ArticlePloS one2018
ProtDataTherm: A database for thermostability analysis and engineering of proteins.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 30 citations in OpenAlex.
- TemBERTure: advancing protein thermostability prediction with deep learning and attention mechanisms.Bioinformatics advances · 2024Article
- Systematic evaluation of computational tools to predict the effects of mutations on protein stability in the absence of experimental structures.Briefings in bioinformatics · 2022Article
- Making the cut with protease engineering.Cell chemical biology · 2022Review
- TEMPURA: Database of Growth TEMPeratures of Usual and RAre Prokaryotes.Microbes and environments · 2020Article
- A Method for Prediction of Thermophilic Protein Based on Reduced Amino Acids and Mixed Features.Frontiers in bioengineering and biotechnology · 2020Article
- Multidisciplinary involvement and potential of thermophiles.Folia microbiologica · 2019Review
- Role of simple descriptors and applicability domain in predicting change in protein thermostability.PloS one · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein thermostability engineering is a powerful tool to improve resistance of proteins against high temperatures and thereafter broaden their applications. For efficient protein thermostability engineering, different thermostability-classified data sources including sequences and 3D structures are needed for different protein families. However, no data source is available providing such data easily. It is the first release of ProtDataTherm database for analysis and engineering of protein thermostability which contains more than 14 million protein sequences categorized based on their thermal stability and protein family. This database contains data needed for better understanding protein thermostability and stability engineering. Providing categorized protein sequences and structures as psychrophilic, mesophilic and thermophilic makes this database useful for the development of new tools in protein stability prediction. This database is available at http://profiles.bs.ipm.ir/softwares/protdatatherm. As a proof of concept, the thermostability that improves mutations were suggested for one sample protein belonging to one of protein families with more than 20 mesophilic and thermophilic sequences and with known experimentally measured ΔT of mutations available within ProTherm database.
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Registered trials
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