Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein - Wikidata - awgldk - TriplyDB

Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein

Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein

http://www.wikidata.org/entity/Q28214794

about

sameAs

Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling BRCA1 and FOXA1 proteins coregulate the expression of the cell cycle-dependent kinase inhibitor p27(Kip1)The SWI/SNF protein BAF60b is ubiquitinated through a signalling process involving Rac GTPase and the RING finger protein Unkempt BRCA1/BARD1 inhibition of mRNA 3' processing involves targeted degradation of RNA polymerase II.The UBXN1 protein associates with autoubiquitinated forms of the BRCA1 tumor suppressor and inhibits its enzymatic function The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin CCDC98 targets BRCA1 to DNA damage sites Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex Degradation of transcription repressor ZBRK1 through the ubiquitin-proteasome pathway relieves repression of Gadd45a upon DNA damage Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex Targeting New Candidate Genes by Small Molecules Approaching Neurodegenerative Diseases RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis The yeast Slx5-Slx8 DNA integrity complex displays ubiquitin ligase activity.Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase Tumor suppressor BRCA1 epigenetically controls oncogenic microRNA-155 BRCA1 targets G2/M cell cycle proteins for ubiquitination and proteasomal degradation BARD1 participates with BRCA1 in homology-directed repair of chromosome breaks MDM2 and MDMX: Alone and together in regulation of p53 Substitution of aspartic acid with glutamic acid at position 67 of the BRCA1 RING domain retains ubiquitin ligase activity and zinc(II) binding with a reduced transition temperature.Assessment of human Nter and Cter BRCA1 mutations using growth and localization assays in yeast.Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility.Rapid recruitment of BRCA1 to DNA double-strand breaks is dependent on its association with Ku80 The ubiquitin system, disease, and drug discovery.USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism.The negative interplay between Aurora A/B and BRCA1/2 controls cancer cell growth and tumorigenesis via distinct regulation of cell cycle progression, cytokinesis, and tetraploidy Identification of Saccharomyces cerevisiae spindle pole body remodeling factors DNA double-strand break repair genes and oxidative damage in brain metastasis of breast cancer.Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding.Centrosomal microtubule nucleation activity is inhibited by BRCA1-dependent ubiquitination Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance Zinc and human health: an update.DNA double-strand break signaling and human disorders.Connection between Tumor Suppressor BRCA1 and PTEN in Damaged DNA Repair BRCA1, PARP, and 53BP1: conditional synthetic lethality and synthetic viability.BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP Characterization of an Italian founder mutation in the RING-finger domain of BRCA1.The BRCA1 variant p.Ser36Tyr abrogates BRCA1 protein function and potentially confers a moderate risk of breast cancer.MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.In Vitro Enhanced Sensitivity to Cisplatin in D67Y BRCA1 RING Domain Protein.Identification and characterization of missense alterations in the BRCA1 associated RING domain (BARD1) gene in breast and ovarian cancer

P2860

Q21144354-16338C4B-3E50-4240-A261-4B9D8DF50910 Q24298165-0D775338-CA89-4B9E-9251-D182959CFEB2 Q24299062-181D2EFB-86EF-4DD2-9090-055FE24A2373 Q24302667-53A218AF-D09E-4F70-90A7-C1DD968C527B Q24305086-7DA8CBE7-EDAF-4BAA-B6C6-EC01C876325D Q24312959-6DF64746-C94C-4A80-B1A6-B2AE7D981444 Q24321418-430BD37F-AC30-4F3E-98C2-471835334795 Q24337578-9FDE0D23-53C6-4FE1-8BE8-F9E4E87686EF Q24653338-8608D05C-4193-4A9F-8A3E-04B15D9AA207 Q24675257-EC93F25E-199B-4CB5-B3BD-96AF67B8C3E1 Q26771812-DF85D746-EB0C-4313-A5AC-F4B4E0FA9654 Q26853207-3983FB28-1B57-4222-ADA6-EF95BF5D395B Q27940090-2FF0A2FA-2BC6-4441-9E05-5810739F46B0 Q28187365-C207875D-0C3A-4B49-9CE2-91C7473AEE9E Q28249114-7AA173CD-67D9-4E89-A695-DE0219F7FE40 Q28389685-0FD6BCD9-9B2B-45FB-955E-221781CCC930 Q28609933-EB1AEFF8-A844-4C0E-AC15-52D5576692BD Q28611422-D12B988D-C8F8-4CF4-9A1A-F342478B745C Q30395158-77DD682F-0AD3-4D60-8345-F4F9B8AD0F12 Q30407141-59D4039F-79D3-412A-88EC-3E5549F5CEF1 Q33231274-7FC39231-77D4-4C35-B208-A2CAEFA4C2FE Q33378036-CAF0DD88-02BB-4036-8B7B-EA555A78A358 Q33384295-CEAB6BFC-F2EC-4A6B-8010-77B1DB3A5BE6 Q33602611-AB1F510E-96D8-4B49-BA7A-3C6527D0E3C5 Q33637754-4A4F927A-44B0-4CAA-A8E8-8240B12CA621 Q33754397-3EB34698-3798-4FA7-9269-A96B5A4F0BAC Q33815545-F7C7A043-FEAF-44FB-89EC-9BF1BCDB0520 Q33885155-AAC1B439-795C-49B0-AF55-8F9BC0F4E465 Q34097098-409BD84D-6A00-422F-B49F-BFE2C19C4F4E Q34132152-90E90B81-0BE5-444F-BA4D-CA95B8F3E657 Q34231267-41521C0B-5C66-4ECC-B957-F672C145C0E1 Q34360500-0F28E5F6-854E-4B01-ABE6-582E3EC117C5 Q34481443-49B133FC-CD0C-442D-A928-1DDCF0417AA4 Q34539782-22C398CF-89D3-4744-BC8C-62950F197853 Q34863348-7F827A2F-2675-4F9C-90EF-078BEB351C66 Q35091400-D617AB33-1EC4-41A1-B6EF-9D78602A4CC4 Q35138569-DDA5005A-4002-4FF3-9E46-7BFC4E3EF0AE Q35245786-C0178BB3-7047-4A97-8C10-0A497E81E2AC Q35440379-1D1CE26E-F258-46E5-B3F4-E989FE63E1E6 Q35448920-8494D44E-5AD7-44F7-98DC-BBD195E04CAC

P2860

Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein

http://www.wikidata.org/entity/Q28214794

description

2003 nî lūn-bûn

@nan

2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@ast

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@en

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@nl

type

label

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@ast

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@en

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@nl

prefLabel

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@ast

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@en

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@nl

P1433

Q28214794-2E8D2525-E5FA-4954-B14E-579D5272FAF8

P1476

Q28214794-2F37806E-B1C3-4A39-9688-467DCBC2F120

P2093

Q28214794-51A21502-B2B0-4728-B21F-8D3755756E44

Q28214794-5A77C04F-9E4E-4141-88A7-ED9DE1857FD3

Q28214794-91C3E934-B341-4D9E-A257-844DF8134071

Q28214794-A3836E0E-DC71-4B72-BCDF-F0DABD2D6A27

Q28214794-A9FB1FB0-E78E-4795-86FB-A782B91AB415

P2860

Q28214794-0084C83A-6E3D-4642-86F0-917D1E7BF0FF

Q28214794-018EB6A8-E149-4F7D-94C6-DD7CE0525CB5

Q28214794-01F3C8F5-1FA9-47EC-9C1F-861326782811

Q28214794-0855379B-A4FB-450E-9F90-03CA84BFA659

Q28214794-0A08A615-9265-41CB-B136-9349D509D319

Q28214794-118684FC-DDC4-4BC4-8C93-7085E912DFA5

Q28214794-120F1D45-F9DF-43EE-AB79-B08585BCFE53

Q28214794-15E8F08C-274C-490D-91AD-7836F75C3CDF

Q28214794-1AC60957-F575-477C-9F8B-72D56519CE6D

Q28214794-22141188-AAD0-4B5F-B469-57AC356C465F

P304

Q28214794-D053655C-AC08-4880-AC9C-21735E8A26D5

P31

Q28214794-53DF00A9-F286-4769-8BB3-76A29447F122

P356

Q28214794-C0F316EB-D560-4BCD-9EEA-75B3195A7571

P407

Q28214794-C6F687AC-979B-43E8-BC4F-EF20E860C834

P433

Q28214794-F1950204-2B30-4694-826E-AF68AACAF7C1

P478

Q28214794-55372C6E-A06B-4E32-8EE8-396AFFBE714F

P577

Q28214794-EA90227E-51B7-4F39-A07E-B0BD8BEC163C

P5875

Q28214794-8DD4E68C-14ED-40C2-B6D5-EE2D2C9D45D3

P698

Q28214794-B2E78576-33C6-4C59-9AD5-3DCF0DECC98D

P356

P1433

Journal of Biological Chemistry

P1476

Enhancement of BRCA1 E3 ubiqui ...... raction with the BARD1 protein

@en

P2093

Gerald M Pao

http://www.w3.org/2001/XMLSchema#string

Hong-Wu Chen

http://www.w3.org/2001/XMLSchema#string

Inder M Verma

http://www.w3.org/2001/XMLSchema#string

Tony Hunter

http://www.w3.org/2001/XMLSchema#string

Yan Xia

http://www.w3.org/2001/XMLSchema#string

P2860

Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair

Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein

Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor

BRCA1 is associated with a human SWI/SNF-related complex: linking chromatin remodeling to breast cancer

Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13

BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations.

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

Roles of BRCA1 in centrosome duplication

P304

5255-63

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M204591200

http://www.w3.org/2001/XMLSchema#string

P407

P433

7

http://www.w3.org/2001/XMLSchema#string

P478

278

http://www.w3.org/2001/XMLSchema#string

P577

2003-02-14T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11035395

http://www.w3.org/2001/XMLSchema#string

P698

12431996

http://www.w3.org/2001/XMLSchema#string