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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

DOT1 Dot1p

Dot1, Dot1p, DOT1L
The protein encoded by this gene is a histone methyltransferase that methylates lysine-79 of histone H3. It is inactive against free core histones, but shows significant histone methyltransferase activity against nucleosomes. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: Histone, MLL, CAN, SET, POLYMERASE
Papers using Dot1 antibodies
Adiponectin reduces proteinuria in streptozotocin-induced diabetic Wistar rats
Maeda Shiro, In PLoS ONE, 2010
... Belmont, MA, USA), anti-Af9 (Bethyl Laboratory, Montgomery, TX, USA), anti-di-methyl H3 K79 (H3m2K79, abcam), and anti-Dot1l (abcam and Bethyl) antibodies, mouse ...
Identification of a novel isoform of Cdk9.
Zeleznik-Le Nancy, In PLoS Biology, 2002
... In addition, the cDNAs of ENL, AF4, AF5, CYCT2, and Dot1l were inserted into the general expression vectors pcDNA3.0
Papers on Dot1
DOT1L histone methyltransferase regulates the expression of BCAT1 and is involved in sphere formation and cell migration of breast cancer cell lines.
Suzuki et al., Kanazawa, Japan. In Biochimie, Feb 2016
UNASSIGNED: DOT1L is a histone H3 lysine 79 (H3K79) methyltransferase mainly implicated in leukemia.
Resetting the epigenome for heart regeneration.
Hudson et al., Brisbane, Australia. In Semin Cell Dev Biol, Feb 2016
BMP, bone morphogenetic protein; Bvht, Braveheart; CBP, CREB-binding protein; Cdkn, cyclin dependent kinase inhibitor; DOT1L, disruptor of telomeric silencing-1; DNMTs, DNA methyltransferases; eRNAs, enhancer RNAs; ESCs, embryonic stem cells; FGF, fibroblast growth factor; FOX, Forkhead box; Gcn5, general control of amino acid synthesis protein 5; HATs, histone acetyl transferases; HDACs, histone deacteylases; H3K27, histone 3, lysine 27; HMTs, histone methyltransferases; Jmj, Jumonji; JMJD3, Jumonji domain-containing protein 3; KDMs, histone lysine demethylases; lncRNAs, long non-coding RNAs; Mhrt, Myheart; miRNAs, microRNAs; Myh, myosin heavy chain; PRC2, polycomb repressive complex 2; PSCs, pluripotent stem cells; PTM, post-translational modification; SIRTs, Sirtuins; SMYD1, SET and MYND domain containing 1; Srf, serum response factor; TET, Ten-eleven translocation; TGF-β, transforming growth factor beta; TFs, transcription factors; UTX, ubiquitously transcribed tetratricopeptide repeat, X chromosome.
The upstreams and downstreams of H3K79 methylation by DOT1L.
van Leeuwen et al., Amsterdam, Netherlands. In Chromosoma, Feb 2016
An example of this is DOT1L, the enzyme that can mono-, di-, and trimethylate the nucleosome core on lysine 79 of histone H3 (H3K79).
Metabolism and disposition of the DOT1L inhibitor, pinometostat (EPZ-5676), in rat, dog and human.
Chesworth et al., Cambridge, United States. In Cancer Chemother Pharmacol, Jan 2016
PURPOSE: The metabolism and disposition of the first-in-class DOT1L inhibitor, EPZ-5676 (pinometostat), was investigated in rat and dog.
MLL-Rearranged Acute Lymphoblastic Leukemias Activate BCL-2 through H3K79 Methylation and Are Sensitive to the BCL-2-Specific Antagonist ABT-199.
Konopleva et al., Houston, United States. In Cell Rep, Jan 2016
We demonstrate that MLL/AF4 specifically upregulates the BCL-2 gene but not other BCL-2 family members via DOT1L-mediated H3K79me2/3.
The Double-Strand Break Landscape of Meiotic Chromosomes Is Shaped by the Paf1 Transcription Elongation Complex in Saccharomyces cerevisiae.
Shinohara et al., Ōsaka, Japan. In Genetics, Jan 2016
Set1-dependent histone H3K4 methylation and Dot1-dependent H3K79 methylation play important roles in this process in budding yeast.
Challenges in profiling and lead optimization of drug discovery for methyltransferases.
Horiuchi, United States. In Drug Discov Today Technol, Nov 2015
Protein methyltransferases are one of the target classes which have gained attention as potential therapeutic targets after promising results of inhibitors for EZH2 and DOT1L in clinical trials.
Overview: A New Era of Cancer Genome in Myeloid Malignancies.
Kiyoi, Nagoya, Japan. In Oncology, Nov 2015
Dr. Eytan Stein showed that there are promising anti-leukemia effects of IDH2 inhibitor, AG-221, and DOT1L inhibitor, EPZ-5676, based on early-phase clinical studies.
Recent progress in the treatment of infant acute lymphoblastic leukemia.
Tomizawa, Tokyo, Japan. In Pediatr Int, Oct 2015
Recent progress has clarified the unique mechanism of MLL-r ALL: the aberrant methylation and histone modifications via DOT1L and other related molecules by MLL fusion proteins lead to leukemogenetic gene expression, thus to overt leukemia.
NF-κB activation impairs somatic cell reprogramming in ageing.
López-Otín et al., Oviedo, Spain. In Nat Cell Biol, Aug 2015
Conversely, ageing-associated NF-κB hyperactivation impairs the generation of iPSCs by eliciting the reprogramming repressor DOT1L, which reinforces senescence signals and downregulates pluripotency genes.
DOT1L inhibits SIRT1-mediated epigenetic silencing to maintain leukemic gene expression in MLL-rearranged leukemia.
Armstrong et al., New York City, United States. In Nat Med, Apr 2015
This gene expression program is dependent on the disruptor of telomeric silencing 1-like histone 3 lysine 79 (H3K79) methyltransferase DOT1L, and small-molecule DOT1L inhibitors show promise as therapeutics for these leukemias.
DOTting the path to doom: how acceleration of histone methylation leads to leukemia.
Slany et al., Erlangen, Germany. In Cancer Cell, 2015
In this issue of Cancer Cell, Deshpande and colleagues demonstrate that AF10, an interaction partner of the histone methyltransferase DOT1L, is essential for efficient H3K79 methylation, thus regulating HOX-gene transcription and transformation in myeloid leukemia.
AF10 regulates progressive H3K79 methylation and HOX gene expression in diverse AML subtypes.
Armstrong et al., Boston, United States. In Cancer Cell, 2015
We show that H3K79 methyltransferase activity as well as H3K79me1-to-H3K79me2 conversion is regulated by the DOT1L cofactor AF10.
The histone methyltransferase DOT1L: regulatory functions and a cancer therapy target.
Liu et al., Australia. In Am J Cancer Res, 2014
DOT1L is a unique histone methyltransferase that targets the histone H3 lysine 79 (H3K79) residue for mono-, di- and tri- methylation.
AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation.
Shi et al., Beijing, China. In Cell, 2014
ChIP-seq experiments revealed a strong colocalization of AF9 and H3K9 acetylation genome-wide, which is important for the chromatin recruitment of the H3K79 methyltransferase DOT1L.
Histone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2.
Allis et al., New York City, United States. In J Biol Chem, 2012
Data show that histone monoubiquitylation H2Aub did not influence histone methyltransferase Dot1L activity.
Genome-wide association and functional studies identify the DOT1L gene to be involved in cartilage thickness and hip osteoarthritis.
van Meurs et al., Rotterdam, Netherlands. In Proc Natl Acad Sci U S A, 2012
Immunohistochemical staining of the DOT1L protein in mouse limbs supports a role for DOT1L in chondrogenic differentiation and adult articular cartilage.
Bat3 facilitates H3K79 dimethylation by DOT1L and promotes DNA damage-induced 53BP1 foci at G1/G2 cell-cycle phases.
Wang et al., Durham, United States. In Embo J, 2012
These findings identify a novel role for Bat3 in regulating DOT1L function, which plays a critical role in DNA damage response.
Deficiency of H3K79 histone methyltransferase Dot1-like protein (DOT1L) inhibits cell proliferation.
Kim et al., Seoul, South Korea. In J Biol Chem, 2012
down-regulation of DOT1L-mediated H3K79 methylation disturbs proliferation of human cells
AF17 facilitates Dot1a nuclear export and upregulates ENaC-mediated Na+ transport in renal collecting duct cells.
Zhang et al., Houston, United States. In Plos One, 2010
AF17 promotes Dot1a nuclear export and upregulates basal, but not aldosterone-stimulated ENaC expression, leading to an increase in ENaC-mediated Na(+) transport in renal collecting duct cells.
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