Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes

Gillian L. Dalgliesh; Kyle Furge; Chris Greenman; Lina Chen; Graham R. Bignell; Adam P. Butler; Helen Davies; Sarah Edkins; Claire Hardy; Calli Latimer; Jon W. Teague; J. M. Andrews; Syd Barthorpe; Dave Beare; Gemma Buck; Peter J. Campbell; Simon Forbes; Mingming Jia; David Jones; Henry Knott; Chai Yin Kok; King Wai Lau; Catherine Leroy; Meng‐Lay Lin; David J. McBride; Mark Maddison; Simon Maguire; Kirsten McLay; Andrew Menzies; Tatiana Mironenko; Lee Mulderrig; Laura Mudie; Sarah O’Meara; Erin Pleasance; Arjunan Rajasingham; Rebecca Shepherd; Raffaella Smith; Lucy Stebbings; Philip Stephens; Gurpreet Tang; Patrick Tarpey; Kelly Turrell; Karl Dykema; Sok Kean Khoo; David Petillo; Bill Wondergem; John Anema; Richard J. Kahnoski; Bin Tean Teh; Michael R. Stratton; P. Andrew Futreal

doi:10.1038/nature08672

Keywords

DemethylaseBiologyGeneticsHistoneHistone H3GeneCancer epigeneticsHistone methyltransferaseMutationEpigeneticsCancer research

Affiliated Institutions

Related Publications

SetDB1 contributes to repression of genes encoding developmental regulators and maintenance of ES cell state

Steve Bilodeau , Michael H. Kagey , Garrett M. Frampton +2 more

Transcription factors that play key roles in regulating embryonic stem (ES) cell state have been identified, but the chromatin regulators that help maintain ES cells are less we...

2009 Genes & Development 341 citations

Enhancer-associated H3K4 monomethylation by Trithorax-related, the <i>Drosophila</i> homolog of mammalian Mll3/Mll4

Hans-Martin Herz , Man Mohan , Alexander S. Garruss +6 more

Monomethylation of histone H3 on Lys 4 (H3K4me1) and acetylation of histone H3 on Lys 27 (H3K27ac) are histone modifications that are highly enriched over the body of actively t...

2012 Genes & Development 384 citations

Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications

Suming Huang , Michael D. Litt , Gary Felsenfeld

PRMT1 is a histone methyltransferase that methylates Arg3 on histone H4. When we used siRNA to knock down PRMT1 in an erythroid cell line, it resulted in nearly complete loss of...

2005 Genes & Development 247 citations

Spatial Distribution of Di- and Tri-methyl Lysine 36 of Histone H3 at Active Genes

Andrew J. Bannister , Robert Schneider , Fiona A. Myers +3 more

Methylation of lysine 4 of histone H3 (K4/H3) is linked to transcriptional activity, whereas methylation of K9/H3 is tightly associated with gene inactivity. These are well char...

2005 Journal of Biological Chemistry 445 citations

Translating the Histone Code

Thomas Jenuwein , C. David Allis

Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone ami...

2001 Science 9575 citations

Publication Info

Year: 2010
Type: article
Volume: 463
Issue: 7279
Pages: 360-363
Citations: 1167
Access: Closed

External Links

View on DOI.org

Social Impact

Altmetric

Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes

PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

1167

OpenAlex

Cite This

APA Style

                            
                                
                                    Gillian L. Dalgliesh, 
                                
                                    Kyle Furge, 
                                
                                    Chris Greenman
                                
                                et al.
                            
                            (2010). 
                            Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes. 
                            Nature
                            , 463
                            (7279)
                            , 360-363.
                            https://doi.org/10.1038/nature08672
                        

Identifiers

DOI: 10.1038/nature08672