Evidence map›Paper›PMID 30248088›Full record

ArticlePLoS computational biology2018

Proteome-scale relationships between local amino acid composition and protein fates and functions.

Sean M Cascarina, Eric D Ross

Abstract read
In one paragraph

Article in PLoS computational biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

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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

2 authors.

Sean M CascarinaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, United States of America.ORCID 0000-0002-3054-2332
Eric D RossDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, United States of America.ORCID 0000-0002-6473-9977

Funding

The determinants of aggregation and toxicity of prion-like domainsR01GM105991 · NIGMS · COLORADO STATE UNIVERSITY · PI ROSS, ERIC D · 2013 to 2017
$1.5M
NIGMS NIH HHS R01 GM105991
6 · The paper itself

Abstract

Proteins with low-complexity domains continue to emerge as key players in both normal and pathological cellular processes. Although low-complexity domains are often grouped into a single class, individual low-complexity domains can differ substantially with respect to amino acid composition. These differences may strongly influence the physical properties, cellular regulation, and molecular functions of low-complexity domains. Therefore, we developed a bioinformatic approach to explore relationships between amino acid composition, protein metabolism, and protein function. We find that local compositional enrichment within protein sequences is associated with differences in translation efficiency, abundance, half-life, protein-protein interaction promiscuity, subcellular localization, and molecular functions of proteins on a proteome-wide scale. However, local enrichment of related amino acids is sometimes associated with opposite effects on protein regulation and function, highlighting the importance of distinguishing between different types of low-complexity domains. Furthermore, many of these effects are discernible at amino acid compositions below those required for classification as low-complexity or statistically-biased by traditional methods and in the absence of homopolymeric amino acid repeats, indicating that thresholds employed by classical methods may not reflect biologically relevant criteria. Application of our analyses to composition-driven processes, such as the formation of membraneless organelles, reveals distinct composition profiles even for closely related organelles. Collectively, these results provide a unique perspective and detailed insights into relationships between amino acid composition, protein metabolism, and protein functions.

Indexed as

ProteomicsAlgorithmsAmino Acid MotifsAmino AcidsAnimalsCaenorhabditis elegansCell MembraneComputational BiologyEvolution, MolecularOpen Reading FramesPolymersProtein DomainsProtein Interaction MappingProteinsProteomeSaccharomyces cerevisiaeAmino AcidsPolymersProteinsProteome

Identifiers

PMID30248088
PMCPMC6171957

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.