Evidence map›Paper›PMID 29927094›Full record

ArticleCurrent protocols in chemical biology2018

Identification of Phosphorylated Proteins on a Global Scale.

Anton Iliuk

Abstract read
In one paragraph

Article in Current protocols in chemical biology, 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
–field-weighted citation impact
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.

  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

1 author.

Anton IliukTymora Analytical Operations, Innovations, West Lafayette, Indiana.

Funding

Novel soluble nanopolymers for enrichment of low abundant phosphoproteinsR43CA162767 · NCI · TYMORA ANALYTICAL OPERATIONS, LLC · PI ILIUK, ANTON · 2012 to 2013
$294k
NCI NIH HHS R43 CA162767
6 · The paper itself

Abstract

Liquid chromatography (LC) coupled with tandem mass spectrometry (MS/MS) has enabled researchers to analyze complex biological samples with unprecedented depth. It facilitates the identification and quantification of modifications within thousands of proteins in a single large-scale proteomic experiment. Analysis of phosphorylation, one of the most common and important post-translational modifications, has particularly benefited from such progress in the field. Here, detailed protocols are provided for a few well-regarded, common sample preparation methods for an effective phosphoproteomic experiment. © 2018 by John Wiley & Sons, Inc.

Indexed as

Chromatography, LiquidPhosphorylationProtein Processing, Post-TranslationalProteinsTandem Mass SpectrometryProteinsLC-MSphosphopeptide enrichmentphosphoproteomicsprotein phosphorylationproteomicssample preparation

Identifiers

PMID29927094
PMCPMC6125197

What OpenQuestion holds

Textmetadata
LicenceTDM
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.