Evidence map›Paper›PMID 16330754›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Combining chemical genetics and proteomics to identify protein kinase substrates.

Noah Dephoure, Russell W Howson, Justin D Blethrow, Kevan M Shokat, Erin K O'Shea

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 116 citations in OpenAlex.

  1. Review
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  3. Mapping proteome-wide targets of protein kinases in plant stress responses.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 2 institutions in 1 country.

Noah DephoureHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, 94143, USA.
Russell W Howson
Justin D Blethrow
Kevan M Shokat
Erin K O'Shea
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

REGULATION OF YEAST PHO5 GENER01GM051377 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI O'SHEA, ERIN K. · 1994 to 2011
$3.7M
NIGMS NIH HHS GM51377NIGMS NIH HHS R01 GM051377
6 · The paper itself

Abstract

Phosphorylation is a ubiquitous protein modification important for regulating nearly every aspect of cellular biology. Protein kinases are highly conserved and constitute one of the largest gene families. Identifying the substrates of a kinase is essential for understanding its cellular role, but doing so remains a difficult task. We have developed a high-throughput method to identify substrates of yeast protein kinases that employs a collection of yeast strains each expressing a single epitope-tagged protein and a chemical genetic strategy that permits kinase reactions to be performed in native, whole-cell extracts. Using this method, we screened 4,250 strains expressing epitope-tagged proteins and identified 24 candidate substrates of the Pho85-Pcl1 cyclin-dependent kinase, including the known substrate Rvs167. The power of this method to identify true kinase substrates is strongly supported by functional overlap and colocalization of candidate substrates and the kinase, as well as by the specificity of Pho85-Pcl1 for some of the substrates compared with another Pho85-cyclin kinase complex. This method is readily adaptable to other yeast kinases.

Indexed as

Genetic TechniquesCyclin-Dependent KinasesImmunoblottingKineticsMicrofilament ProteinsProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityCyclin-Dependent KinasesMicrofilament ProteinsPHO85 protein, S cerevisiaeRVS167 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID16330754
PMCPMC1306798
OpenAlexW2149049196

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.