ReviewFrontiers in molecular biosciences2016
Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.
Review in Frontiers in molecular biosciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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
21 citing papers in PubMed, 38 citations in OpenAlex.
- Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress.Science advances · 2026Article
- Hsp60-Bearing Exosomes inCells · 2025Review
- Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states.Nature communications · 2025Article
- Targeted Analysis of Mitochondrial Protein Conformations and Interactions by Endogenous ROS-Triggered Cross-Linker Release.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Glutamine sustains energy metabolism and alleviates liver injury in burn sepsis by promoting the assembly of mitochondrial HSP60-HSP10 complex via SIRT4 dependent protein deacetylation.Redox report : communications in free radical research · 2024Article
- Impact of Non-Invasive Physical Plasma on Heat Shock Protein Functionality in Eukaryotic Cells.Biomedicines · 2023Article
- Review
- Editorial: A focus on chaperone clients.Frontiers in molecular biosciences · 2023Article
- Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities.MedComm · 2022Review
- Allosteric differences dictate GroEL complementation of E. coli.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Heat shock proteins with an emphasis on HSP 60.Molecular biology reports · 2021Review
- Failure to Guard: Mitochondrial Protein Quality Control in Cancer.International journal of molecular sciences · 2021Review
- Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.Scientific reports · 2021Article
- Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.The Plant cell · 2020Article
- Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin.Nature communications · 2020Article
- Hsp60 Post-translational Modifications: Functional and Pathological Consequences.Frontiers in molecular biosciences · 2020Review
- Bridging human chaperonopathies and microbial chaperonins.Communications biology · 2019Review
- Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics.Frontiers in molecular biosciences · 2018Review
- Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications.Frontiers in molecular biosciences · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The GroEL-GroES chaperonin system is probably one of the most studied chaperone systems at the level of the molecular mechanism. Since the first reports of a bacterial gene involved in phage morphogenesis in 1972, these proteins have stimulated intensive research for over 40 years. During this time, detailed structural and functional studies have yielded constantly evolving concepts of the chaperonin mechanism of action. Despite of almost three decades of research on this oligomeric protein, certain aspects of its function remain controversial. In this review, we highlight one central aspect of its function, namely, the active intermediates of its reaction cycle, and present how research to this day continues to change our understanding of chaperonin-mediated protein folding.
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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.