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Epstein-Barr Virus Nuclear Antigen 3C Augments Mdm2-Mediated p53 Ubiquitination and Degradation by Deubiquitinating Mdm2
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1096-9896(199701)181:1<51::aid-path689>3.0.co;2-nopenalex-snapshot
p21WAF1/CIP1 AND MDM2 EXPRESSION IN NON-HODGKIN'S LYMPHOMA AND THEIR RELATIONSHIP TO p53 STATUS: A p53+, MDM2−, p21− IMMUNOPHENOTYPE ASSOCIATED WITH MISSENSE p53 MUTATIONS
inferredcites →https://doi.org/10.1002/ijc.2910020505openalex-snapshot
Two established in vitro cell lines from human mesenchymal tumours
inferredcites →https://doi.org/10.1002/ijc.2910160114openalex-snapshot
Production by EBV infection of an EBNA‐positive subline from an EBNA‐negative human lymphoma cell line without detectable EBV DNA
inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06634.xopenalex-snapshot
EBNA‐2 and EBNA‐LP cooperate to cause G0 to G1 transition during immortalization of resting human B lymphocytes by Epstein‐Barr virus.
inferredcites →https://doi.org/10.1002/j.1460-2075.1995.tb06978.xopenalex-snapshot
B‐cell proliferation and induction of early G1‐regulating proteins by Epstein‐Barr virus mutants conditional for EBNA2.
inferredcites →https://doi.org/10.1006/jmbi.2000.4042openalex-snapshot
T-coffee: a novel method for fast and accurate multiple sequence alignment 1 1Edited by J. Thornton
inferredcites →https://doi.org/10.1007/bf01535205openalex-snapshot
Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
inferredcites →https://doi.org/10.1007/bf03401903openalex-snapshot
The MDM2 Oncoprotein Binds Specifically to RNA through its RING Finger Domain
inferredcites →https://doi.org/10.1016/j.cell.2004.06.016openalex-snapshot
Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity
inferredcites →https://doi.org/10.1016/j.cell.2004.11.022openalex-snapshot
A Single Nucleotide Polymorphism in the MDM2 Promoter Attenuates the p53 Tumor Suppressor Pathway and Accelerates Tumor Formation in Humans
inferredcites →https://doi.org/10.1016/j.molcel.2005.02.029openalex-snapshot
Structure of the p53 Binding Domain of HAUSP/USP7 Bound to Epstein-Barr Nuclear Antigen 1
inferredcites →https://doi.org/10.1016/j.molcel.2005.04.024openalex-snapshot
Loss of HAUSP-Mediated Deubiquitination Contributes to DNA Damage-Induced Destabilization of Hdmx and Hdm2
inferredcites →https://doi.org/10.1016/j.molcel.2006.01.020openalex-snapshot
p53 Ubiquitination: Mdm2 and Beyond
inferredcites →https://doi.org/10.1016/s0092-8674(00)81400-2openalex-snapshot
The Ink4a Tumor Suppressor Gene Product, p19Arf, Interacts with MDM2 and Neutralizes MDM2's Inhibition of p53
inferredcites →https://doi.org/10.1016/s0092-8674(00)81401-4openalex-snapshot
ARF Promotes MDM2 Degradation and Stabilizes p53: ARF-INK4a Locus Deletion Impairs Both the Rb and p53 Tumor Suppression Pathways
inferredcites →https://doi.org/10.1016/s0378-1119(99)00487-4openalex-snapshot
MDM2 — master regulator of the p53 tumor suppressor protein
inferredcites →https://doi.org/10.1016/s0955-0674(00)00216-7openalex-snapshot
Regulation and function of the p53 tumor suppressor protein
inferredcites →https://doi.org/10.1016/s0968-0004(97)01119-5openalex-snapshot
MDM2-arbiter of p53's destruction
inferredcites →https://doi.org/10.1016/s1074-5521(02)00248-xopenalex-snapshot
Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family
inferredcites →https://doi.org/10.1016/s1097-2765(00)80140-9openalex-snapshot
p300/MDM2 Complexes Participate in MDM2-Mediated p53 Degradation
inferredcites →https://doi.org/10.1016/s1097-2765(00)80309-3openalex-snapshot
RB Regulates the Stability and the Apoptotic Function of p53 via MDM2
inferredcites →https://doi.org/10.1016/s1097-2765(04)00157-1openalex-snapshot
A Dynamic Role of HAUSP in the p53-Mdm2 Pathway
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/35095584openalex-snapshot
Epstein-Barr virus: exploiting the immune system
inferredcites →https://doi.org/10.1038/375691a0openalex-snapshot
Stimulation of E2F1/DP1 transcriptional activity by MDM2 oncoprotein
inferredcites →https://doi.org/10.1038/375694a0openalex-snapshot
Interaction between the retinoblastoma protein and the oncoprotein MDM2
inferredcites →https://doi.org/10.1038/387296a0openalex-snapshot
Mdm2 promotes the rapid degradation of p53
inferredcites →https://doi.org/10.1038/nature01803openalex-snapshot
CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
inferredcites →https://doi.org/10.1038/ncb1442openalex-snapshot
Critical role for Daxx in regulating Mdm2
inferredcites →https://doi.org/10.1038/ncb1562openalex-snapshot
C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
inferredcites →https://doi.org/10.1038/nrc2012openalex-snapshot
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
inferredcites →https://doi.org/10.1038/sj.emboj.7600145openalex-snapshot
Accelerated MDM2 auto‐degradation induced by DNA‐damage kinases is required for p53 activation
inferredcites →https://doi.org/10.1038/sj.emboj.7601465openalex-snapshot
The Mdm2 RING domain C‐terminus is required for supramolecular assembly and ubiquitin ligase activity
inferredcites →https://doi.org/10.1038/sj.onc.1203464openalex-snapshot
Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
inferredcites →https://doi.org/10.1038/sj.onc.1204241openalex-snapshot
The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
inferredcites →https://doi.org/10.1038/sj.onc.1206851openalex-snapshot
MDM2-ARF complex regulates p53 sumoylation
inferredcites →https://doi.org/10.1073/pnas.0503886102openalex-snapshot
Epstein–Barr virus latent antigen 3C can mediate the degradation of the retinoblastoma protein through an SCF cellular ubiquitin ligase
inferredcites →https://doi.org/10.1073/pnas.95.14.8292openalex-snapshot
Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2
inferredcites →https://doi.org/10.1073/pnas.95.26.15608openalex-snapshot
Overexpression of Mdm2 in mice reveals a p53-independent role for Mdm2 in tumorigenesis
inferredcites →https://doi.org/10.1073/pnas.96.26.14973openalex-snapshot
Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
inferredcites →https://doi.org/10.1073/pnas.97.23.12547openalex-snapshot
MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
inferredcites →https://doi.org/10.1074/jbc.272.49.30651openalex-snapshot
The MDM2 C-terminal Region Binds to TAFII250 and Is Required for MDM2 Regulation of the Cyclin A Promoter
inferredcites →https://doi.org/10.1074/jbc.275.12.8945openalex-snapshot
Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53
inferredcites →https://doi.org/10.1074/jbc.m004252200openalex-snapshot
A Novel Cellular Protein (MTBP) Binds to MDM2 and Induces a G1 Arrest That Is Suppressed by MDM2
inferredcites →https://doi.org/10.1074/jbc.m303977200openalex-snapshot
Protein Profiling with Epstein-Barr Nuclear Antigen-1 Reveals an Interaction with the Herpesvirus-associated Ubiquitin-specific Protease HAUSP/USP7
inferredcites →https://doi.org/10.1093/emboj/17.2.554openalex-snapshot
Nucleo‐cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
inferredcites →https://doi.org/10.1093/emboj/19.1.94openalex-snapshot
Recognition of the polyubiquitin proteolytic signal
inferredcites →https://doi.org/10.1093/nar/26.15.3453openalex-snapshot
The MDM2 gene amplification database
inferredcites →https://doi.org/10.1099/0022-1317-36-1-59openalex-snapshot
Characteristics of a Human Cell Line Transformed by DNA from Human Adenovirus Type 5
inferredcites →https://doi.org/10.1099/vir.0.80763-0openalex-snapshot
Epstein–Barr virus EBNA3 proteins bind to the C8/α7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells
inferredcites →https://doi.org/10.1101/gad.11.6.714openalex-snapshot
Targeted expression of MDM2 uncouples S phase from mitosis and inhibits mammary gland development independent of p53.
inferredcites →https://doi.org/10.1101/gad.12.19.2984openalex-snapshot
Tumor surveillance via the ARF–p53 pathway
inferredcites →https://doi.org/10.1101/gad.886901openalex-snapshot
ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
inferredcites →https://doi.org/10.1126/science.274.5289.948openalex-snapshot
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
inferredcites →https://doi.org/10.1128/.74.11.5151-5160.2000openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3C Activates the Latent Membrane Protein 1 Promoter in the Presence of Epstein-Barr Virus Nuclear Antigen 2 through Sequences Encompassing an Spi-1/Spi-B Binding Site
inferredcites →https://doi.org/10.1128/jvi.02500-07openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3C Interacts with and Enhances the Stability of the c-Myc Oncoprotein
inferredcites →https://doi.org/10.1128/jvi.69.5.3108-3116.1995openalex-snapshot
Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappa
inferredcites →https://doi.org/10.1128/jvi.70.6.4179-4183.1996openalex-snapshot
EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJkappa in Epstein-Barr virus-transformed B lymphocytes
inferredcites →https://doi.org/10.1128/jvi.76.1.232-242.2002openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3C Putative Repression Domain Mediates Coactivation of the LMP1 Promoter with EBNA-2
inferredcites →https://doi.org/10.1128/jvi.78.1.367-377.2004openalex-snapshot
EBNA3C Coactivation with EBNA2 Requires a SUMO Homology Domain
inferredcites →https://doi.org/10.1128/jvi.78.4.1981-1991.2004openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3C Regulates Cyclin A/p27 Complexes and Enhances Cyclin A-Dependent Kinase Activity
inferredcites →https://doi.org/10.1128/mcb.13.7.4107openalex-snapshot
Mapping of the p53 and mdm-2 Interaction Domains
inferredcites →https://doi.org/10.1128/mcb.14.11.7414openalex-snapshot
The Ribosomal L5 Protein Is Associated with mdm-2 and mdm-2-p53 Complexes
inferredcites →https://doi.org/10.1128/mcb.16.5.2445openalex-snapshot
mdm-2 Inhibits the G1 Arrest and Apoptosis Functions of the p53 Tumor Suppressor Protein
inferredcites →https://doi.org/10.1128/mcb.19.5.3704openalex-snapshot
Transcription Factor E2F-1 Is Upregulated in Response to DNA Damage in a Manner Analogous to That of p53
inferredcites →https://doi.org/10.1128/mcb.20.15.5722-5735.2000openalex-snapshot
Modulation of Histone Acetyltransferase Activity through Interaction of Epstein-Barr Nuclear Antigen 3C with Prothymosin Alpha
inferredcites →https://doi.org/10.1128/mcb.20.6.2186-2197.2000openalex-snapshot
Apoptotic and Growth-Promoting Activity of E2F Modulated by MDM2
inferredcites →https://doi.org/10.1128/mcb.22.17.6170-6182.2002openalex-snapshot
Hypophosphorylation of Mdm2 Augments p53 Stability
inferredcites →https://doi.org/10.1128/mcb.23.14.4939-4947.2003openalex-snapshot
Critical Contribution of the MDM2 Acidic Domain to p53 Ubiquitination
inferredcites →https://doi.org/10.1128/mcb.25.5.1749-1763.2005openalex-snapshot
SCF Skp2 Complex Targeted by Epstein-Barr Virus Essential Nuclear Antigen
inferredcites →https://doi.org/10.1146/annurev.biochem.67.1.425openalex-snapshot
THE UBIQUITIN SYSTEM
inferredcites →https://doi.org/10.1177/002215549904701011openalex-snapshot
High Expression of MDM2 Protein and Low Rate of p21 WAF1/CIP1 Expression in SCID Mice Epstein Barr Virus-induced Lymphoproliferation
inferredcites →https://doi.org/10.2174/138920306776359777openalex-snapshot
Structure and Function of the Epstein-Barr Virus Transcription Factor, EBNA 3C
inferredcites →https://doi.org/10.2174/1389557033488178openalex-snapshot
The p53-Mdm2 Pathway: Targets for the Development of New Anticancer Therapeutics
inferredcites →https://doi.org/10.4049/jimmunol.155.3.1047openalex-snapshot
Latent membrane protein-1 induces cyclin D2 expression, pRb hyperphosphorylation, and loss of TGF-β 1-mediated growth inhibition in EBV-positive B cells
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Clinical Evidence and Therapeutic Treatments at the Time of the Coronaviruses Responsible for SARS: A Perspective Point of View.
inferred← citeshttps://doi.org/10.1002/ijc.25414openalex-snapshot
Epstein‐Barr virus‐encoded EBNA‐5 forms trimolecular protein complexes with MDM2 and p53 and inhibits the transactivating function of p53
inferred← citeshttps://doi.org/10.1002/mc.20689openalex-snapshot
Role of the MDM2 SNP309 polymorphism in the initiation and early age of onset of nasopharyngeal carcinoma
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Epstein-Barr Virus-Positive Diffuse Large B-Cell Lymphoma, Not Otherwise Specified
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From Family Study to Population Study: A History of Genetic Mapping for Nasopharyngeal Carcinoma (NPC)
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Interaction of Epstein-Barr virus (EBV) with human B-lymphocytes
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HIV-1 Nef promotes ubiquitination and proteasomal degradation of p53 tumor suppressor protein by using E6AP
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CRISPR/Cas9 Screens Reveal Epstein-Barr Virus-Transformed B Cell Host Dependency Factors
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DNA damage checkpoints in nasopharyngeal carcinoma
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KSHV LANA and EBV LMP1 induce the expression of UCH-L1 following viral transformation
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Three Epstein–Barr virus latency proteins independently promote genomic instability by inducing DNA damage, inhibiting DNA repair and inactivating cell cycle checkpoints
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Transcriptional and epigenetic modulation of autophagy promotes EBV oncoprotein EBNA3C induced B-cell survival
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Intrinsic p53 activation restricts gammaherpesvirus driven germinal center B cell expansion during latency establishment
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HIV-1 Tat potently stabilises Mdm2 and enhances viral replication
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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL pro via E3 ubiquitin ligase RCHY1
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p53 Controls Murine Gammaherpesvirus Latency and Prevents Infection-Associated IgH/c-Myc Translocations
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MDM4 is an essential disease driver targeted by 1q gain in Burkitt lymphoma
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Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin‐related modifiers
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The F-box E3 ligase protein FBXO11 regulates EBNA3C-associated degradation of BCL6
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Epstein-Barr Virus MicroRNA miR-BART5-3p Inhibits p53 Expression
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Transcriptional Downregulation of p27KIP1 through Regulation of E2F Function during LMP1-Mediated Transformation
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EBNA3C Attenuates the Function of p53 through Interaction with Inhibitor of Growth Family Proteins 4 and 5
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EBNA3C-Mediated Regulation of Aurora Kinase B Contributes to Epstein-Barr Virus-Induced B-Cell Proliferation through Modulation of the Activities of the Retinoblastoma Protein and Apoptotic Caspases
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Murine Gammaherpesvirus 68 LANA and SOX Homologs Counteract ATM-Driven p53 Activity during Lytic Viral Replication
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Epstein-Barr Virus Essential Antigen EBNA3C Attenuates H2AX Expression
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Extensive Co-Operation between the Epstein-Barr Virus EBNA3 Proteins in the Manipulation of Host Gene Expression and Epigenetic Chromatin Modification
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Upregulation of the Cell-Cycle Regulator RGC-32 in Epstein-Barr Virus-Immortalized Cells
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Epigenetic Repression of p16INK4A by Latent Epstein-Barr Virus Requires the Interaction of EBNA3A and EBNA3C with CtBP
inferred← citeshttps://doi.org/10.1371/journal.ppat.1001275openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3C Facilitates G1-S Transition by Stabilizing and Enhancing the Function of Cyclin D1
inferred← citeshttps://doi.org/10.1371/journal.ppat.1002418openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3C Stabilizes Gemin3 to Block p53-mediated Apoptosis
inferred← citeshttps://doi.org/10.1371/journal.ppat.1002573openalex-snapshot
E2F1 Mediated Apoptosis Induced by the DNA Damage Response Is Blocked by EBV Nuclear Antigen 3C in Lymphoblastoid Cells
inferred← citeshttps://doi.org/10.1371/journal.ppat.1003186openalex-snapshot
Epstein - Barr Virus Transforming Protein LMP-1 Alters B Cells Gene Expression by Promoting Accumulation of the Oncoprotein ΔNp73α
inferred← citeshttps://doi.org/10.1371/journal.ppat.1003187openalex-snapshot
Induction of p16INK4a Is the Major Barrier to Proliferation when Epstein-Barr Virus (EBV) Transforms Primary B Cells into Lymphoblastoid Cell Lines
inferred← citeshttps://doi.org/10.1371/journal.ppat.1003314openalex-snapshot
The EBV Latent Antigen 3C Inhibits Apoptosis through Targeted Regulation of Interferon Regulatory Factors 4 and 8
inferred← citeshttps://doi.org/10.1371/journal.ppat.1004304openalex-snapshot
EBNA3C Augments Pim-1 Mediated Phosphorylation and Degradation of p21 to Promote B-Cell Proliferation
inferred← citeshttps://doi.org/10.1371/journal.ppat.1004415openalex-snapshot
Epstein-Barr Virus Nuclear Antigen 3A Promotes Cellular Proliferation by Repression of the Cyclin-Dependent Kinase Inhibitor p21WAF1/CIP1
inferred← citeshttps://doi.org/10.1371/journal.ppat.1004822openalex-snapshot
The EBNA3 Family of Epstein-Barr Virus Nuclear Proteins Associates with the USP46/USP12 Deubiquitination Complexes to Regulate Lymphoblastoid Cell Line Growth
inferred← citeshttps://doi.org/10.1371/journal.ppat.1005844openalex-snapshot
EBV Nuclear Antigen 3C Mediates Regulation of E2F6 to Inhibit E2F1 Transcription and Promote Cell Proliferation
inferred← citeshttps://doi.org/10.1371/journal.ppat.1006500openalex-snapshot
An essential EBV latent antigen 3C binds Bcl6 for targeted degradation and cell proliferation
inferred← citeshttps://doi.org/10.1371/journal.ppat.1007514openalex-snapshot
EBNA3C facilitates RASSF1A downregulation through ubiquitin-mediated degradation and promoter hypermethylation to drive B-cell proliferation
inferred← citeshttps://doi.org/10.1371/journal.ppat.1007796openalex-snapshot
EBV epitranscriptome reprogramming by METTL14 is critical for viral-associated tumorigenesis
inferred← citeshttps://doi.org/10.1371/journal.ppat.1008105openalex-snapshot
Proteasomal inhibition triggers viral oncoprotein degradation via autophagy-lysosomal pathway
inferred← citeshttps://doi.org/10.1371/journal.ppat.1012250openalex-snapshot
Combination of bortezomib and venetoclax targets the pro-survival function of LMP-1 and EBNA-3C of Epstein-Barr virus in spontaneous lymphoblastoid cell lines
inferred← citeshttps://doi.org/10.18632/oncotarget.3310openalex-snapshot
EBNA3C regulates p53 through induction of Aurora kinase B
inferred← citeshttps://doi.org/10.18632/oncotarget.5002openalex-snapshot
Dissecting the contribution of EBNA3C domains important for EBV-induced B-cell growth and proliferation
inferred← citeshttps://doi.org/10.18632/oncotarget.7502openalex-snapshot
An EBV recombinant deleted for residues 130-159 in EBNA3C can deregulate p53/Mdm2 and Cyclin D1/CDK6 which results in apoptosis and reduced cell proliferation
inferred← citeshttps://doi.org/10.2147/cmar.s37745openalex-snapshot
Developments in Burkitt's lymphoma: novel cooperations in oncogenic MYC signaling
inferred← citeshttps://doi.org/10.2174/1381612811319180008openalex-snapshot
Deubiquitinating Enzymes as Promising Drug Targets for Infectious Diseases
inferred← citeshttps://doi.org/10.2217/fmb.12.147openalex-snapshot
Impact of EBV Essential Nuclear Protein EBNA-3C on B-Cell Proliferation and Apoptosis
inferred← citeshttps://doi.org/10.2217/fvl-2019-0015openalex-snapshot
Epstein–Barr Virus: Overcoming the DNA Damage Response
inferred← citeshttps://doi.org/10.31487/j.nnb.2022.01.01openalex-snapshot
Bell’s Palsy May Associate with Increased IL1R1: A Pilot Novel Gene and lncRNA Study
inferred← citeshttps://doi.org/10.3389/fimmu.2018.02999openalex-snapshot
Shrimp miR-1000 Functions in Antiviral Immunity by Simultaneously Triggering the Degradation of Two Viral mRNAs
inferred← citeshttps://doi.org/10.3389/fmicb.2011.00161openalex-snapshot
Viral Takeover of the Host Ubiquitin System
inferred← citeshttps://doi.org/10.3389/fmicb.2016.00457openalex-snapshot
Role of EBNA-3 Family Proteins in EBV Associated B-cell Lymphomagenesis
inferred← citeshttps://doi.org/10.3389/fmicb.2016.00585openalex-snapshot
The Modulation of Apoptotic Pathways by Gammaherpesviruses
inferred← citeshttps://doi.org/10.3389/fonc.2018.00265openalex-snapshot
Epstein–Barr Virus-Associated Malignancies: Roles of Viral Oncoproteins in Carcinogenesis
inferred← citeshttps://doi.org/10.3389/fonc.2019.00081openalex-snapshot
Viral-Targeted Strategies Against EBV-Associated Lymphoproliferative Diseases
inferred← citeshttps://doi.org/10.3390/biom12010127openalex-snapshot
The Role of Epstein-Barr Virus in Modulating Key Tumor Suppressor Genes in Associated Malignancies: Epigenetics, Transcriptional, and Post-Translational Modifications
inferred← citeshttps://doi.org/10.3390/biom15040514openalex-snapshot
Neurotropic Viruses as Acute and Insidious Drivers of Aging
inferred← citeshttps://doi.org/10.3390/ijms14024030openalex-snapshot
The Role of F-Box Proteins during Viral Infection
inferred← citeshttps://doi.org/10.3390/ijms27073054openalex-snapshot
Exploring EBNA3C Genetic Variability and Recombination in Epstein–Barr Virus-Associated Cancers
inferred← citeshttps://doi.org/10.3390/pathogens7010031openalex-snapshot
The Cooperative Functions of the EBNA3 Proteins Are Central to EBV Persistence and Latency
inferred← citeshttps://doi.org/10.3390/v13081457openalex-snapshot
Human Coronaviruses: Counteracting the Damage by Storm
inferred← citeshttps://doi.org/10.3390/v15091935openalex-snapshot
E3 Ubiquitin Ligases in Gammaherpesviruses and HIV: A Review of Virus Adaptation and Exploitation
inferred← citeshttps://doi.org/10.3390/v9110339openalex-snapshot
EBV and Apoptosis: The Viral Master Regulator of Cell Fate?
inferred← citeshttps://doi.org/10.3390/v9110352openalex-snapshot
Therapeutic Strategies against Epstein-Barr Virus-Associated Cancers Using Proteasome Inhibitors
inferred← citeshttps://doi.org/10.4161/cbt.10.10.13923openalex-snapshot
Tumor viruses and cancer biology: Modulating signaling pathways for therapeutic intervention
inferred← citeshttps://doi.org/10.70675/1123b896zdfdaz408az9372z41cc116e27dfopenalex-snapshot
Modulation of the innate immune response by the oncoviruses EBV and HPV
inferred← citeshttps://doi.org/10.70675/4ade78c4z0bf6z4533zb4a6z084522268290openalex-snapshot
Rôle des virus EBV et VIH dans la formation de la translocation chromosomique t(8;14) du Lymphome de Burkitt
inferred← citeshttps://doi.org/10.7243/2052-6202-1-5openalex-snapshot
Oncogenic viruses: DUBbing their way to cancer
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