The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
Open accessAbstract
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology.The MEROPS database (http://merops. sanger.ac.uk) aims to fulfill the need for an integrated source of information about these.The database has hierarchical classifications in which homologous sets of peptidases and protein inhibitors are grouped into protein species, which are grouped into families, which are in turn grouped into clans.Recent developments include the following.A community annotation project has been instigated in which acknowledged experts are invited to contribute summaries for peptidases.Software has been written to provide an Internetbased data entry form.Contributors are acknowledged on the relevant web page.A new display showing the intron/exon structures of eukaryote peptidase genes and the phasing of the junctions has been implemented.It is now possible to filter the list of peptidases from a completely sequenced bacterial genome for a particular strain of the organism.The MEROPS filing pipeline has been altered to circumvent the restrictions imposed on non-interactive blastp searches, and a HMMER search using specially generated alignments to maximize the distribution of organisms returned in the search results has been added.
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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
Self-citationMEROPS: the peptidase database
Rawlings, N. D., Barrett, A. J., & Bateman, A. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp971 · Cited by 971
Self-citationEvolutionary families of peptidases
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Portune, K. J., Beaumont, M., Davila, A.-M., Tomé, D., Blachier, F., & Sanz, Y. (2016) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2016.08.011 · Cited by 356
Kant, M. R., Jonckheere, W., Knegt, B., Lemos, F., Liu, J., Schimmel, B. C. J., Villarroel, C. A., Ataide, L. M. S., Dermauw, W., Glas, J. J., et al. (2015) · Annals of Botany · doi:10.1093/aob/mcv054 · Cited by 360
He, Y., Li, M., Perumal, V., Feng, X., Fang, J., Xie, J., Sievert, S. M., & Wang, F. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.35 · Cited by 346
Eckhard, U., Huesgen, P. F., Schilling, O., Bellac, C. L., Butler, G. S., Cox, J. H., Dufour, A., Goebeler, V., Kappelhoff, R., Keller, U. A. D., et al. (2016) · Matrix Biology · doi:10.1016/j.matbio.2015.09.003 · Cited by 212
Metadata
- Authors
- Rawlings, N. D., Waller, M., Barrett, A. J., & Bateman, A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-10-23
- Volume
- 42
- Issue
- D1
- Pages
- D503-D509
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W4230386739
- Cited by
- 873
- References
- 22
- FWCI
- 32.18
- Type
- journal article
- Language
- en
- Open access
- gold
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