Evidence map›Paper›PMID 26225966›Full record

ReviewInternational journal of molecular sciences2015

Protein Folding and Mechanisms of Proteostasis.

José Fernando Díaz-Villanueva, Raúl Díaz-Molina, Victor García-González

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 325 citations in OpenAlex.

  1. Review
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  9. Review
  10. Molecular underpinnings of induced degenerative heterogeneity in the retinal pigment epithelium.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Review
  12. Article
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  18. 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
  19. Article
  20. Neutralization of the Pandemic Influenza A/H1N1 Virus withAntibodies (Basel, Switzerland) · 2025
    Article

92 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 at 1 institution in 1 country.

José Fernando Díaz-VillanuevaFacultad de Medicina, Universidad Autónoma de Baja California, Mexicali, Baja California 21000, México. jdiaz92@uabc.edu.mx.
Raúl Díaz-MolinaFacultad de Medicina, Universidad Autónoma de Baja California, Mexicali, Baja California 21000, México. rauldiaz@uabc.edu.mx.
Victor García-GonzálezFacultad de Medicina, Universidad Autónoma de Baja California, Mexicali, Baja California 21000, México. vgarcia62@uabc.edu.mx.
Universidad Autónoma de Baja California · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Highly sophisticated mechanisms that modulate protein structure and function, which involve synthesis and degradation, have evolved to maintain cellular homeostasis. Perturbations in these mechanisms can lead to protein dysfunction as well as deleterious cell processes. Therefore in recent years the etiology of a great number of diseases has been attributed to failures in mechanisms that modulate protein structure. Interconnections among metabolic and cell signaling pathways are critical for homeostasis to converge on mechanisms associated with protein folding as well as for the preservation of the native structure of proteins. For instance, imbalances in secretory protein synthesis pathways lead to a condition known as endoplasmic reticulum (ER) stress which elicits the adaptive unfolded protein response (UPR). Therefore, taking this into consideration, a key part of this paper is developed around the protein folding phenomenon, and cellular mechanisms which support this pivotal condition. We provide an overview of chaperone protein function, UPR via, spatial compartmentalization of protein folding, proteasome role, autophagy, as well as the intertwining between these processes. Several diseases are known to have a molecular etiology in the malfunction of mechanisms responsible for protein folding and in the shielding of native structure, phenomena which ultimately lead to misfolded protein accumulation. This review centers on our current knowledge about pathways that modulate protein folding, and cell responses involved in protein homeostasis.

Indexed as

Protein UnfoldingUnfolded Protein ResponseAnimalsHomeostasisHumansMolecular ChaperonesMolecular Chaperonesfoldingmisfoldingproteinsproteostasis

Identifiers

PMID26225966
PMCPMC4581189
OpenAlexW1927299328

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.