Evidence map›Paper›PMID 20395639›Full record

ArticleMolecular & cellular proteomics : MCP2010

Integrated phosphoproteomics analysis of a signaling network governing nutrient response and peroxisome induction.

Ramsey A Saleem, Richard S Rogers, Alexander V Ratushny, David J Dilworth, Paul T Shannon, David Shteynberg, Yakun Wan, Robert L Moritz, Alexey I Nesvizhskii, Richard A Rachubinski and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 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
1.9field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Signaling dynamics and peroxisomes.Current opinion in cell biology · 2015
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Peroxisomes take shape.Nature reviews. Molecular cell biology · 2013
    Review
  14. Combining results of multiple search engines in proteomics.Molecular & cellular proteomics : MCP · 2013
    Review
  15. Review
  16. The peroxisome: an update on mysteries.Histochemistry and cell biology · 2012
    Review
  17. Review
  18. Article
  19. 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

11 authors at 3 institutions in 2 countries.

Ramsey A SaleemInstitute for Systems Biology, Seattle, Washington 98103, USA.
Richard S Rogers
Alexander V Ratushny
David J Dilworth
Paul T Shannon
David Shteynberg
Yakun Wan
Robert L Moritz
Alexey I Nesvizhskii
Richard A Rachubinski
John D Aitchison
Institute for Systems Biology · USUniversity of Alberta · CAUniversity of Michigan–Ann Arbor · US

Funding

Quantitative Systems BiologyP50GM076547 · NIGMS · INSTITUTE FOR SYSTEMS BIOLOGY · PI BALIGA, NITIN S · 2006 to 2016
$30.6M
NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
Oleate-responsive gene regulatory networks governing peroxisome proliferationR01GM075152 · NIGMS · SEATTLE BIOMEDICAL RESEARCH INSTITUTE · PI AITCHISON, JOHN D. · 2008 to 2011
$1.9M
CIHR 53326NCRR NIH HHS RR022220NCRR NIH HHS U54 RR022220NIGMS NIH HHS GM075152NIGMS NIH HHS GM076547NIGMS NIH HHS P50 GM076547NIGMS NIH HHS R01 GM075152
6 · The paper itself

Abstract

Phosphorylation of proteins is a key posttranslational modification in cellular signaling, regulating many aspects of cellular responses. We used a quantitative, integrated, phosphoproteomics approach to characterize the cellular responses of the yeast Saccharomyces cerevisiae to the fatty acid oleic acid, a molecule with broad human health implications and a potent inducer of peroxisomes. A combination of cryolysis and urea solubilization was used to minimize the opportunity for reorientation of the phosphoproteome, and hydrophilic interaction liquid chromatography and IMAC chemistries were used to fractionate and enrich for phosphopeptides. Using these approaches, numerous phosphorylated peptides specific to oleate-induced and glucose-repressed conditions were identified and mapped to known signaling pathways. These include several transcription factors, two of which, Pip2p and Cst6p, must be phosphorylated for the normal transcriptional response of fatty acid-responsive loci encoding peroxisomal proteins. The phosphoproteome data were integrated with results from genome-wide assays studying the effects of signaling molecule deletions and known protein-protein interactions to generate a putative fatty acid-responsive signaling network. In this network, the most highly connected nodes are those with the largest effects on cellular responses to oleic acid. These properties are consistent with a scale-free topology, demonstrating that scale-free properties are conserved in condition-specific networks.

Indexed as

PeroxisomesProteomicsSignal TransductionMass SpectrometryOligonucleotide Array Sequence AnalysisPhosphoproteinsSaccharomyces cerevisiaePhosphoproteins

Identifiers

PMID20395639
PMCPMC2938103
OpenAlexW2141491800

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.