ArticleBiophysical journal2019
A Dynamic Hydrophobic Core and Surface Salt Bridges Thermostabilize a Designed Three-Helix Bundle.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
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Who cites it
14 citing papers in PubMed.
- Unlocking the molecular engineering of Geobacillus glycoside hydrolases as a source of industrial biocatalysts.Biotechnology letters · 2026Review
- Designing Novel Aspartic Protease (NAP) Using Ancestral Sequence Reconstruction (ASR) for Cheesemaking.Molecular biotechnology · 2026Article
- Thermostable Proteases fromMicroorganisms · 2025Review
- Enhancing the Thermostability ofMolecules (Basel, Switzerland) · 2025Article
- dUTP pyrophosphatases from hyperthermophilic eubacterium and archaeon: Structural and functional examinations on the suitability for PCR application.Protein science : a publication of the Protein Society · 2024Article
- Computer-aided design of novel cellobiose 2-epimerase for efficient synthesis of lactulose using lactose.Bioprocess and biosystems engineering · 2023Article
- Thermostability engineering of industrial enzymes through structure modification.Applied microbiology and biotechnology · 2022Review
- The stability and dynamics of computationally designed proteins.Protein engineering, design & selection : PEDS · 2022Review
- Thermostabilization mechanisms in thermophilic versus mesophilic three-helix bundle proteins.Journal of computational chemistry · 2022Article
- Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.Biophysical journal · 2021Article
- Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases.Biophysical journal · 2021Article
- Recent Progress Using De Novo Design to Study Protein Structure, Design and Binding Interactions.Life (Basel, Switzerland) · 2021Review
- The Role of Electrostatics and Folding Kinetics on the Thermostability of Homologous Cold Shock Proteins.Journal of chemical information and modeling · 2020Article
- Molecular dynamics simulations suggest stabilizing mutations in a de novo designed α/β protein.Protein engineering, design & selection : PEDS · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermostable proteins are advantageous in industrial applications, as pharmaceuticals or biosensors, and as templates for directed evolution. As protein-design methodologies improve, bioengineers are able to design proteins to perform a desired function. Although many rationally designed proteins end up being thermostable, how to intentionally design de novo, thermostable proteins is less clear. UVF is a de novo-designed protein based on the backbone structure of the Engrailed homeodomain (EnHD) and is highly thermostable (T
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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.