Evidence map›Paper›PMID 34565314›Full record

ReviewBiochemistry. Biokhimiia2021

Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.

Andrei A Korostelev

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry. Biokhimiia, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

1 author at 1 institution in 1 country.

Andrei A KorostelevRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical School, Worcester, MA, USA. Andrei.Korostelev@umassmed.edu.
University of Massachusetts Chan Medical School · US

Funding

Translational Control: Discovery and MechanismsR35GM127094 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Andrei Korostelev · 2018 to 2026
$5.5M
Insight into the Ebola virus glycoprotein fusion mechanism gleaned from the 2013-2016 epidemic GP-A82V variantR01AI148784 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LUBAN, JEREMY · 2020 to 2024
$4.1M
Structural bases for cellular stress responses mediated by stalled translationR01GM106105 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2013 to 2017
$1.6M
Molecular principles of translation terminationR01GM107465 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2015 to 2018
$1.3M
Molecular principles of stringent response activation in bacteriaR56AI151372 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2021 to 2021
$534k
NIAID NIH HHS R01 AI148784NIAID NIH HHS R56 AI151372NIGMS NIH HHS R01 GM106105NIGMS NIH HHS R01 GM107465NIGMS NIH HHS R35 GM127094
6 · The paper itself

Abstract

When a ribosome encounters the stop codon of an mRNA, it terminates translation, releases the newly made protein, and is recycled to initiate translation on a new mRNA. Termination is a highly dynamic process in which release factors (RF1 and RF2 in bacteria; eRF1•eRF3•GTP in eukaryotes) coordinate peptide release with large-scale molecular rearrangements of the ribosome. Ribosomes stalled on aberrant mRNAs are rescued and recycled by diverse bacterial, mitochondrial, or cytoplasmic quality control mechanisms. These are catalyzed by rescue factors with peptidyl-tRNA hydrolase activity (bacterial ArfA•RF2 and ArfB, mitochondrial ICT1 and mtRF-R, and cytoplasmic Vms1), that are distinct from each other and from release factors. Nevertheless, recent structural studies demonstrate a remarkable similarity between translation termination and ribosome rescue mechanisms. This review describes how these pathways rely on inherent ribosome dynamics, emphasizing the active role of the ribosome in all translation steps.

Indexed as

BacteriaBacterial ProteinsCarboxylic Ester HydrolasesCytoplasmMitochondriaPeptide Chain Termination, TranslationalProtein BiosynthesisRibosomal ProteinsRibosomesRNA-Binding Proteinsaminoacyl-tRNA hydrolaseBacterial ProteinsCarboxylic Ester HydrolasesRibosomal ProteinsRNA-Binding Proteinsrescueribosometerminationtranslation

Identifiers

PMID34565314
PMCPMC8943824
OpenAlexW3200223938

What OpenQuestion holds

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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.