Evidence map›Paper›PMID 30504455›Full record

ReviewThe Journal of biological chemistry2019

The stop-and-go traffic regulating protein biogenesis: How translation kinetics controls proteostasis.

Kevin C Stein, Judith Frydman

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

93 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The regulation, function and disease relevance of cytoplasmic tRNAs.Nature reviews. Molecular cell biology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Translational landscape during seed germination revealed by ribosome profiling.The Plant journal : for cell and molecular biology · 2026
    Article
  13. Energetic and structural control of polyspecificity in a multidrug transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Predicting gene sequences with AI to study codon usage patterns.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

33 more citing papers are in PubMed but not listed here.

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.

Kevin C SteinFrom the Departments of Biology and.ORCID 0000-0002-0622-8319
Judith FrydmanFrom the Departments of Biology and jfrydman@stanford.edu.
Stanford University · US

Funding

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
Stanford Training Program in Aging ResearchT32AG047126 · NIA · STANFORD UNIVERSITY · PI VYJEYANTHI S PERIYAKOIL, TONY WYSS-CORAY · 2014 to 2026
$4.3M
NIA NIH HHS T32 AG047126NIGMS NIH HHS R01 GM056433NIGMS NIH HHS R37 GM056433
6 · The paper itself

Abstract

Generating a functional proteome requires the ribosome to carefully regulate disparate co-translational processes that determine the fate of nascent polypeptides. With protein synthesis being energetically expensive, the ribosome must balance the costs of efficiently making a protein with those of properly folding it. Emerging as a primary means of regulating this trade-off is the nonuniform rate of translation elongation that defines translation kinetics. The varying speeds with which the ribosome progresses along a transcript have been implicated in several aspects of protein biogenesis, including co-translational protein folding and translational fidelity, as well as gene expression by mediating mRNA decay and protein quality control pathways. The optimal translation kinetics required to efficiently execute these processes can be distinct. Thus, the ribosome is tasked with tightly regulating translation kinetics to balance these processes while maintaining adaptability for changing cellular conditions. In this review, we first discuss the regulatory role of translation elongation in protein biogenesis and what factors influence elongation kinetics. We then describe how changes in translation kinetics signal downstream pathways that dictate the fate of nascent polypeptides. By regulating these pathways, the kinetics of translation elongation has emerged as a critical tool for driving gene expression and maintaining proteostasis through varied mechanisms, including nascent chain folding and binding different ribosome-associated machinery. Indeed, a growing number of examples demonstrate the important role of local changes in elongation kinetics in modulating the pathophysiology of human disease.

Indexed as

Peptide Chain Elongation, TranslationalProtein FoldingProteostasisAnimalsHumansKineticsProteomeProteomechaperonecotranslational foldingelongation ratenascent chainprotein foldingprotein misfoldingribosome functiontranslationtranslational fidelity

Identifiers

PMID30504455
PMCPMC6369277
OpenAlexW2902674068

What OpenQuestion 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 OpenQuestion graph.