Evidence map›Paper›PMID 17947660›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2007

Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.

Lulu Cao, Kebing Yu, Cindy Banh, Vinh Nguyen, Anna Ritz, Benjamin J Raphael, Yuko Kawakami, Toshiaki Kawakami, Arthur R Salomon

Open access · greenAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Signal transduction and chemotaxis in mast cells.European journal of pharmacology · 2016
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Isolating specific embryonic cells of the sea urchin by FACS.Methods in molecular biology (Clifton, N.J.) · 2014
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Phosphoproteomic analysis of liver homogenates.Methods in molecular biology (Clifton, N.J.) · 2012
    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

9 authors at 2 institutions in 1 country.

Lulu CaoDepartment of Chemistry, Brown University, Providence, RI 02912, USA.
Kebing Yu
Cindy Banh
Vinh Nguyen
Anna Ritz
Benjamin J Raphael
Yuko Kawakami
Toshiaki Kawakami
Arthur R Salomon
Brown University · USLa Jolla Institute for Immunology · US

Funding

WNT SIGNALING IN HEPATOCELLULAR CARCINOMAP20RR015578 · NCRR · BROWN UNIVERSITY · PI THOMPSON, WILLIAM ALBERT · 2000 to 2009
$22.8M
NCRR NIH HHS 2P20RR015578NCRR NIH HHS P20 RR015578
6 · The paper itself

Abstract

Mast cells play a central role in type I hypersensitivity reactions and allergic disorders such as anaphylaxis and asthma. Activation of mast cells, through a cascade of phosphorylation events, leads to the release of mediators of the early phase allergic response. Understanding the molecular architecture underlying mast cell signaling may provide possibilities for therapeutic intervention in asthma and other allergic diseases. Although many details of mast cell signaling have been described previously, a systematic, quantitative analysis of the global tyrosine phosphorylation events that are triggered by activation of the mast cell receptor is lacking. In many cases, the involvement of particular proteins in mast cell signaling has been established generally, but the precise molecular mechanism of the interaction between known signaling proteins often mediated through phosphorylation is still obscure. Using recently advanced methodologies in mass spectrometry, including automation of phosphopeptide enrichments and detection, we have now substantially characterized, with temporal resolution as short as 10 s, the sites and levels of tyrosine phosphorylation across 10 min of FcepsilonRI-induced mast cell activation. These results reveal a far more extensive array of tyrosine phosphorylation events than previously known, including novel phosphorylation sites on canonical mast cell signaling molecules, as well as unexpected pathway components downstream of FcepsilonRI activation. Furthermore, our results, for the first time in mast cells, reveal the sequence of phosphorylation events for 171 modification sites across 121 proteins in the MCP5 mouse mast cell line and 179 modification sites on 117 proteins in mouse bone marrow-derived mast cells.

Indexed as

Signal TransductionActinsAnimalsCell LineCytoskeletonMast CellsMicePhosphoproteinsPhosphorylationProteomicsTandem Mass SpectrometryTime FactorsActinsPhosphoproteins

Identifiers

PMID17947660
PMCPMC2727709
OpenAlexW1484096248

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.