Evidence map›Paper›PMID 30626733›Full record

ReviewThe Journal of biological chemistry2019

Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic series.

Johannes Buchner

Abstract 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. A Workflow Guide to RNA-Seq Analysis of Chaperone Function and Beyond.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. Article
  19. Cytoplasmic molecular chaperones in Pseudomonas species.Journal of microbiology (Seoul, Korea) · 2022
    Review
  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

1 author.

Johannes BuchnerFrom the Department of Chemistry, Technical University of Munich, 85747 Garching, Germany johannes.buchner@tum.de.ORCID 0000-0003-1282-7737

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein folding is a spontaneous process. However, under physiological conditions, proteins are inherently unstable, and the protein concentrations in living cells favor unspecific interactions between partially folded proteins. Thus, the cellular proteome requires the assistance of helper factors, the molecular chaperones, for quality control and the maintenance of protein homeostasis. This series of reviews delves into how these molecular machines work in the eukaryotic cell, how they convey resilience to life, how these functions have allowed expansion of the protein universe, and how we can target them for therapeutic purposes. Together, they present the progress made in recent years in our understanding of one of the most fundamental aspects of life.

Indexed as

Protein FoldingProteostasisAnimalsHumansMolecular ChaperonesProteomeMolecular ChaperonesProteomechaperonechemical biologydrug designprotein assemblyprotein foldingribosome function

Identifiers

PMID30626733
PMCPMC6369298

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.