about
The biology of the Ets1 proto-oncogeneVirion assembly factories in the nucleus of polyomavirus-infected cellsSumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activityThe histone deacetylase 9 gene encodes multiple protein isoformsHuman SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expressionPML colocalizes with and stabilizes the DNA damage response protein TopBP1The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteinsSUMO-1 modification of human transcription factor (TF) IID complex subunits: inhibition of TFIID promoter-binding activity through SUMO-1 modification of hsTAF5Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.Modification with SUMO. A role in transcriptional regulationThe SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylaseRole for SUMO modification in facilitating transcriptional repression by BKLF.SUMO-2/3 regulates topoisomerase II in mitosisRecruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML proteinG2E3 is a nucleo-cytoplasmic shuttling protein with DNA damage responsive localizationPhosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1Proteins with two SUMO-like domains in chromatin-associated complexes: the RENi (Rad60-Esc2-NIP45) familyThe potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1Sumoylation of MITF and its related family members TFE3 and TFEBPromyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactionsPhysical and functional interactions between PML and MDM2Identification and characterization of DEN1, a deneddylase of the ULP familyThe promyelocytic leukemia protein represses A20-mediated transcriptionRepression of the Transactivating Capacity of the Oncoprotein PLAG1 by SUMOylationNoncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia proteinSumoylation of CCAAT/enhancer-binding protein alpha and its functional roles in hepatocyte differentiationIkaros SUMOylation: switching out of repressionIdentification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library.Identification of Xenopus heat shock transcription factor-2: conserved role of sumoylation in regulating deoxyribonucleic acid-binding activity of heat shock transcription factor-2 proteinsDeconstructing PML-induced premature senescence.The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugation system.Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner.The role of post-translational modifications in fine-tuning BLM helicase function during DNA repairHow ubiquitination and autophagy participate in the regulation of the cell response to bacterial infection.A new Saccharomyces cerevisiae strain with a mutant Smt3-deconjugating Ulp1 protein is affected in DNA replication and requires Srs2 and homologous recombination for its viability.Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport.Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense.SIRT1 stabilizes PML promoting its sumoylationSUMOylation of DLX3 by SUMO1 promotes its transcriptional activity.
P2860
Q21245748-BD6CF2C6-7B87-4696-9D42-2A86FCD9827BQ21558475-D6D4D3C6-AEB7-4718-B3E0-F95EBA617175Q24294867-CFF444C2-A1DE-4638-963B-F3BDFFBE912EQ24294872-C2A6ACCA-7B14-49EF-9515-D6F12AA66508Q24297146-51E86A26-2A21-4FBE-807B-E658F223FC31Q24298241-FF0EAEF0-D3BC-4A84-991A-EAC0DFB010A0Q24303540-F8B071B0-85FB-494D-866B-28DD18221416Q24313641-4BAA85E5-77E5-4300-8B20-5F1D26090DF8Q24337572-BB3ED835-BDE6-4686-94F7-AEBC3C50C6E1Q24529880-FF8B0D27-EBD3-42B7-8526-88F196A09DC5Q24534589-FFF37FD6-01F4-453E-89E8-EABCD07D3952Q24534918-0D1A4136-7BBD-44F3-A6A9-688039646900Q24556900-BB4FCFF2-7C03-4439-AD31-1338C22DF9FAQ24672260-872C0C8A-8ADC-46A6-AB2E-F857010D36D2Q24675942-131D6613-0EB1-43B3-86B7-3B667DEC03FCQ24681594-053020A0-502C-4044-A608-012A297F7D92Q24685095-FF2CC1F1-38FD-46F3-8EC8-339F2A1A1177Q24806914-55508B3A-2B54-4369-BBF3-128F7AB1E6E9Q27027918-3335923C-82AC-489E-B74E-9777CE8B0E7EQ28118825-A8D27DC4-E222-4B7E-B91B-78AFD34E5C1EQ28200940-E03A3857-3193-4872-8B8E-8661670B025CQ28205380-E8F489B9-CB56-4336-B235-F73B6C655C8EQ28205400-0CEE8591-42D4-4089-BD5F-48985C2C8F8CQ28206387-F4FDB1AD-F4FB-4C6E-9783-372B3C1D39CEQ28267812-729BE9A1-D991-4751-B03E-CDEC59A3432BQ28295561-51796A38-A874-4801-9E06-075DA4F708DCQ28569405-2308D85C-C099-4475-A47C-F0348CC986A2Q28591955-F320938C-6490-4B9F-82DF-8FAD76BDBCB1Q33301578-C84A1ABB-F4C0-4476-B2C6-540C16B26C92Q33716903-DFF2D897-7F6C-4E46-A973-069474D8B85CQ34089507-F291C672-E9EC-4345-87A9-3F6562EACD7AQ34152334-D551B564-3BB9-4EEB-86A3-86A0D8B87226Q34183048-4EE75D17-70F5-40F3-BB15-C4DF4747948EQ34244028-44E0CE1A-A1D1-4F54-AD23-A4153CD2A74EQ34286023-F7704C52-8ADE-4C8F-AA12-1AFCAE0ADD5BQ34345773-4034A28F-8D70-48B3-A86E-F36CFB31D8F2Q34637173-8802B562-C9FC-4176-B992-017BC535D670Q35024144-495DAD52-8B6E-42DA-B827-2F5CEC319FBFQ35092583-9750227B-8804-416C-A4FD-B58FB043BA1FQ35234133-E0D782FA-5F4E-4EC6-9C45-C00F94F3273E
P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
SUMO: of branched proteins and nuclear bodies.
@ast
SUMO: of branched proteins and nuclear bodies.
@en
SUMO: of branched proteins and nuclear bodies.
@nl
type
label
SUMO: of branched proteins and nuclear bodies.
@ast
SUMO: of branched proteins and nuclear bodies.
@en
SUMO: of branched proteins and nuclear bodies.
@nl
prefLabel
SUMO: of branched proteins and nuclear bodies.
@ast
SUMO: of branched proteins and nuclear bodies.
@en
SUMO: of branched proteins and nuclear bodies.
@nl
P2860
P356
P1433
P1476
SUMO: of branched proteins and nuclear bodies.
@en
P2093
P2860
P2888
P304
P356
10.1038/SJ.ONC.1204758
P407
P50
P577
2001-10-01T00:00:00Z
P5875
P6179
1009458963