Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase
about
Cullin-RING ubiquitin ligases: global regulation and activation cyclesThe histone variant macroH2A1 marks repressed autosomal chromatin, but protects a subset of its target genes from silencingTumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal mitosis in mammalian cellsUbiquitylation-dependent localization of PLK1 in mitosisWeak but uniform enrichment of the histone variant macroH2A1 along the inactive X chromosomeStructure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1bmacroH2A1 histone variant represses rDNA transcriptionUbiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressorStructure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complexSPOP promotes tumorigenesis by acting as a key regulatory hub in kidney cancerA novel role for Xist RNA in the formation of a repressive nuclear compartment into which genes are recruited when silencedThe Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimerExpression and functionality of histone H2A variants in cancerStructures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin LigasesIs there more to BARD1 than BRCA1?Bood POZ containing gene type 2 is a human counterpart of yeast Btb3p and promotes the degradation of terminal deoxynucleotidyltransferaseSwitches, excitable responses and oscillations in the Ring1B/Bmi1 ubiquitination systemPcif1 modulates Pdx1 protein stability and pancreatic β cell function and survival in miceConstitutive turnover of cyclin E by Cul3 maintains quiescenceUbiquitination and degradation of ribonucleotide reductase M1 by the polycomb group proteins RNF2 and Bmi1 and cellular response to gemcitabineMacroH2A histone variants act as a barrier upon reprogramming towards pluripotencyCilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conservedMouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatinEvolution from XIST-independent to XIST-controlled X-chromosome inactivation: epigenetic modifications in distantly related mammalsPolycomb silencers control cell fate, development and cancerHistone variant macroH2A confers resistance to nuclear reprogramming.Transcription of the rat testis-specific Rtdpoz-T1 and -T2 retrogenes during embryo development: co-transcription and frequent exonisation of transposable element sequences.A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila.Ubiquitin E3 ligase Ring1b/Rnf2 of polycomb repressive complex 1 contributes to stable maintenance of mouse embryonic stem cellsThe Polycomb protein and E3 ubiquitin ligase Ring1B harbors an IRES in its highly conserved 5' UTRHistone variants: emerging players in cancer biology.The histone variant MacroH2A1 regulates target gene expression in part by recruiting the transcriptional coregulator PELP1.The U2AF1S34F mutation induces lineage-specific splicing alterations in myelodysplastic syndromes.Histone variant macroH2A1 deletion in mice causes female-specific steatosis.The histone H2A variant macroH2A1 does not localize to the centrosome.The Mbd1-Atf7ip-Setdb1 pathway contributes to the maintenance of X chromosome inactivation.X chromosome inactivation and differentiation occur readily in ES cells doubly-deficient for macroH2A1 and macroH2A2.QKI-mediated alternative splicing of the histone variant MacroH2A1 regulates cancer cell proliferationAssociation of BMI1 with polycomb bodies is dynamic and requires PRC2/EZH2 and the maintenance DNA methyltransferase DNMT1
P2860
Q21203558-7F3E85B9-BE73-4658-B7B8-494450AF784BQ22001529-D1244BA1-2BAF-4B82-AC8C-15797136A4D7Q24303428-2BE9C7CE-BAA7-4C31-A48D-6D0FCBADFDC5Q24317195-AA720FE5-6EE3-4482-BEBE-DF622BE6DC28Q24322683-504B2F9B-CA5E-43A7-96CA-EB13B426918CQ24336021-3A3D3EB0-71AE-48AF-B97B-0ADF2E680C93Q24337331-721541FB-AE01-43D3-8CC9-5D03BC7EAD5DQ24337356-5CC54D67-5A20-4B0F-AE56-CCA80CA735A5Q24337508-D86F8979-B1BC-451F-9511-F76093BE562CQ24337578-359B1FCC-BB6C-4307-A599-344744F237D5Q24339492-46CA08EE-7AB5-4E94-939E-75E408546332Q24672840-C43567E3-804E-4BAA-9409-A274D74BA74DQ24685712-CAE1228D-0BA5-4B3B-B6C7-D6945561A5ADQ27014044-61F617C8-8279-4B48-A78E-3A8EE87E9ECFQ27657740-C9EEE158-0EC9-4692-8E71-E3F64AA451CEQ28236135-DDD57BE1-5238-46CF-92FC-2449C5D1073AQ28277430-2262C4AD-F25C-4445-93B0-45643C444334Q28478440-B668C4CB-666B-4D75-B11B-F9F41C69EF29Q28506102-3DFCFE41-355F-4685-B4EE-569B5559F61BQ28506695-62467E08-DBF7-4CA2-A2A1-B59DB05342AEQ28540690-205BF91E-A5AC-4995-916D-F75A5F8A3A4CQ28571328-679450F4-4259-48A3-AED2-4C45015703C0Q28585804-1753B23A-C6E3-4AAA-8F14-9862702D32F7Q28587001-E497E9AF-477A-4672-97F1-E8CA36941C75Q28740797-EB4460BB-7E3C-4113-8ABE-08A40D4DD318Q29619697-E5AC7832-0C68-4977-B9B4-D226C65390E1Q30501191-58E64EDB-951D-492D-B97B-813DDEA6A872Q30870995-BE4CD404-E507-4D77-B215-24B3AF2A8437Q33299579-21A14128-9493-4690-B136-584D2B565631Q33336429-88D4BD16-98A4-4FDD-B666-742200BF28CCQ33340261-7ACE9304-E714-4819-8E97-638C075C8DB5Q33630867-153643D9-3910-43FA-8D4A-5ED111D1910DQ33743684-27076DD4-2558-4EBD-8371-2406AC0DA14EQ33746465-E7012D49-DBC1-4C8D-8ABF-A268D027C02DQ33803202-43B480F0-82C0-42A0-AD51-D10B53C75195Q33833996-CDA3982E-45E7-4286-B540-56D506F91407Q33904558-94099159-225B-4063-8EBC-E8C565608F7DQ33954976-445B2715-18D9-4914-A753-10E0A4C398BBQ34208257-C864B732-3DAB-4439-98CB-5CBB44741F13Q34230837-7EA690F8-CB45-4136-9987-B7806001471E
P2860
Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase
description
2005 nî lūn-bûn
@nan
2005 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@ast
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en-gb
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@nl
type
label
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@ast
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en-gb
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@nl
prefLabel
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@ast
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en-gb
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@nl
P2093
P2860
P3181
P356
P1476
Stable X chromosome inactivati ...... LLIN3/SPOP ubiquitin E3 ligase
@en
P2093
Anders H Lund
Barbara Panning
Dmitri A Nusinow
Els Verhoeven
Erwin Boutsma
Inhua Muijrers
Inmaculada Hernández-Muñoz
Maarten van Lohuizen
Petra van der Stoop
York Marahrens
P2860
P304
P3181
P356
10.1073/PNAS.0408918102
P407
P577
2005-05-16T00:00:00Z