ReviewThe Journal of biological chemistry2017
Chaperone-client interactions: Non-specificity engenders multifunctionality.
Review in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed.
- Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Oligomeric State and Holding Activity of Hsp60.International journal of molecular sciences · 2023Article
- The Molecular Chaperone Mechanism of the C-Terminal Domain of Large-Size Subunit Catalases.Antioxidants (Basel, Switzerland) · 2023Article
- Real-time single-molecule observation of chaperone-assisted protein folding.Science advances · 2022Article
- Article
- An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated RidA.Redox biology · 2022Article
- Insights into the client protein release mechanism of the ATP-independent chaperone Spy.Nature communications · 2022Article
- Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen PhosphorylaseInternational journal of molecular sciences · 2022Article
- The interactions of molecular chaperones with client proteins: why are they so weak?The Journal of biological chemistry · 2021Review
- Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.mBio · 2021Article
- Mechanism of the small ATP-independent chaperone Spy is substrate specific.Nature communications · 2021Article
- Proteotoxicity: A Fatal Consequence of Environmental Pollutants-Induced Impairments in Protein Clearance Machinery.Journal of personalized medicine · 2021Review
- Review
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
- Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.The Journal of biological chemistry · 2020Article
- Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery.Acta pharmaceutica Sinica. B · 2020Review
- Article
- Successes and challenges in simulating the folding of large proteins.The Journal of biological chemistry · 2020Review
- Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease.Advances in experimental medicine and biology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Here, we provide an overview of the different mechanisms whereby three different chaperones, Spy, Hsp70, and Hsp60, interact with folding proteins, and we discuss how these chaperones may guide the folding process. Available evidence suggests that even a single chaperone can use many mechanisms to aid in protein folding, most likely due to the need for most chaperones to bind clients promiscuously. Chaperone mechanism may be better understood by always considering it in the context of the client's folding pathway and biological function.
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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.