Evidence map›Paper›PMID 23159844›Full record

ReviewClinica chimica acta; international journal of clinical chemistry2013

Is phosphoproteomics ready for clinical research?

Anton B Iliuk, W Andy Tao

Abstract readReview
In one paragraph

Review in Clinica chimica acta; international journal of clinical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Trial
  2. Article
  3. Mass spectrometry-based phosphoproteomics in clinical applications.Trends in analytical chemistry : TRAC · 2023
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. 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

2 authors.

Anton B IliukDepartment of Biochemistry, Purdue University, West Lafayette, IN 47907, United States.
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
NIGMS NIH HHS 1R01GM088317NIGMS NIH HHS R01 GM088317
6 · The paper itself

Abstract

backgroundFor many diseases such as cancer where phosphorylation-dependent signaling is the foundation of disease onset and progression, single-gene testing and genomic profiling alone are not sufficient in providing most critical information. The reason for this is that in these activated pathways the signaling changes and drug resistance are often not directly correlated with changes in protein expression levels. In order to obtain the essential information needed to evaluate pathway activation or the effects of certain drugs and therapies on the molecular level, the analysis of changes in protein phosphorylation is critical.

methodsExisting approaches do not differentiate clinical disease subtypes on the protein and signaling pathway level, and therefore hamper the predictive management of the disease and the selection of therapeutic targets.

conclusionsThe mini-review examines the impact of emerging systems biology tools and the possibility of applying phosphoproteomics to clinical research.

Indexed as

Biomedical ResearchHumansPhosphoproteinsPhosphorylationProteomicsPhosphoproteins

Identifiers

PMID23159844
PMCPMC3637850

What OpenQuestion holds

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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.