Evidence map›Paper›PMID 25489787›Full record

ArticleACS chemical biology2015

Degron protease blockade sensor to image epigenetic histone protein methylation in cells and living animals.

Thillai V Sekar, Kira Foygel, Rammohan Devulapally, Ramasamy Paulmurugan

Open access · bronzeAbstract read
In one paragraph

Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 35% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Coordinated histone modifications and chromatin reorganization in a single cell revealed by FRET biosensors.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  3. Epigenetic mechanisms underlying nervous system diseases.Handbook of clinical neurology · 2018
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Thillai V SekarMolecular Imaging Program at Stanford, Bio-X Program, Stanford University School of Medicine , Stanford, California, United States.
Kira Foygel
Rammohan Devulapally
Ramasamy Paulmurugan
Stanford University · US

Funding

Molecular Sensors for Imaging Histone Methylations in Living AnimalsR01CA161091 · NCI · STANFORD UNIVERSITY · PI PAULMURUGAN, RAMASAMY · 2012 to 2015
$1.3M
NCI NIH HHS R01 CA161091NCI NIH HHS R01CA161091
6 · The paper itself

Abstract

Lysine methylation of histone H3 and H4 has been identified as a promising therapeutic target in treating various cellular diseases. The availability of an in vivo assay that enables rapid screening and preclinical evaluation of drugs that potentially target this cellular process will significantly expedite the pace of drug development. This study is the first to report the development of a real-time molecular imaging biosensor (a fusion protein, [FLuc2]-[Suv39h1]-[(G4S)3]-[H3-K9]-[cODC]) that can detect and monitor the methylation status of a specific histone lysine methylation mark (H3-K9) in live animals. The sensitivity of this sensor was assessed in various cell lines, in response to down-regulation of methyltransferase EHMT2 by specific siRNA, and in nude mice with lysine replacement mutants. In vivo imaging in response to a combination of methyltransferase inhibitors BIX01294 and Chaetocin in mice reveals the potential of this sensor for preclinical drug evaluation. This biosensor thus has demonstrated its utility in the detection of H3-K9 methylations in vivo and potential value in preclinical drug development.

Indexed as

Epigenesis, GeneticProtease InhibitorsAnimalsBiosensing TechniquesCell Line, TumorDrug Evaluation, PreclinicalHistone-Lysine N-MethyltransferaseHistonesHumansLeucineLysineMethylationMiceOptical ImagingPluripotent Stem CellsRecombinant Fusion ProteinsG9a protein, mouseHistone-Lysine N-MethyltransferaseHistonesLeucineLysineProtease InhibitorsRecombinant Fusion ProteinsRNA, Small Interfering

Identifiers

PMID25489787
PMCPMC4301175
OpenAlexW2315590866

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.