Evidence map›Paper›PMID 35457045›Full record

ArticleInternational journal of molecular sciences2022

A Leucyl-tRNA Synthetase Urzyme: Authenticity of tRNA Synthetase Catalytic Activities and Promiscuous Phosphorylation of Leucyl-5'AMP.

Jessica J Hobson, Zhijie Li, Hao Hu, Charles W Carter

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Jessica J HobsonDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7260, USA.ORCID 0000-0002-1896-0339
Zhijie LiDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7260, USA.
Hao HuDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7260, USA.
Charles W CarterDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7260, USA.ORCID 0000-0002-2653-4452
University of North Carolina at Chapel Hill · US

Funding

Sense/Antisense Genetic Coding and the Origins of TranslationR01GM078227 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2006 to 2018
$3.9M
Alfred P. Sloan Foundation G-2021-16944NIGMS NIH HHS GM78227W. M. Keck Foundation Award 21-0715
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetase (aaRS)/tRNA cognate pairs translate the genetic code by synthesizing specific aminoacyl-tRNAs that are assembled on messenger RNA by the ribosome. Deconstruction of the two distinct aaRS superfamilies (Classes) has provided conceptual and experimental models for their early evolution. Urzymes, containing ~120-130 amino acids excerpted from regions where genetic coding sequence complementarities have been identified, are key experimental models motivated by the proposal of a single bidirectional ancestral gene. Previous reports that Class I and Class II urzymes accelerate both amino acid activation and tRNA aminoacylation have not been extended to other synthetases. We describe a third urzyme (LeuAC) prepared from the Class IA

Indexed as

Amino Acyl-tRNA SynthetasesLeucine-tRNA LigaseAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAmino AcidsPhosphorylationAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAmino AcidsAmino Acyl-tRNA SynthetasesLeucine-tRNA Ligaseevolutionary changes in the occupation of sequence spaceevolutionary intermediatesgenetic codingmechanistic enzymologyprotein engineeringprotein synthesissingle turnover kineticsstructural biologyvalidating weak catalytic activities

Identifiers

PMID35457045
PMCPMC9026127
OpenAlexW4223540984

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.