SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.
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Analysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infectionHuman Oncogenic Herpesvirus and Post-translational Modifications - Phosphorylation and SUMOylationFunctional protein microarray as molecular decathlete: a versatile player in clinical proteomicsComputational discovery of Epstein-Barr virus targeted human genes and signalling pathways.The EBNA3 family of Epstein-Barr virus nuclear proteins associates with the USP46/USP12 deubiquitination complexes to regulate lymphoblastoid cell line growthPhosphoproteomic Profiling Reveals Epstein-Barr Virus Protein Kinase Integration of DNA Damage Response and Mitotic SignalingViral manipulation of the cellular sumoylation machinery.A locus encompassing the Epstein-Barr virus bglf4 kinase regulates expression of genes encoding viral structural proteinsSUMO and KSHV ReplicationBGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteinsEpstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.The Epstein-Barr virus miR-BHRF1-1 targets RNF4 during productive infection to promote the accumulation of SUMO conjugates and the release of infectious virusThe cellular ataxia telangiectasia-mutated kinase promotes epstein-barr virus lytic reactivation in response to multiple different types of lytic reactivation-inducing stimuliHsp90 inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cellsInteractome mapping: using protein microarray technology to reconstruct diverse protein networks.Potential of protein kinase inhibitors for treating herpesvirus-associated disease.Viral manipulation of cellular protein conjugation pathways: The SUMO lesson.Understanding Epstein-Barr Virus Life Cycle with Proteomics: A Temporal Analysis of Ubiquitination During Virus Reactivation.Manipulation of ubiquitin/SUMO pathways in human herpesviruses infection.Interindividual Spread of Herpesviruses.EBV-related lymphomas: new approaches to treatment.Viral Interplay with the Host Sumoylation System.Characterization of the subcellular localization of Epstein-Barr virus encoded proteins in live cells.B Cell Receptor Activation and Chemical Induction Trigger Caspase-Mediated Cleavage of PIAS1 to Facilitate Epstein-Barr Virus Reactivation.A novel approach to the analysis of SUMOylation with the independent use of trypsin and elastase digestion followed by database searching utilising consecutive residue addition to lysine.
P2860
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P2860
SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
SUMO binding by the Epstein-Ba ...... is crucial for BGLF4 function.
@en
type
label
SUMO binding by the Epstein-Ba ...... is crucial for BGLF4 function.
@en
prefLabel
SUMO binding by the Epstein-Ba ...... is crucial for BGLF4 function.
@en
P2093
P2860
P356
P1433
P1476
SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function
@en
P2093
Catherine M Guzzo
Gangling Liao
Leyao Wang
S Diane Hayward
P2860
P304
P356
10.1128/JVI.00314-12
P407
P577
2012-03-07T00:00:00Z