Evidence map›Paper›PMID 29540535›Full record

ArticleBioscience reports2018

Target identification reveals protein arginine methyltransferase 1 is a potential target of phenyl vinyl sulfone and its derivatives.

Cheng-Han Yu, Chi-Chi Chou, Der-Yen Lee, Kay-Hooi Khoo, Geen-Dong Chang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioscience reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. Article
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

5 authors at 3 institutions in 1 country.

Cheng-Han YuGraduate Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei 10617, Taiwan.
Chi-Chi ChouInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Der-Yen LeeGraduate Institute of Integrated Medicine, China Medical University, Taichung 40402, Taiwan.
Kay-Hooi KhooGraduate Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei 10617, Taiwan.
Geen-Dong ChangGraduate Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei 10617, Taiwan gdchang@ntu.edu.tw.
National Taiwan University · TWChina Medical University · TWInstitute of Biological Chemistry, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phenyl vinyl sulfone (PVS) and phenyl vinyl sulfonate (PVSN) inactivate protein tyrosine phosphatases (PTPs) by mimicking the phosphotyrosine structure and providing a Michael addition acceptor for the active-site cysteine residue of PTPs, thus forming covalent adducts between PVS (or PVSN) and PTPs. We developed a specific antiserum against PVS. This antiserum can be used in general antibody-based assays such as immunoblotting, immunofluorescence staining, and immunoprecipitation. Target identification through immunoprecipitation and mass spectrometry analysis reveals potential targets of PVS, mostly proteins with reactive cysteine residues or low-p

Indexed as

HeLa CellsHumansProtein-Arginine N-MethyltransferasesRepressor ProteinsSulfonesphenyl vinyl sulfonePRMT1 protein, humanProtein-Arginine N-MethyltransferasesRepressor ProteinsSulfonesBay11-7082covalent drugphenyl vinyl sulfonatephenyl vinyl sulfoneprotein arginine methyltransferase 1target identification

Identifiers

PMID29540535
PMCPMC5968187
OpenAlexW2790970854

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.