MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
By Neil D. Rawlings, Matthew Waller, Alan J. Barrett, Alex Bateman. Nucleic Acids Res., 2013
1,190 citations recorded by the source corpus.
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 Internet-based 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.
Subfields: Biotechnology, Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/5fec3cda0d994c217c737c10b0b7e56d4574edca
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Citations in the corpus
- Biochemistry and physiological functions of ADAMTS7 metalloprotease (2013, background): “Recently, a microRNA, miR-29a/b, was found to play a role in regulating ADAMTS7 expression (Figure2) [25].”
- BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA (2012, neutral): “Merops (22), MODOMICS (23), CAZy (24), Kinomer (25)].”
- Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, neutral): “Among the >800 proteases encoded by a plant genome, ~140 correspond to cysteine proteases (CysProts) that belong to 15 families distributed in five clans as classified in the MEROPS peptidase database (Rawlings et al., 2012).”