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BRCA1 is a component of the RNA polymerase II holoenzyme

BRCA1 is a component of the RNA polymerase II holoenzyme

http://www.wikidata.org/entity/Q24675704

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The human homologue of Drosophila TRF-proximal protein is associated with an RNA polymerase II-SRB complex Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1 Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations.The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activity Interaction between BRCA2 and replication protein A is compromised by a cancer-predisposing mutation in BRCA2 BRCA1 interacts with FHL2 and enhances FHL2 transactivation function Identification of DBC1 as a transcriptional repressor for BRCA1 BRCA1/BARD1 inhibition of mRNA 3' processing involves targeted degradation of RNA polymerase II.PTIP, a novel BRCT domain-containing protein interacts with Pax2 and is associated with active chromatin.A human RNA polymerase II complex containing factors that modify chromatin structure An RNA polymerase II complex containing all essential initiation factors binds to the activation domain of PAR leucine zipper transcription factor thyroid embryonic factor.Structure of an XRCC1 BRCT domain: a new protein-protein interaction module Association of herpes simplex virus type 1 ICP8 and ICP27 proteins with cellular RNA polymerase II holoenzyme Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains Regulation of RelA (p65) function by the large subunit of replication factor C MCM proteins are associated with RNA polymerase II holoenzyme BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures Direct DNA binding by Brca1 Collaboration of signal transducer and activator of transcription 1 (STAT1) and BRCA1 in differential regulation of IFN-gamma target genes BRCA1 inhibition of telomerase activity in cultured cells CBP/p300 interact with and function as transcriptional coactivators of BRCA1 JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction BRCA1 regulates p53-dependent gene expression Increased cell survival by inhibition of BRCA1 using an antisense approach in an estrogen responsive ovarian carcinoma cell line Use of adenoviral E1A protein to analyze K18 promoter deregulation in colon carcinoma cells discloses a role for CtBP1 and BRCA1.BRCA1 Zinc RING Finger Domain Disruption Alters Caspase Response in Ovarian Surface Epithelial Cells.Role of BRCA gene dysfunction in breast and ovarian cancer predisposition.CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus Roles of BRCA1 and BRCA2 in homologous recombination, DNA replication fidelity and the cellular response to ionizing radiation BRCA1 associates with processive RNA polymerase II Distinct parts of minichromosome maintenance protein 2 associate with histone H3/H4 and RNA polymerase II holoenzyme BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1 Redistribution of BRCA1 among four different protein complexes following replication blockage c-Fos oncogene regulator Elk-1 interacts with BRCA1 splice variants BRCA1a/1b and enhances BRCA1a/1b-mediated growth suppression in breast cancer cells Is there more to BARD1 than BRCA1?The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression

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BRCA1 is a component of the RNA polymerase II holoenzyme

http://www.wikidata.org/entity/Q24675704

description

1997 nî lūn-bûn

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1997 թուականի Մայիսին հրատարակուած գիտական յօդուած

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1997 թվականի մայիսին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

BRCA1 is a component of the RNA polymerase II holoenzyme

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BRCA1 is a component of the RNA polymerase II holoenzyme

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BRCA1 is a component of the RNA polymerase II holoenzyme

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type

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BRCA1 is a component of the RNA polymerase II holoenzyme

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BRCA1 is a component of the RNA polymerase II holoenzyme

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BRCA1 is a component of the RNA polymerase II holoenzyme

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prefLabel

BRCA1 is a component of the RNA polymerase II holoenzyme

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BRCA1 is a component of the RNA polymerase II holoenzyme

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BRCA1 is a component of the RNA polymerase II holoenzyme

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PNAS.94.11.5605

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Proceedings of the National Academy of Sciences of the United States of America

P1476

BRCA1 is a component of the RNA polymerase II holoenzyme

@en

P2093

D M Chao

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

D M Livingston

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J D Parvin

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L Ye

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R A Young

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R Scully

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S F Anderson

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W Wei

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P2860

Identification of human cyclin-dependent kinase 8, a putative protein kinase partner for cyclin C

A mammalian SRB protein associated with an RNA polymerase II holoenzyme

General requirement for RNA polymerase II holoenzymes in vivo

CREB-binding protein/p300 are transcriptional coactivators of p65

A kinase-cyclin pair in the RNA polymerase II holoenzyme.

A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II.

A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1

A human RNA polymerase II complex associated with SRB and DNA-repair proteins

Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase II

Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha

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5605-10

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11

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94

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9159119

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