Evidence map›Paper›PMID 20056723›Full record

ReviewBriefings in functional genomics2010

Understanding protein phosphorylation on a systems level.

Jimmy Lin, Zhi Xie, Heng Zhu, Jiang Qian

Abstract readReview
In one paragraph

Review in Briefings in functional genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. ORAI CaBiomolecules · 2024
    Review
  2. Article
  3. Review
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  9. Article
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  15. Article
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  18. Systematic characterization of protein-DNA interactions.Cellular and molecular life sciences : CMLS · 2011
    Review
  19. Phosphorylation meets nuclear import: a review.Cell communication and signaling : CCS · 2010
    Article
  20. 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

4 authors.

Jimmy LinDepartment of Ophthalmology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Zhi Xie
Heng Zhu
Jiang Qian

Funding

DNA-Binding Activity of Human Transcription FactorsR01GM076102 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ZHU, HENG · 2006 to 2014
$2.6M
Computational Analysis of Retinal Regulatory Interactions: structure and dynamicsR01EY017589 · NEI · JOHNS HOPKINS UNIVERSITY · PI QIAN, JIANG · 2007 to 2010
$1.1M
NEI NIH HHS EY017589NIGMS NIH HHS GM076102
6 · The paper itself

Abstract

Protein kinase phosphorylation is central to the regulation and control of protein and cellular function. Over the past decade, the development of many high-throughput approaches has revolutionized the understanding of protein phosphorylation and allowed rapid and unbiased surveys of phosphoproteins and phosphorylation events. In addition to this technological advancement, there have also been computational improvements; recent studies on network models of protein phosphorylation have provided many insights into the cellular processes and pathways regulated by phosphorylation. This article gives an overview of experimental and computational techniques for identifying and analyzing protein phosphorylation on a systems level.

Indexed as

AnimalsCatalytic DomainComprehensionComputational BiologyHigh-Throughput Screening AssaysHumansMetabolic Networks and PathwaysPhosphoproteinsPhosphorylationProtein KinasesProteomicsPhosphoproteinsProtein Kinases

Identifiers

PMID20056723
PMCPMC3096446

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.