Evidence map›Paper›PMID 26656258›Full record

ArticleScientific reports2015

Cross-species conservation of complementary amino acid-ribonucleobase interactions and their potential for ribosome-free encoding.

John G D Cannon, Rachel M Sherman, Victoria M Y Wang, Grace A Newman

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 90% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 3 institutions in 2 countries.

John G D CannonDepartment of Biology, Carleton College, 1 College Street, Northfield MN, 55057, United States.
Rachel M ShermanDepartment of Biology, Harvey Mudd College, 301 Platt Blvd, Claremont CA 91711, United States.
Victoria M Y WangDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, United Kingdom.
Grace A NewmanDepartment of Mathematics, Carleton College, 1 College Street, Northfield MN, 55057, United States.
Carleton College · USHarvey Mudd College · USThe Honourable Society of Lincoln's Inn · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of amino acid-RNA nucleobase interactions in the evolution of RNA translation and protein-mRNA autoregulation remains an open area of research. We describe the inference of pairwise amino acid-RNA nucleobase interaction preferences using structural data from known RNA-protein complexes. We observed significant matching between an amino acid's nucleobase affinity and corresponding codon content in both the standard genetic code and mitochondrial variants. Furthermore, we showed that knowledge of nucleobase preferences allows statistically significant prediction of protein primary sequence from mRNA using purely physiochemical information. Interestingly, ribosomal primary sequences were more accurately predicted than non-ribosomal sequences, suggesting a potential role for direct amino acid-nucleobase interactions in the genesis of amino acid-based ribosomal components. Finally, we observed matching between amino acid-nucleobase affinities and corresponding mRNA sequences in 35 evolutionarily diverse proteomes. We believe these results have important implications for the study of the evolutionary origins of the genetic code and protein-mRNA cross-regulation.

Indexed as

Amino AcidsCodonGenetic CodeHumansNucleic AcidsProteinsRibosomesRNARNA, MessengerAmino AcidsCodonNucleic AcidsProteinsRNARNA, Messenger

Identifiers

PMID26656258
PMCPMC4674897
OpenAlexW2289398305

What OpenQuestion holds

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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.