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Potent inhibition of DOT1L as treatment of MLL-fusion leukemia
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scholarly article
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title
Potent inhibition of DOT1L as treatment of MLL-fusion leukemia
(English)
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main subject
cell biology
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leukemia
1 reference
based on heuristic
inferred from title
author name string
Scott R Daigle
series ordinal
1
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Edward J Olhava
series ordinal
2
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Carly A Therkelsen
series ordinal
3
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Aravind Basavapathruni
series ordinal
4
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Lei Jin
series ordinal
5
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P Ann Boriack-Sjodin
series ordinal
6
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Christina J Allain
series ordinal
7
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Christine R Klaus
series ordinal
8
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Alejandra Raimondi
series ordinal
9
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Margaret Porter Scott
series ordinal
10
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Nigel J Waters
series ordinal
11
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Richard Chesworth
series ordinal
12
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Mikel P Moyer
series ordinal
13
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Robert A Copeland
series ordinal
14
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Victoria M Richon
series ordinal
15
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Roy M Pollock
series ordinal
16
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language of work or name
English
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publication date
8 August 2013
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published in
Blood
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volume
122
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page(s)
1017-25
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issue
6
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cites work
Conformational adaptation drives potent, selective and durable inhibition of the human protein methyltransferase DOT1L
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PubMed Central
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20 March 2017
Selective Inhibitors of Histone Methyltransferase DOT1L: Design, Synthesis, and Crystallographic Studies
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PubMed Central
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20 March 2017
Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom)
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20 March 2017
A higher-order complex containing AF4 and ENL family proteins with P-TEFb facilitates oncogenic and physiologic MLL-dependent transcription
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20 March 2017
hDOT1L links histone methylation to leukemogenesis
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PubMed Central
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20 March 2017
Characterization of the DOT1L network: implications of diverse roles for DOT1L
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PubMed Central
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20 March 2017
Misguided transcriptional elongation causes mixed lineage leukemia
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20 March 2017
MLL targets SET domain methyltransferase activity to Hox gene promoters
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20 March 2017
Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
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PubMed Central
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20 March 2017
MLL translocations, histone modifications and leukaemia stem-cell development
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PubMed Central
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7 April 2017
ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation
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7 April 2017
Bromo-deaza-SAH: a potent and selective DOT1L inhibitor
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PubMed Central
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29 September 2017
Leukemic transformation by the MLL-AF6 fusion oncogene requires the H3K79 methyltransferase Dot1l
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PubMed Central
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29 September 2017
Abrogation of MLL-AF10 and CALM-AF10-mediated transformation through genetic inactivation or pharmacological inhibition of the H3K79 methyltransferase Dot1l.
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PubMed Central
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29 September 2017
Synthesis and structure-activity relationship investigation of adenosine-containing inhibitors of histone methyltransferase DOT1L
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PubMed Central
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29 September 2017
The pathogenesis of mixed-lineage leukemia
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29 September 2017
Function of leukemogenic mixed lineage leukemia 1 (MLL) fusion proteins through distinct partner protein complexes
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29 September 2017
MLL-rearranged leukemia is dependent on aberrant H3K79 methylation by DOT1L.
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PubMed Central
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29 September 2017
Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor.
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PubMed Central
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29 September 2017
The diverse functions of Dot1 and H3K79 methylation.
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PubMed Central
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29 September 2017
DOT1L, the H3K79 methyltransferase, is required for MLL-AF9-mediated leukemogenesis
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3739029
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29 September 2017
Requirement for Dot1l in murine postnatal hematopoiesis and leukemogenesis by MLL translocation.
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PubMed Central
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29 September 2017
Histone H3 lysine 79 methyltransferase Dot1 is required for immortalization by MLL oncogenes
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11q23/MLL acute leukemia : update of clinical aspects
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MLL-AF9 and MLL-ENL alter the dynamic association of transcriptional regulators with genes critical for leukemia
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MLL-AF9-induced leukemogenesis requires coexpression of the wild-type Mll allele.
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PubMed Central
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PubMed Central
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29 September 2017
H3K79 methylation profiles define murine and human MLL-AF4 leukemias
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3739029
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29 September 2017
A role for the MLL fusion partner ENL in transcriptional elongation and chromatin modification
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3739029
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29 September 2017
The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling
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PubMed Central
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29 September 2017
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29 September 2017
Dot1a-AF9 complex mediates histone H3 Lys-79 hypermethylation and repression of ENaCalpha in an aldosterone-sensitive manner
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reference URL
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29 September 2017
Binding to nonmethylated CpG DNA is essential for target recognition, transactivation, and myeloid transformation by an MLL oncoprotein
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29 September 2017
MLL: a histone methyltransferase disrupted in leukemia
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reference URL
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29 September 2017
The oncogenic capacity of HRX-ENL requires the transcriptional transactivation activity of ENL and the DNA binding motifs of HRX.
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3739029
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29 September 2017
11q23 translocations split the "AT-hook" cruciform DNA-binding region and the transcriptional repression domain from the activation domain of the mixed-lineage leukemia (MLL) gene
1 reference
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PubMed Central
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29 September 2017
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29 September 2017
Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3739029
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2 June 2018
Leukemogenic MLL fusion proteins bind across a broad region of the Hox a9 locus, promoting transcription and multiple histone modifications.
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3739029
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27 November 2018
Evaluation of enzyme inhibitors in drug discovery. A guide for medicinal chemists and pharmacologists
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based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1182/BLOOD-2013-04-497644
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
686563
OpenCitations bibliographic resource ID
686563
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
686563
PMCID
3739029
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
686563
PubMed ID
23801631
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
686563
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