ArticleACS chemical biology2016
The L3MBTL3 Methyl-Lysine Reader Domain Functions As a Dimer.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 5 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Gene expression profiling of upregulated mRNAs in granulosa cells of bovine ovulatory follicles following stimulation with hCG.Reproductive biology and endocrinology : RB&E · 2017Article
- Chemical modulators for epigenome reader domains as emerging epigenetic therapies for cancer and inflammation.Current opinion in chemical biology · 2017Review
- Integrative genomic analysis implicates limited peripheral adipose storage capacity in the pathogenesis of human insulin resistance.Nature genetics · 2017Article
- Chemical probes for methyl lysine reader domains.Current opinion in chemical biology · 2016Review
- Chemical genetics approaches for selective intervention in epigenetics.Current opinion in chemical biology · 2016Review
Corrections and comments
- Retraction · 2017-12-19Falsification/Fabrication of Image · Investigation by Company/Institution · Investigation by Journal/Publisher · Misconduct - Official Investigation(s) and/or Finding(s) · Misconduct by Author ·
- Commented on by
- Retracted
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
L3MBTL3 recognizes mono- and dimethylated lysine residues on histone tails. The recently reported X-ray cocrystal structures of the chemical probe UNC1215 and inhibitor UNC2533 bound to the methyl-lysine reading MBT domains of L3MBTL3 demonstrate a unique and flexible 2:2 dimer mode of recognition. In this study, we describe our in vitro analysis of L3MBTL3 dimerization via its MBT domains and additionally show that this dimerization occurs within a cellular context in the absence of small molecule ligands. Furthermore, mutations to the first and second MBT domains abrogated L3MBTL3 dimerization both in vitro and in cells. These observations are consistent with the hypothesis that L3MBTL3 engages methylated histone tails as a dimer while carrying out its normal function and provides an explanation for the presence of repeated MBT domains within L3MBTL3.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.