Evidence map›Paper›PMID 23395271›Full record

ReviewMolecular cell2013

The ribosome as a hub for protein quality control.

Sebastian Pechmann, Felix Willmund, Judith Frydman

Abstract readReview
In one paragraph

Review in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.

0numbers the graph read from it
0cells of the map it votes in
161citing 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

161 citing papers in PubMed.

  1. Article
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  11. Review
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  13. Heterogeneous folding landscapes and predetermined breaking points within a protein family.Protein science : a publication of the Protein Society · 2024
    Article
  14. Article
  15. Article
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  20. Article

101 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

3 authors.

Sebastian PechmannDepartment of Biology, Stanford University, Stanford, CA 94305-5020, USA.
Felix Willmund
Judith Frydman

Funding

Unbiased Functional Characterization of Enterovirus-Host InteractionsP01AI091575 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ANDINO, RAUL · 2011 to 2015
$10.5M
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
NIAID NIH HHS AI91575NIAID NIH HHS P01 AI091575NIGMS NIH HHS GM56433NIGMS NIH HHS R01 GM056433NIGMS NIH HHS R37 GM056433
6 · The paper itself

Abstract

Cells face a constant challenge as they produce new proteins. The newly synthesized polypeptides must be folded properly to avoid aggregation. If proteins do misfold, they must be cleared to maintain a functional and healthy proteome. Recent work is revealing the complex mechanisms that work cotranslationally to ensure protein quality control during biogenesis at the ribosome. Indeed, the ribosome is emerging as a central hub in coordinating these processes, particularly in sensing the nature of the nascent protein chain, recruiting protein folding and translocation components, and integrating mRNA and nascent chain quality control. The tiered and complementary nature of these decision-making processes confers robustness and fidelity to protein homeostasis during protein synthesis.

Indexed as

Protein FoldingAnimalsBiophysical PhenomenaHomeostasisHumansProtein BiosynthesisProteinsRibosomesProteins

Identifiers

PMID23395271
PMCPMC3593112

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.