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Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translationalmodification with significant enrichment around localised sites of sequence variation

Overview of attention for article published in Biology Direct, November 2013
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Title
Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translationalmodification with significant enrichment around localised sites of sequence variation
Published in
Biology Direct, November 2013
DOI 10.1186/1745-6150-8-29
Pubmed ID
Authors

Dinesh C Soares, Catherine M Abbott

Abstract

Translation elongation factors eEF1A1 and eEF1A2 are 92% identical but exhibit non-overlapping expression patterns. While the two proteins are predicted to have similar tertiary structures, it is notable that the minor variations between their sequences are highly localised within their modelled structures. We used recently available high-throughput "omics" data to assess the spatial location of post-translational modifications and discovered that they are highly enriched on those surface regions of the protein that correspond to the clusters of sequence variation. This observation suggests how these two isoforms could be differentially regulated allowing them to perform distinct functions.This article was reviewed by Frank Eisenhaber and Ramanathan Sowdhamini.

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Mendeley readers

The data shown below were compiled from readership statistics for 50 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Spain 1 2%
United States 1 2%
Unknown 48 96%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 18 36%
Student > Master 8 16%
Student > Bachelor 7 14%
Researcher 5 10%
Student > Doctoral Student 1 2%
Other 3 6%
Unknown 8 16%
Readers by discipline Count As %
Agricultural and Biological Sciences 16 32%
Biochemistry, Genetics and Molecular Biology 15 30%
Neuroscience 3 6%
Pharmacology, Toxicology and Pharmaceutical Science 2 4%
Social Sciences 2 4%
Other 4 8%
Unknown 8 16%