Evidence map›Paper›PMID 17287358›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.

An Chi, Curtis Huttenhower, Lewis Y Geer, Joshua J Coon, John E P Syka, Dina L Bai, Jeffrey Shabanowitz, Daniel J Burke, Olga G Troyanskaya, Donald F Hunt

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers.

0numbers the graph read from it
0cells of the map it votes in
254citing papers in PubMed
38.7field-weighted citation impact, top 1% 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

254 citing papers in PubMed, 563 citations in OpenAlex.

  1. Article
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  4. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
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  11. Effective discrimination of gas-phase peptide conformers using TIMS-ECD-ToF MS/MS.Analytical methods : advancing methods and applications · 2021
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  14. Review
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194 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 1 country.

An ChiDepartment of Chemistry, University of Virginia, Charlottesville, VA 22904, USA.
Curtis Huttenhower
Lewis Y Geer
Joshua J Coon
John E P Syka
Dina L Bai
Jeffrey Shabanowitz
Daniel J Burke
Olga G Troyanskaya
Donald F Hunt
University of Virginia · USPrinceton University · USNational Institutes of Health · USThermo Fisher Scientific (United States) · USUniversity of Wisconsin–Madison · US

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
NIGMS NIH HHS GM37537NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

We present a strategy for the analysis of the yeast phosphoproteome that uses endo-Lys C as the proteolytic enzyme, immobilized metal affinity chromatography for phosphopeptide enrichment, a 90-min nanoflow-HPLC/electrospray-ionization MS/MS experiment for phosphopeptide fractionation and detection, gas phase ion/ion chemistry, electron transfer dissociation for peptide fragmentation, and the Open Mass Spectrometry Search Algorithm for phosphoprotein identification and assignment of phosphorylation sites. From a 30-microg (approximately 600 pmol) sample of total yeast protein, we identify 1,252 phosphorylation sites on 629 proteins. Identified phosphoproteins have expression levels that range from <50 to 1,200,000 copies per cell and are encoded by genes involved in a wide variety of cellular processes. We identify a consensus site that likely represents a motif for one or more uncharacterized kinases and show that yeast kinases, themselves, contain a disproportionately large number of phosphorylation sites. Detection of a pHis containing peptide from the yeast protein, Cdc10, suggests an unexpected role for histidine phosphorylation in septin biology. From diverse functional genomics data, we show that phosphoproteins have a higher number of interactions than an average protein and interact with each other more than with a random protein. They are also likely to be conserved across large evolutionary distances.

Indexed as

Binding SitesPhosphoproteinsPhosphorylationPhosphotransferasesProtein BindingProteomicsSaccharomyces cerevisiae ProteinsTandem Mass SpectrometryPhosphoproteinsPhosphotransferasesSaccharomyces cerevisiae Proteins

Identifiers

PMID17287358
PMCPMC1892997
OpenAlexW2090806203

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.