Evidence map›Paper›PMID 36916749›Full record

ArticleBioEssays : news and reviews in molecular, cellular and developmental biology2023

Benefits of co-translational complex assembly for cellular fitness.

Krishnendu Khan, Paul L Fox

Open access · hybridAbstract read
In one paragraph

Article in BioEssays : news and reviews in molecular, cellular and developmental biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026
    Article
  3. Cotranslational assembly directs the biogenesis of the mProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
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 at 1 institution in 1 country.

Krishnendu KhanDepartment of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio, USA.
Paul L FoxDepartment of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio, USA.ORCID 0000-0002-6033-1528
Cleveland Clinic Lerner College of Medicine · US

Funding

Childhood-onset hypomyelinating leukodystrophy and the multi-tRNA synthetase complexR01NS124581 · NINDS · CLEVELAND CLINIC LERNER COM-CWRU · PI Ranjan Dutta, PAUL L FOX · 2023 to 2026
$2.5M
Adipokines, Aging, and Alzheimers DiseaseR01AG067146 · NIA · CLEVELAND CLINIC LERNER COM-CWRU · PI FOX, PAUL L · 2020 to 2024
$2.4M
The mammalian multi-tRNA synthetase complexR01NS124547 · NINDS · CLEVELAND CLINIC LERNER COM-CWRU · PI PAUL L FOX, Valentin Gogonea · 2022 to 2026
$2.4M
NIA NIH HHS R01 AG067146NINDS NIH HHS R01 NS124547NINDS NIH HHS R01 NS124581
6 · The paper itself

Abstract

Complexes of two or more proteins form many, if not most, of the intracellular "machines" that execute physical and chemical work, and transmit information. Complexes can form from stochastic post-translational interactions of fully formed proteins, but recent attention has shifted to co-translational interactions in which the most common mechanism involves binding of a mature constituent to an incomplete polypeptide emerging from a translating ribosome. Studies in yeast have revealed co-translational interactions during formation of multiple major complexes, and together with recent mammalian cell studies, suggest widespread utilization of the mechanism. These translation-dependent interactions can involve a single or multiple mRNA templates, can be uni- or bi-directional, and can use multi-protein sub-complexes as a binding component. Here, we discuss benefits of co-translational complex assembly including accuracy and efficiency, overcoming hidden interfaces, localized and hierarchical assembly, and reduction of orphan protein degradation, toxicity, and dominant-negative pathogenesis, all serving to improve cell fitness.

Indexed as

Protein BiosynthesisRibosomesAnimalsMammalsProteinsSaccharomyces cerevisiaeProteinscomplex assemblyco-translational interactionmRNA translationmultiprotein complexprotein-protein interactionribosome

Identifiers

PMID36916749
PMCPMC10121914
OpenAlexW4324129447

What OpenQuestion holds

Textmetadata
LicenceTDM
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.