about
Structural basis of ubiquitin recognition by the ubiquitin-associated (UBA) domain of the ubiquitin ligase EDDStructure of the HECT C-lobe of the UBR5 E3 ubiquitin ligaseEDD enhances cell survival and cisplatin resistance and is a therapeutic target for epithelial ovarian cancer.HECT E3s and human disease.Modulation of myocardin function by the ubiquitin E3 ligase UBR5.UBR5-mediated ubiquitination of ATMIN is required for ionizing radiation-induced ATM signaling and function.Regulation of DNA damage responses and cell cycle progression by hMOB2.EDD inhibits ATM-mediated phosphorylation of p53.A whole-genome RNAi screen identifies an 8q22 gene cluster that inhibits death receptor-mediated apoptosis.Human Herpesvirus-6 U14 Induces Cell-Cycle Arrest in G2/M Phase by Associating with a Cellular Protein, EDD.The MLLE domain of the ubiquitin ligase UBR5 binds to its catalytic domain to regulate substrate binding.A novel role for RIP1 kinase in mediating TNFα production.RanGTP aids anaphase entry through Ubr5-mediated protein turnover.The novel interaction between microspherule protein Msp58 and ubiquitin E3 ligase EDD regulates cell cycle progression.The E3 ubiquitin ligase EDD is an adverse prognostic factor for serous epithelial ovarian cancer and modulates cisplatin resistance in vitroAn analysis and validation pipeline for large-scale RNAi-based screens.E3 ubiquitin ligase isolated by differential display regulates cervical cancer growth in vitro and in vivo via microRNA-143.Taking the time to make important decisions: the checkpoint effector kinases Chk1 and Chk2 and the DNA damage response.Potential Urinary miRNA Biomarker Candidates for the Accurate Detection of Prostate Cancer among Benign Prostatic Hyperplasia Patients.Gene mutations and actionable genetic lesions in mantle cell lymphoma.GOLPH3 induces epithelial-mesenchymal transition via Wnt/β-catenin signaling pathway in epithelial ovarian cancerE3 ligase EDD1/UBR5 is utilized by the HPV E6 oncogene to destabilize tumor suppressor TIP60.Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B.The E3 ligase PIRH2 polyubiquitylates CHK2 and regulates its turnover.EDD, a ubiquitin-protein ligase of the N-end rule pathway, associates with spindle assembly checkpoint components and regulates the mitotic response to nocodazole.Regulation of the human papillomavirus type 18 E6/E6AP ubiquitin ligase complex by the HECT domain-containing protein EDD.The p90 ribosomal S6 kinase-UBR5 pathway controls Toll-like receptor signaling via miRNA-induced translational inhibition of tumor necrosis factor receptor-associated factor 3.MOAP-1, UBR5 and cisplatin resistance in ovarian cancer.
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
EDD mediates DNA damage-induced activation of CHK2
@ast
EDD mediates DNA damage-induced activation of CHK2
@en
EDD mediates DNA damage-induced activation of CHK2
@nl
type
label
EDD mediates DNA damage-induced activation of CHK2
@ast
EDD mediates DNA damage-induced activation of CHK2
@en
EDD mediates DNA damage-induced activation of CHK2
@nl
prefLabel
EDD mediates DNA damage-induced activation of CHK2
@ast
EDD mediates DNA damage-induced activation of CHK2
@en
EDD mediates DNA damage-induced activation of CHK2
@nl
P2093
P2860
P50
P3181
P356
P1476
EDD mediates DNA damage-induced activation of CHK2
@en
P2093
Amanda J Russell
Brandi Williams
Colin K W Watts
Jennifer L Clancy
Kum Kum Khanna
Marcia A Munoz
Michelle J Henderson
Robert L Sutherland
P2860
P304
39990-40000
P3181
P356
10.1074/JBC.M602818200
P407
P577
2006-12-29T00:00:00Z