Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
about
Virion assembly factories in the nucleus of polyomavirus-infected cellsA novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitroSequestration and inhibition of Daxx-mediated transcriptional repression by PMLNovel alternative splicing and nuclear localization of human RGS12 gene productsCommon properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modificationInteraction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption.Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartmentChromatin components as part of a putative transcriptional repressing complexEvidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1Cellular localization, expression, and structure of the nuclear dot protein 52Identification and characterization of a leukocyte-specific component of the nuclear bodyMolecular cloning of a new interferon-induced PML nuclear body-associated proteinThe interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibilityThe promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma proteinSUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PMLStructural and functional heterogeneity of nuclear bodiesThe promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoterViral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruptionConjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus.Epstein-Barr virus (EBV) SM protein induces and recruits cellular Sp110b to stabilize mRNAs and enhance EBV lytic gene expressionAbility of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cellsCovalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1Intrinsic host restriction factors of human cytomegalovirus replication and mechanisms of viral escapeTranscriptional activation of the adenoviral genome is mediated by capsid protein VIA Structural Basis for the Assembly and Functions of a Viral Polymer that Inactivates Multiple Tumor SuppressorsAdenovirus Early Proteins and Host SumoylationThe Role of Nuclear Antiviral Factors against Invading DNA Viruses: The Immediate Fate of Incoming Viral GenomesIs there a risk of zoonotic disease due to adenoviruses?Identification of the LIM protein FHL2 as a coactivator of beta-cateninThe glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP UArsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemiaAdenovirus type 5 early region 1B 55K oncoprotein-dependent degradation of cellular factor Daxx is required for efficient transformation of primary rodent cellsThe nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiersFunctional connection between Rad51 and PML in homology-directed repair.Transforming potential of the adenovirus type 5 E4orf3 protein.Roles for the E4 orf6, orf3, and E1B 55-kilodalton proteins in cell cycle-independent adenovirus replication.Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PMLRelocalization of the Mre11-Rad50-Nbs1 complex by the adenovirus E4 ORF3 protein is required for viral replicationThe papillomavirus minor capsid protein, L2, induces localization of the major capsid protein, L1, and the viral transcription/replication protein, E2, to PML oncogenic domainsPersistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins.
P2860
Q21558475-260F55BB-18DB-4619-8DB3-0477F84780D5Q22009106-2DBAE20E-F082-4168-9DE2-34E4FC11078BQ22253162-98B6C694-EFE5-4950-B9BC-54B6BF817F46Q22254384-E4B0D62D-65C9-4F27-994A-4467A5B4A79FQ24291154-AE36FE48-EAC2-49FC-B298-946967F5F87FQ24305676-7A664254-F178-4919-AAE8-E82AF1CEEC6CQ24309229-A6D4EE9B-FD62-45CB-B7D8-06323F9DD354Q24309270-4334C9DF-C72E-4B7D-9081-A7EB9C9CD445Q24316222-81EF087A-92A9-4D28-8BE9-8A289363C593Q24318605-440848C2-612A-4DFE-A10F-4ED87B60216CQ24319438-3D4982DA-3A62-43DA-B449-1D2CFA7E9BACQ24319545-93AFC32B-E3AE-43AA-BF90-DEE0F89A40BAQ24324326-37B09477-3EBF-4CB2-886A-EE7AAD46C470Q24324766-FF864269-FF39-4741-9107-13B3E520AE5DQ24338995-891920CE-B86E-40E7-8B20-5BAE4FD52189Q24517779-6C5691F6-763C-4479-A996-3A5939769E1DQ24522845-404FC92C-D088-46BA-9283-EBB84BD4D4C9Q24527246-0A232D47-74DE-4037-91E7-16C3ED6BDC18Q24532901-E68A1885-422D-4EB8-AA70-5AE5AC27376FQ24562972-09DC30A4-89E1-4506-93A6-ED0A245E7E87Q24563268-8FACF9D4-6413-47C7-A4CB-53EF70C2372EQ24656539-3FF8A657-7811-49D2-8976-8DD7BFC3AD44Q26738747-D1AF20A9-4434-4C10-A51B-C0534745795FQ27347199-A35AC99D-4443-40D2-B84A-2997B774241AQ27674473-9E596FE1-6BCA-4F32-9E70-9F8FBFCBE586Q28070074-C22A1D90-1BA1-4742-8923-6F9BC9A54BCCQ28071373-A6F74B1C-7239-4A77-9E26-9F5AB983D841Q28080712-CCD1D4D1-29D8-4EA0-9380-77B85265553EQ28216665-33F65B09-FBC6-4F5A-89E8-928C55602B69Q28253219-7EBDEE13-6ACC-4768-A796-7B6E70F6A781Q28379542-470CB0C1-4FE0-44D0-93FE-4FFB97A30E65Q28574947-6B6BA575-A406-4971-8CFB-1D772A9DA1C9Q28616490-89DCE2AD-21AE-4D33-957F-32FD17387460Q31037336-F7A5C9DA-9904-45EE-B4A9-A17EAFCCC3DAQ33642090-2925E26E-9E31-4803-AEEC-67532D22AD31Q33649728-0B7D02DE-00B5-44CB-959F-32BFD5005320Q33776312-949CA1EE-F1DA-4F43-A321-926F160DDFE8Q33780662-A6F6FD6A-1347-4E6A-B33E-8BDC1875FDDDQ33781905-7E649699-576C-4E96-BDBE-4B1674C379F8Q33783411-46EEA76E-BBD3-4A39-8789-9192260DE0BF
P2860
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
@en
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
@nl
type
label
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
@en
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
@nl
prefLabel
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
@en
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.
@nl
P2093
P2860
P50
P356
P1476
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies
@en
P2093
P2860
P356
10.1083/JCB.131.1.45
P407
P577
1995-10-01T00:00:00Z