about
The chemotherapeutic drug 5-fluorouracil promotes PKR-mediated apoptosis in a p53-independent manner in colon and breast cancer cellsActivation of NF-kB pathway by virus infection requires Rb expression.Kaposi's sarcoma-associated herpesvirus LANA2 is a B-cell-specific latent viral protein that inhibits p53Experimental evolution of an oncolytic vesicular stomatitis virus with increased selectivity for p53-deficient cells.Rotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.Role of monoubiquitylation on the control of IκBα degradation and NF-κB activitySIRT1 stabilizes PML promoting its sumoylationA unified nomenclature and amino acid numbering for human PTEN.Transcriptional regulation of Sox2 by the retinoblastoma family of pocket proteins.Control of virus infection by tumour suppressors.Regulation of Ebola virus VP40 matrix protein by SUMO.Cell senescence is an antiviral defense mechanismAntiviral activity of resveratrol.The impact of PKR activation: from neurodegeneration to cancer.Full activation of RNaseL in animal cells requires binding of 2-5A within ankyrin repeats 6 to 9 of this interferon-inducible enzyme.Dual Role of p53 in Innate Antiviral Immunity.KSHV latent protein LANA2 inhibits sumo2 modification of p53.SUMOylation regulates AKT1 activity.Kaposi's sarcoma-associated herpesvirus lana2 protein interacts with the pocket proteins and inhibits their sumoylation.Covalent modification by SUMO is required for efficient disruption of PML oncogenic domains by Kaposi's sarcoma-associated herpesvirus latent protein LANA2.Kaposi's sarcoma-associated herpesvirus protein LANA2 disrupts PML oncogenic domains and inhibits PML-mediated transcriptional repression of the survivin geneAnalysis of SUMOylated proteins using SUMO-trapsInduction of paclitaxel resistance by the Kaposi's sarcoma-associated herpesvirus latent protein LANA2.Latent protein LANA2 from Kaposi's sarcoma-associated herpesvirus interacts with 14-3-3 proteins and inhibits FOXO3a transcription factor.The latency protein LANA2 from Kaposi's sarcoma-associated herpesvirus inhibits apoptosis induced by dsRNA-activated protein kinase but not RNase L activation.African swine fever virus gene A179L, a viral homologue of bcl-2, protects cells from programmed cell death.BCR-ABL-expressing cells transduced with the HSV-tk gene die by apoptosis upon treatment with ganciclovir.BCR-ABL and interleukin 3 promote haematopoietic cell proliferation and survival through modulation of cyclin D2 and p27Kip1 expression.Vaccinia virus E3L protein is an inhibitor of the interferon (i.f.n.)-induced 2-5A synthetase enzyme.Activation of the IFN-inducible enzyme RNase L causes apoptosis of animal cells.Inducible expression of the 2-5A synthetase/RNase L system results in inhibition of vaccinia virus replication.Conjugation of SUMO to p85 leads to a novel mechanism of PI3K regulation.Characterization of the bipartite nuclear localization signal of protein LANA2 from Kaposi's sarcoma-associated herpesvirusActivation of the double-stranded RNA-dependent protein kinase PKR by small ubiquitin-like modifier (SUMO).Phosphorylable tyrosine residue 162 in the double-stranded RNA-dependent kinase PKR modulates its interaction with SUMOIdentification of functional domains of the interferon-induced enzyme PKR in cells lacking endogenous PKR.The sequential activation of the yeast HOG and SLT2 pathways is required for cell survival to cell wall stress.Identification of a nuclear export signal in the KSHV latent protein LANA2 mediating its export from the nucleus.Resistance to viral infection of super p53 mice.Analysis of PTEN ubiquitylation and SUMOylation using molecular traps.
P50
Q28476682-796733E1-A423-45A1-9135-A2F8E1C2BA97Q33489563-4D7CEEBC-691A-41BD-9D90-6EAC3BEF8A10Q33834993-70183F1C-C2F8-44CC-8138-DC627C5C01C4Q33882758-CD460FBF-A33A-4FF0-957F-1FD01755C203Q34034204-E1CB2DE4-C136-4CB7-8789-AC7F0FCCF7C5Q34055565-6E761597-EF6E-4387-AE5F-8D73BD44C58EQ35092583-635DE4F7-A5D1-4036-8068-EB1669C6485DQ35201003-FF93F6A6-AA96-4958-B3C3-9B2BE09F81CDQ35550151-FCD8D1E3-9C5A-41E2-9907-D282471847B9Q36755131-D2B7FCC4-D0C7-4346-9AB3-0B9D7995F370Q37416624-23228277-E065-4BDB-9591-BC6FD559E1CCQ37416859-DEF3E1CD-726B-42C3-900C-28622EC0E22AQ37674667-6C281AEC-2D93-49C8-BBBE-F93715E22000Q38187546-33C20FE3-4B4E-4C8B-A44F-878FBAD4274CQ38326821-0DBB34E2-DB8C-4FA9-BCCB-E27ADAE268F7Q38613932-E375FB81-8759-4697-9401-FB8CC87B3A8CQ38917974-CE0574DD-4CC9-451F-9EC2-E8F947E4028DQ39007397-462B27A0-DAF8-47D7-97CA-411DF8A04D62Q39210824-202EE148-1A81-4A73-A80B-C0435C259D25Q39649881-9F20A4E4-9123-4646-970B-EBA31FAFF517Q39833667-B212CFAF-A028-4095-AEA8-2E7D47B21EACQ39979661-9BAC2C2A-9633-47DA-9907-B743F13276BCQ40046426-373B8C76-B47E-4944-82F7-2979D9DFA7A8Q40208122-20C4F3F4-704D-4CB1-9024-594759C41C33Q40644374-974AC36A-44A9-40B9-86CF-48028B0379C1Q40662022-A9814DCC-048E-4169-9241-85CDFEF58C28Q40805820-CAF6727A-157B-4B66-B5B8-730217E0B1DBQ40809849-BD424CA7-5DBF-428D-8426-60622EE19562Q41047354-6EA6971E-6858-417D-B4A1-D65D8AF05E82Q41084720-15B6E451-6B86-4DB8-9F0D-216CC13805B9Q41135027-1194EE1B-998D-41E3-9A84-5368AE6F5888Q41303929-F1CB3778-2BBF-4AEF-858E-44574FDF6E30Q42121696-75082517-4977-4D6A-B7CA-5623C243D7C4Q42203018-7F6C8880-2DE4-4AD6-877A-1D473D58C0E6Q42630066-01120135-E916-4B92-AAF2-297A7B277C51Q42808302-8578453B-A360-4466-9B10-3931C1394929Q43069140-10357C2B-7D61-4DEB-8D02-DFE005956DC8Q44403106-71D72396-8124-4D5A-98E9-41FFC8DB428FQ45152311-CA61F6EF-D6F5-432B-B57A-08F7E13710FAQ45345903-0C388FEE-5DDD-4C02-B659-7CA7D20663FE
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Carmen Rivas
@ast
Carmen Rivas
@en
Carmen Rivas
@es
Carmen Rivas
@nl
Carmen Rivas
@sl
type
label
Carmen Rivas
@ast
Carmen Rivas
@en
Carmen Rivas
@es
Carmen Rivas
@nl
Carmen Rivas
@sl
prefLabel
Carmen Rivas
@ast
Carmen Rivas
@en
Carmen Rivas
@es
Carmen Rivas
@nl
Carmen Rivas
@sl
P108
P1053
L-3162-2017
P106
P21
P31
P3829
P496
0000-0002-0518-7199