ArticleNature communications2025
Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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Who cites it
7 citing papers in PubMed.
- Disease-Associated Mutations Impact DNA Methyltransferase 1 Function through Dynamic Allosteric Effects and Solvent Exposure.Journal of chemical theory and computation · 2026Article
- Review
- Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress.Science advances · 2026Article
- Aberrant mitochondrial hsp60 expression affects mitochondria homeostasis and results in muscle dystrophy and premature death.Cell death & disease · 2026Article
- Density Functional Theory Calculations to Investigate the Role Played by an Aspartate Dyad in Hsp60-Catalyzed ATP Hydrolysis.The journal of physical chemistry letters · 2025Article
- Impact of Genetic Variants Associated with Neurodevelopmental Disorders on the WAVE Regulatory Complex.Journal of chemical information and modeling · 2025Article
- Common characteristics of variants linked to autism spectrum disorder in the WAVE regulatory complex.Frontiers in computational neuroscience · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Mitochondrial chaperonin Heat Shock Protein 60 kDa (Hsp60) oversees the correct folding of client proteins in cooperation with Hsp10. Hsp60 monomers M first form 7-meric Single rings (S), which then pair into 14-meric Double rings (D) that accommodate clients in their lumen. Recruitment of 7 Hsp10 molecules per pole yields a sealed 28-meric Football-shaped complex (F). ATP hydrolysis in each Hsp60 unit drives client folding and F disassembly. The V72I mutation in hereditary spastic paraplegia form SPG13 impairs Hsp60 function despite being distant from the active site. We here investigate this impairment with atomistic molecular dynamics (MD) simulations of M, S, D, and F for both WT and mutant Hsp60, considering catalytic aspartates in D and F in different protonation states (even simulating one such state of D post-hydrolysis). Our findings show that-as observed experimentally-V72I rigidifies Hsp60 assemblies, significantly impacting internal dynamics. In monomers, V72I introduces a new allosteric route that bypasses the ATP binding site and affects mechanisms driving reactivity. These insights highlight a multiscale complexity of Hsp60 that could inspire the design of experiments to better understand both its WT and V72I variants.
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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 Socratic graph.