ReviewF1000Research2015
Molecular chaperones: guardians of the proteome in normal and disease states.
Review in F1000Research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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.
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.
Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- Major Oxidative and Antioxidant Mechanisms During Heat Stress-Induced Oxidative Stress in Chickens.Antioxidants (Basel, Switzerland) · 2025Review
- Proteomics Analysis of Proteotoxic Stress Response in In-Vitro Human Neuronal Models.International journal of molecular sciences · 2024Article
- Cellular Responses and Targets in Food Spoilage Yeasts Exposed to Antifungal Prenylated Isoflavonoids.Microbiology spectrum · 2023Article
- Overview of Sigma-1R Subcellular Specific Biological Functions and Role in Neuroprotection.International journal of molecular sciences · 2023Review
- Deciphering the mechanism and function of Hsp100 unfoldases from protein structure.Biochemical Society transactions · 2022Article
- Drug-Induced Hyperthermia Review.Cureus · 2022Review
- Review
- Effects of Cell Proteostasis Network on the Survival of SARS-CoV-2.Biological procedures online · 2021Review
- Mini Review: The Forensic Value of Heat Shock Proteins.Frontiers in medicine · 2021Review
- Catalysis of proline isomerization and molecular chaperone activity in a tug-of-war.Nature communications · 2020Article
- The role of rhomboid superfamily members in protein homeostasis: Mechanistic insight and physiological implications.Biochimica et biophysica acta. Molecular cell research · 2020Review
- HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF).International journal of molecular sciences · 2020Review
- Impact of HDAC Inhibitors on Protein Quality Control Systems: Consequences for Precision Medicine in Malignant Disease.Frontiers in cell and developmental biology · 2020Review
- Immunosurveillance of cancer and the heat shock protein-CD91 pathway.Cellular immunology · 2019Article
- Crystal Structure of the YcjX Stress Protein Reveals a Ras-Like GTP-Binding Protein.Journal of molecular biology · 2019Article
- Proteomic Analysis of Antigen 60 Complex ofVaccines · 2019Article
- Drug- and/or trauma-induced hyperthermia? Characterization of HSP70 and myoglobin expression.PloS one · 2018Article
- Expression times for hsp27 and hsp70 as an indicator of thermal stress during death due to fire.International journal of legal medicine · 2017Article
- Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.Scientific reports · 2017Article
- Expression of Hsp27 and Hsp70 and vacuolization in the pituitary glands in cases of fatal hypothermia.Forensic science, medicine, and pathology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Proteins must adopt a defined three-dimensional structure in order to gain functional activity, or must they? An ever-increasing number of intrinsically disordered proteins and amyloid-forming polypeptides challenge this dogma. While molecular chaperones and proteases are traditionally associated with protein quality control inside the cell, it is now apparent that molecular chaperones not only promote protein folding in the "forward" direction by facilitating folding and preventing misfolding and aggregation, but also facilitate protein unfolding and even disaggregation resulting in the recovery of functional protein from aggregates. Here, we review our current understanding of ATP-dependent molecular chaperones that harness the energy of ATP binding and hydrolysis to fuel their chaperone functions. An emerging theme is that most of these chaperones do not work alone, but instead function together with other chaperone systems to maintain the proteome. Hence, molecular chaperones are the major component of the proteostasis network that guards and protects the proteome from damage. Furthermore, while a decline of this network is detrimental to cell and organismal health, a controlled perturbation of the proteostasis network may offer new therapeutic avenues against human diseases.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.