] [Related]
14. The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T. J Biol Chem; 2001 May 04; 276(18):14537-40. PubMed ID: 11278247 [Abstract] [Full Text] [Related]
15. BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export. Fabbro M, Rodriguez JA, Baer R, Henderson BR. J Biol Chem; 2002 Jun 14; 277(24):21315-24. PubMed ID: 11925436 [Abstract] [Full Text] [Related]
16. Nuclear-cytoplasmic translocation of BARD1 is linked to its apoptotic activity. Jefford CE, Feki A, Harb J, Krause KH, Irminger-Finger I. Oncogene; 2004 Apr 29; 23(20):3509-20. PubMed ID: 15077185 [Abstract] [Full Text] [Related]
19. Interaction of BARD1 and HP1 Is Required for BRCA1 Retention at Sites of DNA Damage. Wu W, Nishikawa H, Fukuda T, Vittal V, Asano M, Miyoshi Y, Klevit RE, Ohta T. Cancer Res; 2015 Apr 01; 75(7):1311-21. PubMed ID: 25634209 [Abstract] [Full Text] [Related]
20. Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase. Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE, Fukuda M, Ohta T. J Biol Chem; 2004 Feb 06; 279(6):3916-24. PubMed ID: 14638690 [Abstract] [Full Text] [Related] Page: [Next] [New Search]