ReviewFrontiers in molecular biosciences2018
A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.
Review in Frontiers in molecular biosciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed.
- Inhibition of rhizobial cheaters by the host Medicago truncatula involves repression of symbiotic functions and induction of defense.The New phytologist · 2025Article
- The Role of Heat Shock Protein (Hsp) Chaperones in Environmental Stress Adaptation and Virulence of Plant Pathogenic Bacteria.International journal of molecular sciences · 2025Review
- Molecular, structural, and functional characterization of delta subunit of T-complex protein-1 fromInfection and immunity · 2024Article
- Large-scale structure-informed multiple sequence alignment of proteins with SIMSApiper.Bioinformatics (Oxford, England) · 2024Article
- Implications of sperm heat shock protein 70-2 in bull fertility.Veterinary world · 2022Review
- The Possible Role of the Type I Chaperonins in Human Insulin Self-Association.Life (Basel, Switzerland) · 2022Article
- Chaperone-Mediated Autophagy and Its Implications for Neurodegeneration and Cancer.International journal of general medicine · 2022Review
- Heat shock protein 60 and cardiovascular diseases: An intricate love-hate story.Medicinal research reviews · 2021Review
- Hsp60 Post-translational Modifications: Functional and Pathological Consequences.Frontiers in molecular biosciences · 2020Review
- Alzheimer Cells on Their Way to Derailment Show Selective Changes in Protein Quality Control Network.Frontiers in molecular biosciences · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperonins are a subclass of molecular chaperones that assist cellular proteins to fold and assemble into their native shape. Much work has been done on Type I chaperonins, which has elucidated their elegant mechanism. Some debate remains about the details in these mechanisms, but nonetheless the roles of these in helping protein folding have been understood in great depth. In this review we discuss the known functions of atypical Type I chaperonins, highlighting evolutionary aspects that might lead chaperonins to perform alternate functions.
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Registered trials
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