about
Identification of phosphorylation sites on transcription factor Sp1 in response to DNA damage and its accumulation at damaged sites.Homologous recombinational repair factors are recruited and loaded onto the viral DNA genome in Epstein-Barr virus replication compartments.Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.Noise cancellation: viral fine tuning of the cellular environment for its own genome replication.The late promoter of the human cytomegalovirus viral DNA polymerase processivity factor has an impact on delayed early and late viral gene products but not on viral DNA synthesisEnhanced phosphorylation of transcription factor sp1 in response to herpes simplex virus type 1 infection is dependent on the ataxia telangiectasia-mutated proteinInduction of Epstein-Barr Virus Oncoprotein LMP1 by Transcription Factors AP-2 and Early B Cell FactorEpstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein.Modes of infection and oncogenesis by the Epstein-Barr virus.Elimination of LMP1-expressing cells from a monolayer of gastric cancer AGS cellsTofacitinib induces G1 cell-cycle arrest and inhibits tumor growth in Epstein-Barr virus-associated T and natural killer cell lymphoma cellsAnti-CCR4 monoclonal antibody mogamulizumab for the treatment of EBV-associated T- and NK-cell lymphoproliferative diseases.Role of latent membrane protein 1 in chronic active Epstein-Barr virus infection-derived T/NK-cell proliferation.Efficient production of infectious viruses requires enzymatic activity of Epstein-Barr virus protein kinase.Expression of Epstein-Barr virus BZLF1 immediate-early protein induces p53 degradation independent of MDM2, leading to repression of p53-mediated transcription.Identification of cis-acting regions that contribute to neuron-specific expression of the GAP-43 gene.The C-Terminus of Epstein-Barr Virus BRRF2 Is Required for its Proper Localization and Efficient Virus Production.The Epstein-Barr Virus BDLF4 Gene Is Required for Efficient Expression of Viral Late Lytic Genes.Phosphorylation of p27Kip1 by Epstein-Barr virus protein kinase induces its degradation through SCFSkp2 ubiquitin ligase actions during viral lytic replication.BGLF2 Increases Infectivity of Epstein-Barr Virus by Activating AP-1 upon De Novo Infection.Mitochondrial defect drives non-autonomous tumour progression through Hippo signalling in Drosophila.Transient increases in p53-responsible gene expression at early stages of Epstein-Barr virus productive replication.Regulation of Epstein-Barr Virus Life Cycle and Cell Proliferation by Histone H3K27 Methyltransferase EZH2 in Akata CellsInitial Characterization of the Epstein⁻Barr Virus BSRF1 Gene ProductDefective Epstein-Barr virus in chronic active infection and haematological malignancyS-Like-Phase Cyclin-Dependent Kinases Stabilize the Epstein-Barr Virus BDLF4 Protein To Temporally Control Late Gene TranscriptionPublisher Correction: Defective Epstein-Barr virus in chronic active infection and haematological malignancyAntitumor activity of cyclin-dependent kinase inhibitor alsterpaullone in Epstein-Barr virus-associated lymphoproliferative disordersOncogenesis of CAEBV revealed: Intragenic deletions in the viral genome and leaky expression of lytic genesThe BOLF1 gene is necessary for effective Epstein-Barr viral infectivityEpstein-Barr Virus BBRF2 Is Required for Maximum InfectivityOncolytic activity of HF10 in head and neck squamous cell carcinomas
P50
Q33350921-51CD6B90-5C13-4F6A-B040-68403EF93764Q33433812-E5ABC1A7-1C21-44D8-AD78-6A9CA065140AQ33489621-3A104AE8-EF7C-4A6B-B506-67E98FDDA220Q33780955-7A86D09B-A8BC-4672-83F7-569012AFAB46Q35857242-A6B3A85E-31E0-448C-B706-E1C194CDD6A3Q36098859-04F82853-18E5-43DF-875B-11A3076642ADQ36736410-EA1E349B-AC37-4268-9F20-5271F1AE7FB0Q37372076-AE2775EC-6DC4-432C-A12A-BD734B7D2D76Q38191876-E1C919B6-AD6F-4F34-BD7B-88365B20E7CAQ38705672-1EF0955F-8F1B-47AB-8AFA-474E3E048AD4Q38741546-DB180491-5FD0-445B-9FF2-05D994F76CE4Q38966715-5B64A96C-25D5-4DFB-8262-BB938CB9BD15Q38998165-4D3EC790-2272-4690-A175-B410FBE8326BQ39854651-F3F6D75F-49AA-4118-A15A-60E76F8583BCQ39859670-7603F430-4B78-4344-B8EF-5FDEA47CD4CDQ40263511-AD3F5523-A4D0-41F3-A2D1-532F6FFD6450Q40333251-4AAD6974-78D1-4219-B220-A3A4C4C29292Q41094782-4AA7BB9E-59E2-4376-B854-CB396179B2EEQ43099184-E1992FD8-F80D-426A-A642-A8C381F2ADBEQ52716630-C699E818-FDAC-4CFD-A4BC-70F7A3FBFAB1Q52744366-D8FA0609-F246-4335-B5A0-86B25AD2A883Q53343352-C97D7352-FEA2-4B36-AFB4-A07E1F1A52DEQ59349700-AA4FF40E-4397-4BB1-A08F-FDA6F4C83AADQ64068330-E462024D-2DB5-4D77-A766-73C31A626C58Q91142437-33FB2996-EA19-407A-B5E5-8622D1BAA18CQ91283191-B85DCAD3-F92E-4274-85EC-4FBA94CA120BQ91297763-A572F311-013B-4DF3-9E21-FCB0CFAB2874Q91339392-9C3E19AF-C349-49F2-952E-E72A39AA5671Q92036259-A3844502-0BFD-4F59-999C-D0DA85A87E42Q92270405-5C72CF46-C56E-4F26-8234-489B2FAD86F9Q92328499-634706C3-A376-4B59-BD9C-366BA95CC3EEQ93064425-78F5A5A4-6879-405D-99D8-CA9AFA3AD58C
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Yoshitaka Sato
@ast
Yoshitaka Sato
@en
Yoshitaka Sato
@es
Yoshitaka Sato
@nl
Yoshitaka Sato
@sl
type
label
Yoshitaka Sato
@ast
Yoshitaka Sato
@en
Yoshitaka Sato
@es
Yoshitaka Sato
@nl
Yoshitaka Sato
@sl
prefLabel
Yoshitaka Sato
@ast
Yoshitaka Sato
@en
Yoshitaka Sato
@es
Yoshitaka Sato
@nl
Yoshitaka Sato
@sl
P1053
P-9728-2015
P106
P21
P2798
P31
P3829
P496
0000-0002-8541-6413
P569
2000-01-01T00:00:00Z