Epstein-Barr virus nuclear antigen 3C and prothymosin alpha interact with the p300 transcriptional coactivator at the CH1 and CH3/HAT domains and cooperate in regulation of transcription and histone acetylation.
about
SCFSkp2 complex targeted by Epstein-Barr virus essential nuclear antigenRole of EBNA-3 Family Proteins in EBV Associated B-cell LymphomagenesisThe Role of Gammaherpesviruses in Cancer PathogenesisEpigenetic Impact on EBV Associated B-Cell LymphomagenesisNovel function of prothymosin alpha as a potent inhibitor of human immunodeficiency virus type 1 gene expression in primary macrophagesRole of chromatin during herpesvirus infections.Epstein-Barr virus nuclear antigen 3C facilitates G1-S transition by stabilizing and enhancing the function of cyclin D1.Epstein-Barr virus nuclear antigen 3C stabilizes Gemin3 to block p53-mediated apoptosis.Epstein-Barr virus nuclear antigen 3A protein regulates CDKN2B transcription via interaction with MIZ-1E2F1 mediated apoptosis induced by the DNA damage response is blocked by EBV nuclear antigen 3C in lymphoblastoid cells.The metastatic suppressor Nm23-H1 interacts with EBNA3C at sequences located between the glutamine- and proline-rich domains and can cooperate in activation of transcriptionEpstein-Barr virus nuclear antigen 3C regulated genes in lymphoblastoid cell lines.The importance of epigenetic alterations in the development of epstein-barr virus-related lymphomas.Epstein-Barr virus nuclear antigens 3C and 3A maintain lymphoblastoid cell growth by repressing p16INK4A and p14ARF expression.EBNA3C coactivation with EBNA2 requires a SUMO homology domain.EBNA3C attenuates the function of p53 through interaction with inhibitor of growth family proteins 4 and 5Epstein-Barr virus nuclear antigen 3C targets p53 and modulates its transcriptional and apoptotic activities.Modulation of enhancer looping and differential gene targeting by Epstein-Barr virus transcription factors directs cellular reprogramming.The ATM/ATR signaling effector Chk2 is targeted by Epstein-Barr virus nuclear antigen 3C to release the G2/M cell cycle blockEpstein-Barr virus oncoprotein super-enhancers control B cell growthEBV Nuclear Antigen 3C Mediates Regulation of E2F6 to Inhibit E2F1 Transcription and Promote Cell Proliferation.C646, a Novel p300/CREB-Binding Protein-Specific Inhibitor of Histone Acetyltransferase, Attenuates Influenza A Virus InfectionFunction of prothymosin alpha in chromatin decondensation and expression of thymosin beta-4 linked to angiogenesis and synaptic plasticity.Prothymosin α overexpression contributes to the development of pulmonary emphysema.Epstein-Barr virus nuclear protein EBNA3C residues critical for maintaining lymphoblastoid cell growth.Epstein-Barr virus nuclear protein 3C domains necessary for lymphoblastoid cell growth: interaction with RBP-Jkappa regulates TCL1.During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription.Tumor viruses and cancer biology: Modulating signaling pathways for therapeutic intervention.Intracellular and extracellular cytokine-like functions of prothymosin α: implications for the development of immunotherapies.Histone modifications in herpesvirus infections.Impact of EBV essential nuclear protein EBNA-3C on B-cell proliferation and apoptosis.Host-virus interactions: from the perspectives of epigenetics.Dissecting the contribution of EBNA3C domains important for EBV-induced B-cell growth and proliferation.Deregulation of the cell cycle machinery by Epstein-Barr virus nuclear antigen 3C.An overview of new biomolecular pathways in pathogen-related cancers.Epstein-Barr virus nuclear protein EBNA3C directly induces expression of AID and somatic mutations in B cells.Knockdown of prothymosin α leads to apoptosis and developmental defects in zebrafish embryos.Epstein-Barr virus EBNA-3C is targeted to and regulates expression from the bidirectional LMP-1/2B promoter.Stress-induced non-vesicular release of prothymosin-α initiated by an interaction with S100A13, and its blockade by caspase-3 cleavage.Biophysical and mutational analysis of the putative bZIP domain of Epstein-Barr virus EBNA 3C.
P2860
Q24556627-451EDE71-56D1-493B-9ED6-46E475DFFA1EQ26752541-91F3572A-3BC0-4C59-B5D2-28C52DA5CCE2Q26767186-1D0E2094-B6DA-4D90-AC23-EB96316A9F6CQ28068361-68AB6523-CC50-4163-BA12-47F8B87E54B8Q30445480-F01867D6-7819-42D2-8566-8B4B9D321CDAQ33346968-F75035E4-D483-49AB-B8A8-4EB81280DFAAQ33828576-FC7531BE-1E92-4D17-B7BB-8CA3F19411A5Q34102722-034D4395-5447-444E-BDDD-D04AA027856DQ34115503-E23D65E2-9865-439A-9EA9-114F06FB8B3EQ34205875-23E5201B-C6DC-4657-B79D-67D1AE062F03Q34362138-FE6318B9-A8EC-4BF0-888F-7F8CE2825914Q34472101-19898831-0188-486B-94E3-447E295FB60DQ34549462-57CA0B84-FBE2-40CE-B9EB-4BE26280FD7FQ34549944-97E28B89-ED91-4D4F-B117-6895BEA553ADQ34552733-AD8AB0A1-EEF6-4693-8EA0-D91DF4D4F33BQ34741776-52919FF2-23F1-440C-A216-D16DA9C29E3DQ34872837-DAA52356-2F52-4D10-889A-9165ECAAAACCQ34998243-3BA59EF0-69D7-4B9D-B124-994772615918Q35857290-0D12D157-26EA-4933-95C1-875DA073D95AQ35963272-54FF6973-B2AF-468F-8E7E-D4FB92F59C74Q36109083-FFF67BB9-2FC3-47A4-8886-A78EC3C647E4Q36644882-63723AEC-7EC5-460F-9A0F-8B104E04A774Q36818209-018C9408-50FC-4DCC-8253-02180BDB0A93Q36906886-BB2DC504-8984-4D0B-8BDA-84C825128BE6Q37132783-6B5ED4C3-D3A3-4DC1-993A-97D83E188A78Q37452130-28555861-F785-464E-90CE-C8294AFEDEB1Q37492667-DD550F6A-CFF8-4CF7-B3DF-AD4CA85F6362Q37810431-590B86BD-E68E-4987-9380-DAC53DB12D99Q37909411-6E0A2A01-796B-477E-A1AE-F7E780925E14Q37970405-E79BE3F3-5ADA-47D1-B733-D39D5B7C3962Q38086861-AC48FFF5-E9EB-4833-86BD-B81BD12CB415Q38200036-8B65E1B3-0207-44F5-A21D-B7A09551E87CQ38286347-E79E87E1-0D5F-44EE-97A8-E6B3F5C094ECQ38337443-E4040BD2-345A-4E33-AE22-CEB5980748ABQ38515827-3DDB9EAE-ED74-48CC-9D1B-E5AD8596A4A2Q38768957-33B8D75E-E207-4070-A78E-37160BCA646AQ39096488-1E888DC7-347A-4A40-ADFF-007B3D684D70Q39306073-E49A4E2E-A698-4EF4-B489-ABA74CE331ADQ39704112-4EA51D98-7279-4AB2-BA0D-4964B8EFCE21Q39756123-167FD339-DF86-471D-B404-50E8CCB9E360
P2860
Epstein-Barr virus nuclear antigen 3C and prothymosin alpha interact with the p300 transcriptional coactivator at the CH1 and CH3/HAT domains and cooperate in regulation of transcription and histone acetylation.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Epstein-Barr virus nuclear ant ...... iption and histone acetylation
@nl
Epstein-Barr virus nuclear ant ...... ption and histone acetylation.
@ast
Epstein-Barr virus nuclear ant ...... ption and histone acetylation.
@en
type
label
Epstein-Barr virus nuclear ant ...... iption and histone acetylation
@nl
Epstein-Barr virus nuclear ant ...... ption and histone acetylation.
@ast
Epstein-Barr virus nuclear ant ...... ption and histone acetylation.
@en
prefLabel
Epstein-Barr virus nuclear ant ...... iption and histone acetylation
@nl
Epstein-Barr virus nuclear ant ...... ption and histone acetylation.
@ast
Epstein-Barr virus nuclear ant ...... ption and histone acetylation.
@en
P2093
P2860
P50
P3181
P1433
P1476
Epstein-Barr virus nuclear ant ...... iption and histone acetylation
@en
P2093
Chitra Subramanian
Sameez Hasan
P2860
P304
P3181
P356
10.1128/JVI.76.10.4699-4708.2002
P407
P577
2002-05-01T00:00:00Z