ReviewProceedings of the National Academy of Sciences of the United States of America1999
Chaperone rings in protein folding and degradation.
Review in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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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.
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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.
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Who cites it
53 citing papers in PubMed, 188 citations in OpenAlex.
- Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023Article
- Crystal structures of dimeric and heptameric mtHsp60 reveal the mechanism of chaperonin inactivation.Life science alliance · 2023Article
- ClpC2 protects mycobacteria against a natural antibiotic targeting ClpC1-dependent protein degradation.Communications biology · 2023Article
- Trends in mitochondrial unfolded protein response research from 2004 to 2022: A bibliometric analysis.Frontiers in cell and developmental biology · 2023Review
- The ins and outs of Bacillus proteases: activities, functions and commercial significance.FEMS microbiology reviews · 2022Review
- Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Functional Diversity of AAA+ Protease Complexes inFrontiers in molecular biosciences · 2017Review
- Selenocystamine improves protein accumulation in chloroplasts of eukaryotic green algae.AMB Express · 2015Article
- Control of mitochondrial integrity in ageing and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Mechanisms of cellular proteostasis: insights from single-molecule approaches.Annual review of biophysics · 2014Review
- Article
- Putting handcuffs on the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The ubiquitin-proteasome system in retinal health and disease.Molecular neurobiology · 2013Review
- Mitochondrial stress: a bridge between mitochondrial dysfunction and metabolic diseases?Cellular signalling · 2011Review
- Molecular chaperone function for myocilin.Investigative ophthalmology & visual science · 2011Article
- Quality control of mitochondrial proteostasis.Cold Spring Harbor perspectives in biology · 2011Review
- Article
- The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.EMBO molecular medicine · 2009Article
- Localization of general and regulatory proteolysis in Bacillus subtilis cells.Molecular microbiology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperone rings play a vital role in the opposing ATP-mediated processes of folding and degradation of many cellular proteins, but the mechanisms by which they assist these life and death actions are only beginning to be understood. Ring structures present an advantage to both processes, providing for compartmentalization of the substrate protein inside a central cavity in which multivalent, potentially cooperative interactions can take place between the substrate and a high local concentration of binding sites, while access of other proteins to the cavity is restricted sterically. Such restriction prevents outside interference that could lead to nonproductive fates of the substrate protein while it is present in non-native form, such as aggregation. At the step of recognition, chaperone rings recognize different motifs in their substrates, exposed hydrophobicity in the case of protein-folding chaperonins, and specific "tag" sequences in at least some cases of the proteolytic chaperones. For both folding and proteolytic complexes, ATP directs conformational changes in the chaperone rings that govern release of the bound polypeptide. In the case of chaperonins, ATP enables a released protein to pursue the native state in a sequestered hydrophilic folding chamber, and, in the case of the proteases, the released polypeptide is translocated into a degradation chamber. These divergent fates are at least partly governed by very different cooperating components that associate with the chaperone rings: that is, cochaperonin rings on one hand and proteolytic ring assemblies on the other. Here we review the structures and mechanisms of the two types of chaperone ring system.
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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.