ArticleMolecules (Basel, Switzerland)2023
The Network Basis for the Structural Thermostability and the Functional Thermoactivity of Aldolase B.
Article in Molecules (Basel, Switzerland), 2023. 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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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Inactivation Switch for Run-up in TRPV2.Research square · 2026Article
- Thermodynamic coupling between cold and heat activations of TRPV2.Scientific reports · 2026Article
- Temperature-dependent gating pathways in TRPV3.Scientific reports · 2026Article
- Thermoring basis for the proton-driven heat activation of a cation-selective channel in myriapods.Scientific reports · 2025Article
- Pathway-dependent cold activation of heat-responsive TRPV channels.Scientific reports · 2025Article
- ATP-dependent thermoring basis for the heat unfolding of the first nucleotide-binding domain isolated from human CFTR.Research square · 2024Article
- Thermoring basis for the TRPV3 bio-thermometer.Scientific reports · 2023Article
- Thermal Ring-Based Heat Switches in Hyperthermophilic Class II Bacterial Fructose Aldolase.ACS omega · 2023Article
- Thermoring basis for the TRPV3 bio-thermometer.Research square · 2023Article
- Network Basis for the Heat-Adapted Structural Thermostability of Bacterial Class II Fructose Bisphosphate Aldolase.ACS omega · 2023Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermostability is important for the thermoactivity of proteins including enzymes. However, it is still challenging to pinpoint the specific structural factors for different temperature thresholds to initiate their specific structural and functional perturbations. Here, graph theory was used to investigate how the temperature-dependent noncovalent interactions as identified in the structures of aldolase B and its prevalent A149P mutant could form a systematic fluidic grid-like mesh network with topological grids to regulate the structural thermostability and the functional thermoactivity upon cyclization against decyclization in an extended range of a subunit. The results showed that the biggest grid may determine the melting temperature thresholds for the changes in their secondary and tertiary structures and specific catalytic activities. Further, a highly conserved thermostable grid may serve as an anchor to secure the flexible active site to achieve the specific thermoactivity. Finally, higher grid-based systematic thermal instability may disfavor the thermoactivity. Thus, this computational study may provide critical clues for the structural thermostability and the functional thermoactivity of proteins including enzymes.
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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.