Evidence map›Paper›PMID 34391802›Full record

ReviewJournal of molecular biology2021

The Proteome Folding Problem and Cellular Proteostasis.

Evan T Powers, Lila M Gierasch

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Supervised learning of protein variant effects across large-scale mutagenesis datasets.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. Factors affecting protein recovery during Hsp40 affinity profiling.Analytical and bioanalytical chemistry · 2024
    Article
  12. A mutational atlas for Parkin proteostasis.Nature communications · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. HSP70-binding motifs function as protein quality control degrons.Cellular and molecular life sciences : CMLS · 2023
    Article
  17. Review
  18. Article
  19. Article
  20. 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

2 authors.

Evan T PowersDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: epowers@scripps.edu.
Lila M GieraschDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts-Amherst, Amherst, MA 01003, USA. Electronic address: gierasch@biochem.umass.edu.

Funding

The proteasome in aging and neurodegenerative diseaseP01AG054407 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2018 to 2022
$14.0M
Protein folding in the cell: Challenges and coping mechanisms Administrative Supplement for Equipment PurchaseR35GM118161 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2016 to 2025
$5.5M
NIA NIH HHS P01 AG054407NIGMS NIH HHS R35 GM118161
6 · The paper itself

Abstract

Stunning advances have been achieved in addressing the protein folding problem, providing deeper understanding of the mechanisms by which proteins navigate energy landscapes to reach their native states and enabling powerful algorithms to connect sequence to structure. However, the realities of the in vivo protein folding problem remain a challenge to reckon with. Here, we discuss the concept of the "proteome folding problem"-the problem of how organisms build and maintain a functional proteome-by admitting that folding energy landscapes are characterized by many misfolded states and that cells must deploy a network of chaperones and degradation enzymes to minimize deleterious impacts of these off-pathway species. The resulting proteostasis network is an inextricable part of in vivo protein folding and must be understood in detail if we are to solve the proteome folding problem. We discuss how the development of computational models for the proteostasis network's actions and the relationship to the biophysical properties of the proteome has begun to offer new insights and capabilities.

Indexed as

Protein FoldingProteostasisAnimalsHumansMolecular ChaperonesProteomeMolecular ChaperonesProteomechaperoneenergy landscapeprotein foldingproteome foldingproteostasis

Identifiers

PMID34391802
PMCPMC8502207

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.