Evidence map›Paper›PMID 38757396›Full record

ArticleProtein science : a publication of the Protein Society2024

Adaptive evolution: Eukaryotic enzyme's specificity shift to a bacterial substrate.

Emi Latifah, Indira Rizqita Ivanesthi, Yi-Kuan Tseng, Hung-Chuan Pan, Chien-Chia Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Adaptive evolution: Eukaryotic enzyme's specificity shift to a bacterial substrate.Protein science : a publication of the Protein Society · 2024
    Article
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

5 authors.

Emi LatifahDepartment of Life Sciences, National Central University, Taoyuan, Taiwan.
Indira Rizqita IvanesthiDepartment of Life Sciences, National Central University, Taoyuan, Taiwan.
Yi-Kuan TsengGraduate Institute of Statistics, National Central University, Taoyuan, Taiwan.
Hung-Chuan PanDepartment of Neurosurgery, Taichung Veterans General Hospital, Taichung, Taiwan.
Chien-Chia WangDepartment of Life Sciences, National Central University, Taoyuan, Taiwan.ORCID 0000-0002-7104-1307

Funding

National Science and Technology Council NSTC 112-2311-B008-001Taipei Veterans General Hospital VGHUST113-G4-1-1
6 · The paper itself

Abstract

Prolyl-tRNA synthetase (ProRS), belonging to the family of aminoacyl-tRNA synthetases responsible for pairing specific amino acids with their respective tRNAs, is categorized into two distinct types: the eukaryote/archaeon-like type (E-type) and the prokaryote-like type (P-type). Notably, these types are specific to their corresponding cognate tRNAs. In an intriguing paradox, Thermus thermophilus ProRS (TtProRS) aligns with the E-type ProRS but selectively charges the P-type tRNA

Indexed as

Amino Acyl-tRNA SynthetasesRNA, Transfer, ProThermus thermophilusAmino Acid MotifsAmino Acid SequenceBacterial ProteinsEvolution, MolecularInverted Repeat SequencesPiperidinesProtein Synthesis InhibitorsQuinazolinonesYeastsAmino Acyl-tRNA SynthetasesBacterial ProteinshalofuginonePiperidinesProtein Synthesis InhibitorsQuinazolinonesRNA, Transfer, Proaminoacyl‐tRNA synthetasehalofuginoneidentity elementprotein synthesisthermophilic bacteriumtRNA

Identifiers

PMID38757396
PMCPMC11099734

What Socratic holds

Textmetadata
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 Socratic graph.