Dot1l methylation epigenetics histones

Show results for

Unknown (2)
Proteomics (2)
Genomics (1)
Transcriptomics (1)

Organisms

Mus musculus (2)
Photobacterium profundum SS9 (2)
Galloanserae (2)
Malassezia sympodialis ATCC 42132 (2)
Deltaproteobacteria bacterium RIFCSPLOWO2_12_FULL_50_11 (2)
Esocidae (2)
Leishmania braziliensis MHOM/BR/75/M2904 (2)
Potentilla saundersiana (2)
Spirometra erinaceieuropaei (2)
Betaproteobacteria bacterium RIFCSPLOWO2_02_64_14 (2)
Cyprinidae (2)
Euzebya tangerina (2)
Toxoplasma gondii type III (2)
Pseudotsuga menziesii var. menziesii (2)
Phasianidae (2)
Priestia megaterium (2)
Noccaea caerulescens (2)
Hebomoia glaucippe (2)
Francisella philomiragia FSC154 (2)
Emiliania (2)
Haptophyta (2)
Strigomonas culicis (2)
Lactococcus cremoris subsp. cremoris UC509.9 (2)
Pseudomonas syringae pv. aptata (2)
Eubacteriales (2)
zebrafish metagenome (2)
vertebrate environmental sample (2)
Lysiphlebus fabarum (2)
Trichomonas gallinae (2)
soil bacterium TS1114R (2)

Repository

biostudies-arrayexpress (2)
pride (2)

Tissue

Permanent cell line cell (1)
Cell culture (1)
Epithelial cell (1)

Technology Type

Mass Spectrometry (2)
Bottom-up proteomics (1)
Shotgun proteomics (1)

Publication Date

2011 (2)
2024 (1)
2018 (1)

Study type

ChIP-seq (1)
Transcription profiling by array (1)

Release Date

2011 (2)
2019 (1)
2014 (1)

Lab affiliation

Structural Genomics Consortium (SGC), Chemical biology Group, University of Oxford, United Kingdom. also affiliated with: Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, United Kingdom. (1)
Division of Systems Medicine, Imperial College London (1)

Modification

N6-dimethyl-L-lysine (1)

Previous page
1 / 1
You're on page 1
Next page

Sort by:

Relevance

Page size

Tracking DOT1L Methyltransferase Activity by Stable Isotope Labelling Using a Selective Synthetic Co-Factor

Histone methylation is a post-translational modification (PTM) regulating gene expression. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (13CD3-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity b...

ORGANISM(S): Homo sapiens (Human)

2024-06-28 | PXD052790 | Pride

Dot1l methylation epigenetics histones

Expression changes after loss of Dot1l in murine MLL-AF9 leukemia cells

MLL-fusions may induce leukemogenic gene expression programs by recruiting the histone H3K79 methyltransferase to MLL-target promoters. We evaluated gene expression changes after cre-mediated loss of Dot1l in leukemia cells obtained from mice injected with MLL-9 transformed lineage negative bone mar...

ORGANISM(S): Mus musculus

2011-09-12 | E-GEOD-25911 | biostudies-arrayexpress

Epigenetic profiling of hematopoietic stem cells and leukemia stem cells

The histone 3 lysine 79 (H3K79) methyltransferase Dot1l has been implicated in the development of leukemias bearing translocations that involve the Mixed Lineage Leukemia (MLL) gene. We identified the MLL-fusion targets in a murine MLL-AF9 leukemia model, and conducted epigenetic profiling for H3K7...

ORGANISM(S): Mus musculus

2011-09-13 | E-GEOD-29130 | biostudies-arrayexpress

AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation.

Not available

S-EPMC4344132 | biostudies-literature

A chemical biology toolbox to study protein methyltransferases and epigenetic signaling.

Not available

S-EPMC6318333 | biostudies-literature

A Chemical Biology Toolbox to Study Protein Methyltransferases and Epigenetic Signaling

Protein methyltransferases (PMTs) comprise a major class of epigenetic regulatory enzymes with therapeutic relevance. Here we present a collection of chemical probes and associated reagents and data to elucidate the function of human and murine PMTs in cellular studies. Our collection provides inhib...