ArticleNucleic acids research2013
ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.
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140 citing papers in PubMed, 1 synthesis or guideline pooled it.
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- Phylogenomic Insights into High Conservation and Lineage-Specific Expansion of the ABAPT Gene Family in Plants.International journal of molecular sciences · 2026Article
- Thermostable Bacterial Esterases From Lipase Family 1.5 Degrade Compostable Polyesters PBAT and PBSA.MicrobiologyOpen · 2025Article
- The Role of Omics Technology in Evaluating Plastic Pollution's Effects on Plants: A Comprehensive Review.International journal of molecular sciences · 2025Review
- It Is Dangerous to Go Alone: Strategies to Optimize PET Biocatalysis and Upcycling through Enzymatic Synergism.ACS omega · 2025Review
- Catalytic His-loop flexibility drives high activity in hyperthermophilic esterase EstE1 while preserving structural stability.Microbiology spectrum · 2025Article
- Identification of Urethanases for Biocatalytic Recycling of Toluene Diisocyanate- and Methylene Diphenyl Diisocyanate-Based Polyurethanes.ChemSusChem · 2025Article
- α/β Hydrolases: Toward Unraveling Entangled Classification.Proteins · 2025Article
- Genomic, Transcriptomic and Suspect/Non-Target Screening Analyses Reveal the Role of CYP450s in the Degradation of Imazalil and Delineate Its Transformation Pathway by Cladosporium herbarum.Microbial biotechnology · 2025Article
- Identifying representative sequences of protein families using submodular optimization.Scientific reports · 2025Article
- Bioinformatics Analysis Suggests That SE_1780 Protein FrommicroPublication biology · 2025Article
- An ecological-evolutionary perspective on the genomic diversity and habitat preferences of theMicrobial genomics · 2025Article
- Increased spontaneous physical activity in female MEST-deficient mice protects against diet-induced obesity.Frontiers in endocrinology · 2025Article
- Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.Frontiers in microbiology · 2025Article
- Structure-based clustering and mutagenesis of bacterial tannases reveals the importance and diversity of active site-capping domains.Protein science : a publication of the Protein Society · 2024Article
- The predicted secreted proteome of activated sludge microorganisms indicates distinct nutrient niches.mSystems · 2024Article
- Comprehensive Insights into Microbial Lipases: Unveiling Structural Dynamics, Catalytic Mechanism, and Versatile Applications.Current microbiology · 2024Review
- In Silico Analysis and Biochemical Characterization ofJournal of microbiology and biotechnology · 2024Article
80 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
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Abstract
The ESTHER database, which is freely available via a web server (http://bioweb.ensam.inra.fr/esther) and is widely used, is dedicated to proteins with an α/β-hydrolase fold, and it currently contains >30 000 manually curated proteins. Herein, we report those substantial changes towards improvement that we have made to improve ESTHER during the past 8 years since our 2004 update. In particular, we generated 87 new families and increased the coverage of the UniProt Knowledgebase (UniProtKB). We also renewed the ESTHER website and added new visualization tools, such as the Overall Table and the Family Tree. We also address two topics of particular interest to the ESTHER users. First, we explain how the different enzyme classifications (bacterial lipases, peptidases, carboxylesterases) used by different communities of users are combined in ESTHER. Second, we discuss how variations of core architecture or in predicted active site residues result in a more precise clustering of families, and whether this strategy provides trustable hints to identify enzyme-like proteins with no catalytic activity.
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