Evidence map›Paper›PMID 24728074›Full record

ArticleMolecular & cellular proteomics : MCP2014

Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.

Kin K Leung, Ronald J Hause, John L Barkinge, Mark F Ciaccio, Chih-Pin Chuu, Richard B Jones

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Autocrine/Paracrine Loop Between SCFFrontiers in immunology · 2022
    Article
  7. Cancer-associated mutations in the p85α N-terminal SH2 domain activate a spectrum of receptor tyrosine kinases.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
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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

6 authors at 3 institutions in 2 countries.

Kin K LeungFrom the ‡Committee on Cancer Biology.
Ronald J Hause¶Committee on Genetics, Genomics, and Systems Biology, and.
John L BarkingeFrom the ‡Committee on Cancer Biology, ¶Committee on Genetics, Genomics, and Systems Biology, and ‡‡Committee on Cellular and Molecular Physiology, The Ben May Department for Cancer Research and the Institute for Genomics and Systems Biology, The Gwen and Jules Knapp Center for Biomedical Discovery, University of Chicago, Chicago, Illinois 60637.
Mark F Ciaccio‡‡Committee on Cellular and Molecular Physiology, The Ben May Department for Cancer Research and the Institute for Genomics and Systems Biology, The Gwen and Jules Knapp Center for Biomedical Discovery, University of Chicago, Chicago, Illinois 60637.
Chih-Pin ChuuFrom the ‡Committee on Cancer Biology, ¶Committee on Genetics, Genomics, and Systems Biology, and ‡‡Committee on Cellular and Molecular Physiology, The Ben May Department for Cancer Research and the Institute for Genomics and Systems Biology, The Gwen and Jules Knapp Center for Biomedical Discovery, University of Chicago, Chicago, Illinois 60637.
Richard B JonesFrom the ‡Committee on Cancer Biology, ¶Committee on Genetics, Genomics, and Systems Biology, and richardbjones@gmail.com.
Committee on Climate Change · GBJoint Center for Structural Genomics · USUniversity of Chicago · US

Funding

Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
NCATS NIH HHS UL1 TR000430
6 · The paper itself

Abstract

Many human diseases are associated with aberrant regulation of phosphoprotein signaling networks. Src homology 2 (SH2) domains represent the major class of protein domains in metazoans that interact with proteins phosphorylated on the amino acid residue tyrosine. Although current SH2 domain prediction algorithms perform well at predicting the sequences of phosphorylated peptides that are likely to result in the highest possible interaction affinity in the context of random peptide library screens, these algorithms do poorly at predicting the interaction potential of SH2 domains with physiologically derived protein sequences. We employed a high throughput interaction assay system to empirically determine the affinity between 93 human SH2 domains and phosphopeptides abstracted from several receptor tyrosine kinases and signaling proteins. The resulting interaction experiments revealed over 1000 novel peptide-protein interactions and provided a glimpse into the common and specific interaction potentials of c-Met, c-Kit, GAB1, and the human androgen receptor. We used these data to build a permutation-based logistic regression classifier that performed considerably better than existing algorithms for predicting the interaction potential of several SH2 domains.

Indexed as

src Homology DomainsAdaptor Proteins, Signal TransducingBinding SitesErbB ReceptorsFluorescence PolarizationHumansPhosphorylationPhosphotyrosineProtein BindingProto-Oncogene Proteins c-kitProto-Oncogene Proteins c-metReceptors, AndrogenSignal TransductionTyrosineAdaptor Proteins, Signal TransducingAR protein, humanEGFR protein, humanErbB ReceptorsGAB1 protein, humanPhosphotyrosineProto-Oncogene Proteins c-kitProto-Oncogene Proteins c-metReceptors, AndrogenTyrosine

Identifiers

PMID24728074
PMCPMC4083110
OpenAlexW2171770174

What Socratic 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 Socratic graph.