Evidence map›Paper›PMID 22890988›Full record

ArticleProteomics2012

Validation of regulated protein phosphorylation events in yeast by quantitative mass spectrometry analysis of purified proteins.

Wolfgang Reiter, Dorothea Anrather, Ilse Dohnal, Peter Pichler, Jiri Veis, Morten Grøtli, Francesc Posas, Gustav Ammerer

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

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  7. Regulation of Pkc1 Hyper-Phosphorylation by Genotoxic Stress.Journal of fungi (Basel, Switzerland) · 2021
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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

8 authors at 5 institutions in 3 countries.

Wolfgang ReiterDepartment for Biochemistry, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria. wolfgang.l.reiter@univie.ac.at
Dorothea Anrather
Ilse Dohnal
Peter Pichler
Jiri Veis
Morten Grøtli
Francesc Posas
Gustav Ammerer
University of Vienna · ATChristian Doppler Laboratory for Thermoelectricity · ATGothia Innovation (Sweden) · SEMax Perutz Labs · ATPompeu Fabra University · ES

Funding

Austrian Science Fund FWF F 3402
6 · The paper itself

Abstract

Global phosphoproteomic studies based on MS have generated qualitative and quantitative data describing protein phosphorylation events in various biological systems. Since high-throughput data for protein modifications are inherently incomplete, we developed a strategy to extend and validate such primary datasets. We selected interesting protein candidates from a global screen in yeast and employed a modified histidine biotin tag that allows tandem affinity purifications of our targets under denaturing conditions. Products in question can be digested directly from affinity resins and phosphopeptides can be further enriched via TiO(2) before MS analysis. Our robust protocol can be amended for SILAC as well as iTRAQ quantifications or label-free approaches based on selective reaction monitoring, allowing completion of the phosphorylation pattern in a first step, followed by a detailed analysis of the phosphorylation kinetics. We exemplify the value of such a strategy by an in-depth analysis of Pan1, a highly phosphorylated factor involved in early steps of endocytosis. The study of Pan1 under osmotic stress conditions in different mutant backgrounds allowed us to differentiate between mitogen-activated protein kinase Hog1 driven and Hog1 independent stress responses.

Indexed as

Amino Acid SequenceEndocytosisFungal ProteinsIsotope LabelingMass SpectrometryMicrofilament ProteinsMitogen-Activated Protein KinasesMolecular Sequence DataMutationPhosphoproteinsPhosphorylationProteomicsReproducibility of ResultsSaccharomyces cerevisiae ProteinsSignal TransductionStress, PhysiologicalEde1 protein, S cerevisiaeFungal ProteinsHOG1 protein, S cerevisiaeMicrofilament ProteinsMitogen-Activated Protein KinasesPAN1 protein, S cerevisiaePhosphoproteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22890988
PMCPMC6049613
OpenAlexW2045173386

What OpenQuestion holds

Textmetadata
LicenceTDM
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.