ArticleBiology direct2011
Evolutionary patterns of phosphorylated serines.
Article in Biology direct, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- The evolutionary scaling of cellular traits imposed by the drift barrier.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Theoretical Framework for Evolutionary Cell Biology.Journal of molecular biology · 2020Review
- Article
- Evaluation of functionality for serine and threonine phosphorylation with different evolutionary ages in human and mouse.BMC genomics · 2018Article
- Where do phosphosites come from and where do they go after gene duplication?International journal of evolutionary biology · 2012Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslationally modified amino acids are chemically distinct types of amino acids and in terms of evolution they might behave differently from their non-modified counterparts. In order to check this possibility, we reconstructed the evolutionary history of phosphorylated serines in several groups of organisms. Comparisons of substitution vectors have revealed some significant differences in the evolution of modified and corresponding non-modified amino acids. In particular, phosphoserines are more frequently substituted to aspartate and glutamate, compared to non-phosphorylated serines.
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Registered trials
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