Evidence map›Paper›PMID 29094114›Full record

ReviewThe Analyst2017

Recent advances in phosphoproteomics and application to neurological diseases.

Justine V Arrington, Chuan-Chih Hsu, Sarah G Elder, W Andy Tao

Abstract readReview
In one paragraph

Review in The Analyst, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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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.

Justine V ArringtonDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA. watao@purdue.edu.
Chuan-Chih Hsu
Sarah G Elder
W Andy Tao

Funding

New Proteomic Technologies for the Analysis of Tyrosine Kinase Signaling PathwaysR01GM088317 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2010 to 2014
$1.6M
A Proteomic Platform to identify and Validate Biomarkers in Metabolic Syndrome and Coronary Artery DiseaseR01GM111788 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2015 to 2017
$900k
NIGMS NIH HHS R01 GM088317NIGMS NIH HHS R01 GM111788
6 · The paper itself

Abstract

Phosphorylation has an incredible impact on the biological behavior of proteins, altering everything from intrinsic activity to cellular localization and complex formation. It is no surprise then that this post-translational modification has been the subject of intense study and that, with the advent of faster, more accurate instrumentation, the number of large-scale mass spectrometry-based phosphoproteomic studies has swelled over the past decade. Recent developments in sample preparation, phosphorylation enrichment, quantification, and data analysis strategies permit both targeted and ultra-deep phosphoproteome profiling, but challenges remain in pinpointing biologically relevant phosphorylation events. We describe here technological advances that have facilitated phosphoproteomic analysis of cells, tissues, and biofluids and note applications to neuropathologies in which the phosphorylation machinery may be dysregulated, much as it is in cancer.

Indexed as

ChromatographyHumansNervous System DiseasesPhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryPhosphoproteins

Identifiers

PMID29094114
PMCPMC5708141

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.