A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
about
Herpes simplex virus 2 ICP0 mutant viruses are avirulent and immunogenic: implications for a genital herpes vaccineThe RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERADThe epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia proteinPML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7-mediated deubiquitination of β-cateninThe USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1USP7 counteracts SCFbetaTrCP- but not APCCdh1-mediated proteolysis of ClaspinInfected cell protein 0 functional domains and their coordination in herpes simplex virus replicationThe Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme.Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selectionHSV-1 ICP0: paving the way for viral replicationA ubiquitin shuttle DC-UbP/UBTD2 reconciles protein ubiquitination and deubiquitination via linking UbE1 and USP5 enzymesCrystal Structure of USP7 Ubiquitin-like Domains with an ICP0 Peptide Reveals a Novel Mechanism Used by Viral and Cellular Proteins to Target USP7A proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection.Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies.Comparison of the biological and biochemical activities of several members of the alphaherpesvirus ICP0 family of proteins.The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies.HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate ImmunityNovel roles of cytoplasmic ICP0: proteasome-independent functions of the RING finger are required to block interferon-stimulated gene production but not to promote viral replication.Usp7 protects genomic stability by regulating Bub3.Effects of partner proteins on BCA2 RING ligase activity.E3 ubiquitin ligases in ErbB receptor quantity control.Centromere architecture breakdown induced by the viral E3 ubiquitin ligase ICP0 protein of herpes simplex virus type 1.A ubiquitin-specific protease possesses a decisive role for adenovirus replication and oncogene-mediated transformation.Identification of TRIM27 as a novel degradation target of herpes simplex virus 1 ICP0.A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virusThe checkpoints of viral gene expression in productive and latent infection: the role of the HDAC/CoREST/LSD1/REST repressor complexHerpes simplex virus immediate-early protein ICP0 is targeted by SIAH-1 for proteasomal degradation.The auto-ubiquitylation of E3 ubiquitin-protein ligase Chfr at G2 phase is required for accumulation of polo-like kinase 1 and mitotic entry in mammalian cells.Proteomic profiling of the human cytomegalovirus UL35 gene products reveals a role for UL35 in the DNA repair responseChanging the ubiquitin landscape during viral manipulation of the DNA damage response.The ubiquitin-specific protease USP7 modulates the replication of Kaposi's sarcoma-associated herpesvirus latent episomal DNAHSV ICP0 recruits USP7 to modulate TLR-mediated innate responseA quantitative assay to monitor HSV-1 ICP0 ubiquitin ligase activity in vitroOverexpression of the ubiquitin-specific protease 7 resulting from transfection or mutations in the ICP0 binding site accelerates rather than depresses herpes simplex virus 1 gene expressionThe Caenorhabditis elegans ekl (enhancer of ksr-1 lethality) genes include putative components of a germline small RNA pathwayN-terminal phosphorylation sites of herpes simplex virus 1 ICP0 differentially regulate its activities and enhance viral replication.The Epstein-Barr virus nuclear antigen-1 reprograms transcription by mimicry of high mobility group A proteinsRegulation of catalytic activities of HECT ubiquitin ligasesUbiquitin-specific protease 9X in host cells interacts with herpes simplex virus 1 ICP0.
P2860
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P2860
A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@ast
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@en
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@nl
type
label
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@ast
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@en
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@nl
prefLabel
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@ast
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@en
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@nl
P2093
P2860
P356
P1476
A RING finger ubiquitin ligase ...... iquitin-specific protease USP7
@en
P2093
Jane Parkinson
Mary Canning
Roger D Everett
P2860
P304
P356
10.1074/JBC.M402885200
P407
P577
2004-09-10T00:00:00Z