about
PML nuclear bodiesRegulation of p53 activity in nuclear bodies by a specific PML isoformCommon properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modificationThe tripartite motif family identifies cell compartments.PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA.Sp100 interacts with ETS-1 and stimulates its transcriptional activityPromyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodiesFLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodiesSumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activityCoordinated regulation of p53 apoptotic targets BAX and PUMA by SMAR1 through an identical MAR elementHuman SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infectionsMageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBsPML colocalizes with and stabilizes the DNA damage response protein TopBP1Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption.Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteinsThe mechanisms of PML-nuclear body formationEpstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9MOZ increases p53 acetylation and premature senescence through its complex formation with PMLSumoylation of the novel protein hRIP{beta} is involved in replication protein A deposition in PML nuclear bodiesThe promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damageProteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression.Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodiesTranscription factor Sp3 is silenced through SUMO modification by PIAS1Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2.Self-association of coilin reveals a common theme in nuclear body localizationProtein inhibitor of activated STAT Y (PIASy) and a splice variant lacking exon 6 enhance sumoylation but are not essential for embryogenesis and adult lifeAbility of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cellsRepression of PML nuclear body-associated transcription by oxidative stress-activated Bach2TRIM family proteins and their emerging roles in innate immunityPhosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1The zebrafish moonshine gene encodes transcriptional intermediary factor 1gamma, an essential regulator of hematopoiesisThe potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1Dynamic Response of IFI16 and Promyelocytic Leukemia Nuclear Body Components to Herpes Simplex Virus 1 InfectionDeficient sumoylation of yeast 2-micron plasmid proteins Rep1 and Rep2 associated with their loss from the plasmid-partitioning locus and impaired plasmid inheritance.Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradationCooperation of sumoylated chromosomal proteins in rDNA maintenanceTelomeric DNA mediates de novo PML body formationKaposi's sarcoma-associated herpesvirus K-Rta exhibits SUMO-targeting ubiquitin ligase (STUbL) like activity and is essential for viral reactivation
P2860
Q22065791-CD550F5D-86AD-42D0-8070-79394EFD607BQ24290520-75C35926-4970-4912-B499-CCC48E0FCED1Q24291154-849060E8-B85F-429A-91E3-27ED5BBD6F47Q24291183-CC0A641D-91D5-4D41-A615-9C140570700BQ24291551-8FFCBA42-520D-44E8-BFF5-991FB70C2601Q24292513-D6DF21B4-E85B-44E5-9A9C-FA4709D2A271Q24293202-2518C097-25F2-46EC-BE22-1C1600AB96B6Q24294356-C508F6F5-6B1F-4A4D-BF3E-C9185A80E61FQ24294867-A4569D22-93A0-4068-8011-08E26A34C0ECQ24295165-C7F4068D-06A0-4AD7-8CBC-F8CB02A1BFD4Q24297146-930026C8-D9F5-49A9-B79E-32FA1313D8EFQ24298207-2DDB60A5-79BA-4325-938A-002DAF1B1C69Q24298226-3E022AF2-B277-4D3A-8B88-B928FA222B0BQ24298306-F7629C20-76B8-48B1-B8E5-F6E3CB95FB13Q24303540-0DFF2EFA-DBA6-43F2-97B3-99C52C12E62EQ24305676-46836017-518A-4EB4-98BE-2C8C1AE708DBQ24309409-FFF7306A-2C48-48F2-94D5-0861A2ADD5E6Q24311595-9B271A1C-AE67-41E3-AA1D-D804E845F892Q24317074-50C3C12B-CC38-4837-8ADB-3DFF72CB05CBQ24319117-05B783FF-116F-4A7E-97E0-6D10491E9066Q24319535-8F7358C7-2E28-48CC-AA45-80F30560DFBCQ24337110-75D86C4B-2E82-4166-906E-A723C680C1A5Q24529191-A38C04D5-0E02-4A78-8BB7-7DCD4E5A775AQ24529499-DE0AD2AC-3CEB-4316-B535-F272901D78CEQ24534887-5E8CE1F1-1598-4B1F-91A7-3F5C6F811C1BQ24540313-BCE43195-C613-43BE-8685-177515BC41CEQ24551044-99675FF0-ABA5-480D-8D8D-53BBAD0595EEQ24561977-9FABD0FE-4F4D-4C99-B31F-DA44D432EB84Q24563268-787E4F47-3ADC-4B6C-8368-E5BC07ED7451Q24602452-E815B6F7-C4FC-4A41-B53B-8335CB8EDCD6Q24607229-81A67FBC-79AA-4298-9875-A71A722D6FDBQ24685095-5EBEB8EA-EE04-4074-A510-F16FAC8DB651Q24798941-B9A3D0A6-1A02-4985-BFF7-A1C9BF6334FFQ27027918-01F33215-DB8A-4FCA-8FE2-81F62303F61DQ27321075-5D3EA63E-4E03-4ECD-99A3-AC0FF4B0631BQ27936318-7AB225CB-7B46-4D95-BC28-E29CE3A8ADAFQ28367104-35461B9B-549E-4DA4-B2D4-11E84ADCE6F9Q28473816-F441AB23-B9B5-4914-8AC8-AC6740A5A809Q28508824-B9B3741C-51F2-4F36-8372-849B21E86913Q28535568-ABA51424-4DF2-439B-A8C0-B25DED888C8A
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Role of SUMO-1-modified PML in nuclear body formation
@ast
Role of SUMO-1-modified PML in nuclear body formation
@en
Role of SUMO-1-modified PML in nuclear body formation
@en-gb
Role of SUMO-1-modified PML in nuclear body formation
@nl
type
label
Role of SUMO-1-modified PML in nuclear body formation
@ast
Role of SUMO-1-modified PML in nuclear body formation
@en
Role of SUMO-1-modified PML in nuclear body formation
@en-gb
Role of SUMO-1-modified PML in nuclear body formation
@nl
prefLabel
Role of SUMO-1-modified PML in nuclear body formation
@ast
Role of SUMO-1-modified PML in nuclear body formation
@en
Role of SUMO-1-modified PML in nuclear body formation
@en-gb
Role of SUMO-1-modified PML in nuclear body formation
@nl
P2093
P3181
P1433
P1476
Role of SUMO-1-modified PML in nuclear body formation
@en
P2093
P P Pandolfi
P S Freemont
P304
P3181
P407
P577
2000-05-01T00:00:00Z