The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions
Open accessAbstract
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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Cites
Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,355
FastTree 2 – Approximately Maximum-Likelihood Trees for Large Alignments
Price, M. N., Dehal, P. S., & Arkin, A. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009490 · Cited by 14,894
The Pfam Protein Families Database
Bateman, A. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,000
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
Cantarel, B. L., Coutinho, P. M., Rancurel, C., Bernard, T., Lombard, V., & Henrissat, B. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn663 · Cited by 5,972
The Pfam protein families database
Punta, M., Coggill, P. C., Eberhardt, R. Y., Mistry, J., Tate, J., Boursnell, C., Pang, N., Forslund, K., Ceric, G., Clements, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1065 · Cited by 3,719
Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., et al. (1992) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/5.3.197 · Cited by 2,120
MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
Rawlings, N. D., Barrett, A. J., & Bateman, A. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr987 · Cited by 1,544
Jaeger, K.-E., & Eggert, T. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00341-5 · Cited by 1,376
Bacterial lipolytic enzymes: classification and properties
Arpigny, J. L., & Jaeger, K. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3430177 · Cited by 1,236
Reorganizing the protein space at the Universal Protein Resource (UniProt)
The UniProt Consortium (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr981 · Cited by 1,220
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Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate
Palm, G. J., Reisky, L., Böttcher, D., Müller, H., Michels, E. A. P., Walczak, M. C., Berndt, L., Weiss, M. S., Bornscheuer, U. T., & Weber, G. (2019) · Nature Communications · doi:10.1038/s41467-019-09326-3 · Cited by 491
Spang, A., Stairs, C. W., Dombrowski, N., Eme, L., Lombard, J., Caceres, E. F., Greening, C., Baker, B. J., & Ettema, T. J. G. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0406-9 · Cited by 200
Sommer, B., Overy, D. P., Haltli, B., & Kerr, R. G. (2016) · Microbiology · doi:10.1099/mic.0.000299 · Cited by 32
(2023) · doi:10.1128/aem.01704-22 · Cited by 25
Varejão, N., De-Andrade, R. A., Almeida, R. V., Anobom, C. D., Foguel, D., & Reverter, D. (2018) · Structure · doi:10.1016/j.str.2017.12.004 · Cited by 14
Metadata
- Authors
- Lenfant, N., Hotelier, T., Velluet, E., Bourne, Y., Marchot, P., & Chatonnet, A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2012-11-26
- Volume
- 41
- Issue
- D1
- Pages
- D423-D429
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2108923073
- Cited by
- 317
- References
- 35
- FWCI
- 6.08
- Type
- journal article
- Language
- en
- Open access
- gold
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- Lenfant, N., Hotelier, T., Velluet, E., Bourne, Y., Marchot, P., & Chatonnet, A. (2012). ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Research. https://doi.org/10.1093/nar/gks1154
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