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Modeling of RAS complexes supports roles in cancer for less studied partners

Overview of attention for article published in BMC Biophysics, August 2017
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Title
Modeling of RAS complexes supports roles in cancer for less studied partners
Published in
BMC Biophysics, August 2017
DOI 10.1186/s13628-017-0037-6
Pubmed ID
Authors

H. Billur Engin, Daniel Carlin, Dexter Pratt, Hannah Carter

Abstract

RAS protein interactions have predominantly been studied in the context of the RAF and PI3kinase oncogenic pathways. Structural modeling and X-ray crystallography have demonstrated that RAS isoforms bind to canonical downstream effector proteins in these pathways using the highly conserved switch I and II regions. Other non-canonical RAS protein interactions have been experimentally identified, however it is not clear whether these proteins also interact with RAS via the switch regions. To address this question we constructed a RAS isoform-specific protein-protein interaction network and predicted 3D complexes involving RAS isoforms and interaction partners to identify the most probable interaction interfaces. The resulting models correctly captured the binding interfaces for well-studied effectors, and additionally implicated residues in the allosteric and hyper-variable regions of RAS proteins as the predominant binding site for non-canonical effectors. Several partners binding to this new interface (SRC, LGALS1, RABGEF1, CALM and RARRES3) have been implicated as important regulators of oncogenic RAS signaling. We further used these models to investigate competitive binding and multi-protein complexes compatible with RAS surface occupancy and the putative effects of somatic mutations on RAS protein interactions. We discuss our findings in the context of RAS localization to the plasma membrane versus within the cytoplasm and provide a list of RAS protein interactions with possible cancer-related consequences, which could help guide future therapeutic strategies to target RAS proteins.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 31 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 31 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 6 19%
Student > Bachelor 5 16%
Researcher 5 16%
Student > Master 3 10%
Professor 1 3%
Other 3 10%
Unknown 8 26%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 15 48%
Immunology and Microbiology 2 6%
Agricultural and Biological Sciences 2 6%
Mathematics 1 3%
Computer Science 1 3%
Other 1 3%
Unknown 9 29%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 12 August 2017.
All research outputs
#17,911,821
of 22,997,544 outputs
Outputs from BMC Biophysics
#46
of 69 outputs
Outputs of similar age
#228,295
of 318,512 outputs
Outputs of similar age from BMC Biophysics
#3
of 3 outputs
Altmetric has tracked 22,997,544 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 69 research outputs from this source. They receive a mean Attention Score of 3.5. This one is in the 31st percentile – i.e., 31% of its peers scored the same or lower than it.
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We're also able to compare this research output to 3 others from the same source and published within six weeks on either side of this one.