Evidence map›Paper›PMID 23358503›Full record

ArticleMolecular & cellular proteomics : MCP2013

Phosphotyrosine signaling proteins that drive oncogenesis tend to be highly interconnected.

Grigoriy Koytiger, Alexis Kaushansky, Andrew Gordus, John Rush, Peter K Sorger, Gavin MacBeath

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

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  17. Integrating phosphoproteomics in systems biology.Computational and structural biotechnology journal · 2014
    Review
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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 4 institutions in 1 country.

Grigoriy KoytigerDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Alexis Kaushansky
Andrew Gordus
John Rush
Peter K Sorger
Gavin MacBeath
Center for Systems Biology · USHarvard University · USCell Signaling Technology (United States) · USCenter for Infectious Disease Research · US

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
Measuring and Predicting PDZ Domain-Peptide Interactions on a Genome-wide ScaleR01GM072872 · NIGMS · HARVARD UNIVERSITY · PI MACBEATH, GAVIN · 2005 to 2013
$3.1M
Quantitative Interaction Networks for Tyrosine-Phosphorylated ProteinsR33CA128726 · NCI · HARVARD UNIVERSITY · PI MACBEATH, GAVIN · 2007 to 2009
$1.2M
NCI NIH HHS R33 CA128726NCI NIH HHS R33CA128726NIGMS NIH HHS 5 T32 GM07598NIGMS NIH HHS R01 GM072872NIGMS NIH HHS T32 GM007598
6 · The paper itself

Abstract

Mutation and overexpression of receptor tyrosine kinases or the proteins they regulate serve as oncogenic drivers in diverse cancers. To better understand receptor tyrosine kinase signaling and its link to oncogenesis, we used protein microarrays to systematically and quantitatively measure interactions between virtually every SH2 or PTB domain encoded in the human genome and all known sites of tyrosine phosphorylation on 40 receptor tyrosine kinases and on most of the SH2 and PTB domain-containing adaptor proteins. We found that adaptor proteins, like RTKs, have many high affinity bindings sites for other adaptor proteins. In addition, proteins that drive cancer, including both receptors and adaptor proteins, tend to be much more highly interconnected via networks of SH2 and PTB domain-mediated interactions than nononcogenic proteins. Our results suggest that network topological properties such as connectivity can be used to prioritize new drug targets in this well-studied family of signaling proteins.

Indexed as

CarcinogenesisHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsOncogene ProteinsPhosphotyrosineProtein BindingProtein Interaction Domains and MotifsProtein Interaction MapsReceptor Protein-Tyrosine KinasesSignal TransductionIntracellular Signaling Peptides and ProteinsOncogene ProteinsPhosphotyrosineReceptor Protein-Tyrosine Kinases

Identifiers

PMID23358503
PMCPMC3650332
OpenAlexW2150582475

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.