The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence - sprookjes - yvandenbroek - TriplyDB

The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence

The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence

http://www.wikidata.org/entity/Q28245403

about

FOXM1 induces a global methylation signature that mimics the cancer epigenome in head and neck squamous cell carcinoma Interplay between Homeobox proteins and Polycomb repressive complexes in p16INK⁴a regulation H3K27 demethylation by JMJD3 at a poised enhancer of anti-apoptotic gene BCL2 determines ERα ligand dependency Epigenetic regulation of the INK4b-ARF-INK4a locus: in sickness and in health Covalent histone modifications--miswritten, misinterpreted and mis-erased in human cancers Long non-coding RNA ANRIL is required for the PRC2 recruitment to and silencing of p15(INK4B) tumor suppressor gene A histone demethylase is necessary for regeneration in zebrafish Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS ROS, Cell Senescence, and Novel Molecular Mechanisms in Aging and Age-Related Diseases Hypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related Diseases Oxidative stress and epigenetic regulation in ageing and age-related diseases Epigenetic plasticity: a central regulator of epithelial-to-mesenchymal transition in cancer The C. elegans H3K27 demethylase UTX-1 is essential for normal development, independent of its enzymatic activity Cellular defense against latent colonization foiled by human cytomegalovirus UL138 protein.Integrating Epigenomics into the Understanding of Biomedical Insight JMJD3 as an epigenetic regulator in development and disease A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype The histone demethylase UTX enables RB-dependent cell fate control A kinase-independent function of CDK6 links the cell cycle to tumor angiogenesis UTX and UTY demonstrate histone demethylase-independent function in mouse embryonic development Histone demethylase Jumonji D3 (JMJD3) as a tumor suppressor by regulating p53 protein nuclear stabilization A novel zinc finger protein Zfp277 mediates transcriptional repression of the Ink4a/arf locus through polycomb repressive complex 1 Alterations in chromatin are associated with increases in collagen III expression in aging nephropathy Postnatal development, maturation and aging in the mouse cochlea and their effects on hair cell regeneration.JMJD3 suppresses stem cell-like characteristics in breast cancer cells by downregulation of Oct4 independently of its demethylase activity.Epigenetic repression of p16(INK4A) by latent Epstein-Barr virus requires the interaction of EBNA3A and EBNA3C with CtBP.Histone deacetylase controls adult stem cell aging by balancing the expression of polycomb genes and jumonji domain containing 3 The localization of histone H3K27me3 demethylase Jmjd3 is dynamically regulated MIR146A inhibits JMJD3 expression and osteogenic differentiation in human mesenchymal stem cells.p53 interaction with JMJD3 results in its nuclear distribution during mouse neural stem cell differentiation.Stage-dependent and locus-specific role of histone demethylase Jumonji D3 (JMJD3) in the embryonic stages of lung development.KDM6 demethylase independent loss of histone H3 lysine 27 trimethylation during early embryonic development.The molecular balancing act of p16(INK4a) in cancer and aging.The histone demethylase Jarid1b (Kdm5b) is a novel component of the Rb pathway and associates with E2f-target genes in MEFs during senescence.MSK1 triggers the expression of the INK4AB/ARF locus in oncogene-induced senescence.Activation of Bmp2-Smad1 signal and its regulation by coordinated alteration of H3K27 trimethylation in Ras-induced senescence.Chromatin and oxygen sensing in the context of JmjC histone demethylases DNA methylation-mediated repression of miR-941 enhances lysine (K)-specific demethylase 6B expression in hepatoma cells.Polycomb group proteins: multi-faceted regulators of somatic stem cells and cancer.Aging, rejuvenation, and epigenetic reprogramming: resetting the aging clock.

P2860

Q21561022-601B5E7D-EB5B-42FA-AC35-E65373E99EDF Q24322448-9658F5E6-6958-46F6-B87D-B30E4E1EADA1 Q24322697-B72D4F8A-11A1-4FFC-B4E8-58F07B092D1F Q24604190-BEC80382-F414-4419-868D-C2B44908B3F2 Q24605342-03430999-ED72-4A8D-B909-9C32032C27E2 Q24632383-3A3C6A98-3251-4F8D-BDC7-C438B1A94ACD Q24648837-01F2FC02-E283-4346-A699-E4F09654E6A5 Q24657459-D6AC9619-216A-40A1-842A-24AE98A3F36C Q26744325-4C56AF32-43C4-4E6A-B281-3548200D05A7 Q26750099-9579883B-355B-4E7F-8F23-DB95DBF74E4B Q26991587-2B0A9728-D8AC-423C-81B2-152F37A227CD Q27022720-356D8498-1120-47AA-B26C-BEFE1AAD280B Q27334177-87CF35B0-5AB4-4445-8588-0E9BD1CBE82E Q27335160-6962DDDC-4EE6-4D75-BA38-80546E2EF4EC Q28077579-97EEADA5-4246-464D-ACC8-7ADA90E4BAD6 Q28084146-F749BCD2-9815-47B8-80F1-5D6BB6E9C2D5 Q28117127-AA4344A9-A389-4D7F-A5C1-D2C6307E1B55 Q28272073-EECA25B1-8A93-4F39-8E48-5198A2349BB9 Q28296641-D87B1D5E-A0E5-40FE-9B6C-00CE80E9B6F1 Q28484095-FF659574-A94A-4F5E-A59B-31691FF66E71 Q28484242-590BD48E-37B7-4255-8955-4711AAA1F8F6 Q28506253-FFC4FBD6-3976-4AA4-9D11-7132BA79010C Q28580895-F2A12E2A-E932-4124-AFC2-8495A97CFA8D Q30442295-3B8B0419-74F2-4998-9183-A34D467071EA Q33591745-7739EAD4-02E4-4577-B3B6-C5DE82DB1766 Q33604848-9CA7F531-6634-41C3-B0A4-6CB53D235300 Q33716041-326256CD-B6C1-4CF9-9141-A788DC5A4D4B Q33784590-B76FAFAC-ACFA-4CAB-A58B-B6518DC3A76C Q33852976-81DCCBA0-322C-4251-842C-F85E1E1B04F8 Q33869591-2874D751-DE31-4806-9B41-D0CE863D49BC Q33981809-1213FFD6-6553-43C6-A05F-C1934ADC1289 Q34015127-624CFCCE-FAB7-4C0A-9780-31EE7835240A Q34038585-363E4746-8691-4A1A-BC47-FF34BE28B1F4 Q34042999-B9D5F14B-BCFB-41F6-A3CF-3026714D6D30 Q34047137-C9F80EBA-548F-4498-ACE0-C96CCA43C2AA Q34071417-2BD523B6-D577-4DEE-998A-5B68C16C824D Q34103385-9AE02026-742C-4E44-A61C-B439375C5696 Q34107419-BE48E8AF-2748-4102-908B-45F8AAAAB6EE Q34134903-055146B6-7CFA-494C-8DAD-C9EEC2926FA9 Q34248727-1DEC8091-184A-46F3-9B40-A3ACEA972171

P2860

The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence

http://www.wikidata.org/entity/Q28245403

description

2009 nî lūn-bûn

@nan

2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@ast

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@en

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@nl

type

label

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@ast

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@en

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@nl

prefLabel

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@ast

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@en

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@nl

P1433

Q28245403-E75CB982-A4E1-440B-8116-296AFA4FEB06

P1476

Q28245403-B85AB268-103F-406F-B1E1-D2947D2F38FC

P2093

Q28245403-777CD1F3-E152-4B1E-AB7F-DE6689CD5013

Q28245403-8F153349-5276-48E0-9AB5-FD2CC1EE3F18

Q28245403-B238630A-BDCC-4549-8AD0-CAB7C06B37F4

Q28245403-C563E796-9428-482E-800F-9290E538B206

Q28245403-DBB8013E-77A9-4B48-B0EA-11D4FC4389CB

P2860

Q28245403-10F76440-B27C-41F3-A441-BDC5786EF6EF

Q28245403-14624696-D8E0-4FE2-94C3-C2BF48D442DA

Q28245403-24BBBAA2-CE52-4D13-B2E8-C252996112E6

Q28245403-26EFBD3D-4165-4AC5-A55D-866895754E26

Q28245403-2BD05E15-6097-4B33-99FA-716112ADE50C

Q28245403-2D32736C-2061-47AB-B9C0-3A996F0DDA06

Q28245403-385407A9-A680-45CF-AADB-659ADEFD67D9

Q28245403-55922093-4762-4AAD-B1CB-97120D6C7CE0

Q28245403-56292C66-E416-4BB7-A6AB-7FB4880C3257

Q28245403-5F507E0D-110A-44C7-A987-13D854BD59B4

P304

Q28245403-F6B797CB-67F2-451D-9B1D-28F8207F5E3D

P31

Q28245403-F5951EB6-C3C0-4E92-8E42-11FF4CF58830

P3181

Q28245403-66030924-246B-4F85-B019-A95581441B74

P356

Q28245403-E339FD13-AF65-4DEA-9003-8828108B3A7E

P407

Q28245403-0061359E-0C05-45C5-BA36-3FE537EE894C

P433

Q28245403-034BE677-A428-4B52-8AE8-527B667ACD4D

P478

Q28245403-63E094E8-7179-4B13-99A6-6BCEE807F1F1

P50

Q28245403-0DB01B75-C4B5-4A9D-A966-3CD60C00078C

Q28245403-E8465E1D-92ED-4705-82EA-DFBBA8259370

P577

Q28245403-0EA01DC6-7CD5-494A-A80D-C148293DFFBA

P5875

Q28245403-9CDC3800-E6D3-43DE-AE04-C562DA4B970A

P698

Q28245403-4FBDF47A-FB62-4F0C-A6D6-33A09AD4A564

P932

Q28245403-0809A238-99F5-4A70-A9B3-A4D740E0D8A1

P3181

P356

P1433

Genes & Development

P1476

The H3K27me3 demethylase JMJD3 ...... and stress-induced senescence

@en

P2093

Gitte Andersen

http://www.w3.org/2001/XMLSchema#string

Jesper Christensen

http://www.w3.org/2001/XMLSchema#string

Karl Agger

http://www.w3.org/2001/XMLSchema#string

Lise Rudkjaer

http://www.w3.org/2001/XMLSchema#string

Paul A C Cloos

http://www.w3.org/2001/XMLSchema#string

P2860

Bypass of senescence by the polycomb group protein CBX8 through direct binding to the INK4A-ARF locus

The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells

The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing

The INK4a/ARF network in tumour suppression

UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development

A histone H3 lysine 27 demethylase regulates animal posterior development

Mutations in the p53 gene occur in diverse human tumour types

SMRT-mediated repression of an H3K27 demethylase in progression from neural stem cell to neuron

Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease

Oxygen sensitivity severely limits the replicative lifespan of murine fibroblasts

P304

1171-6

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1736776

http://www.w3.org/2001/XMLSchema#string

P356

10.1101/GAD.510809

http://www.w3.org/2001/XMLSchema#string

P407

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

23

http://www.w3.org/2001/XMLSchema#string

P50

Kristine Williams

P577

2009-05-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

24436040

http://www.w3.org/2001/XMLSchema#string

P698

19451217

http://www.w3.org/2001/XMLSchema#string

P932

2685535

http://www.w3.org/2001/XMLSchema#string