Evidence map›Paper›PMID 35472290›Full record

ReviewAnnual review of biomedical data science2022

Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes.

Fabián Morales-Polanco, Jae Ho Lee, Natália M Barbosa, Judith Frydman

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biomedical data science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chaperonin recognition of protein dynamics drives drug resistance.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Journal of virology · 2025
    Article
  13. Article
  14. A privileged ER compartment for posttranslational heteromeric assembly of an ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. The role of heat shock proteins in placental ischemic disease: A narrative review of the current literature.International journal of gynaecology and obstetrics: the official organ of the International Federation of Gynaecology and Obstetrics · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024
    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

4 authors at 1 institution in 1 country.

Fabián Morales-PolancoDepartment of Biology, Stanford University, Stanford, California, USA; email: jfrydman@stanford.edu.
Jae Ho LeeDepartment of Biology, Stanford University, Stanford, California, USA; email: jfrydman@stanford.edu.
Natália M BarbosaDepartment of Biology, Stanford University, Stanford, California, USA; email: jfrydman@stanford.edu.
Judith FrydmanDepartment of Biology, Stanford University, Stanford, California, USA; email: jfrydman@stanford.edu.
Stanford University · US

Funding

The proteasome in aging and neurodegenerative diseaseP01AG054407 · NIA · NORTHWESTERN UNIVERSITY · PI FINLEY, DANIEL J · 2018 to 2022
$14.0M
Training in Basic Research on Aging and Age-Related DiseaseT32AG000266 · NIA · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Lisa M Ellerby · 1998 to 2026
$13.8M
PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLR01GM056433 · NIGMS · STANFORD UNIVERSITY · PI Judith Frydman · 1997 to 2026
$5.0M
Protein Folding in the Eukaryotic CytosolR37GM056433 · NIGMS · STANFORD UNIVERSITY · PI FRYDMAN, JUDITH · 2013 to 2022
$4.6M
NIA NIH HHS P01 AG054407NIA NIH HHS T32 AG000266NIGMS NIH HHS R01 GM056433NIGMS NIH HHS R37 GM056433
6 · The paper itself

Abstract

The formation of protein complexes is crucial to most biological functions. The cellular mechanisms governing protein complex biogenesis are not yet well understood, but some principles of cotranslational and posttranslational assembly are beginning to emerge. In bacteria, this process is favored by operons encoding subunits of protein complexes. Eukaryotic cells do not have polycistronic mRNAs, raising the question of how they orchestrate the encounter of unassembled subunits. Here we review the constraints and mechanisms governing eukaryotic co- and posttranslational protein folding and assembly, including the influence of elongation rate on nascent chain targeting, folding, and chaperone interactions. Recent evidence shows that mRNAs encoding subunits of oligomeric assemblies can undergo localized translation and form cytoplasmic condensates that might facilitate the assembly of protein complexes. Understanding the interplay between localized mRNA translation and cotranslational proteostasis will be critical to defining protein complex assembly in vivo.

Indexed as

Protein BiosynthesisProtein FoldingMolecular ChaperonesRNA, MessengerSaccharomyces cerevisiaeMolecular ChaperonesRNA, Messengerchaperonescotranslational protein foldingHsp70nascent polypeptideorganelle targetingprotein complex assemblyRNA granulestranslation elongationTRiC/CCT

Identifiers

PMID35472290
PMCPMC11040709
OpenAlexW4224998205

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.