
pmc: PMC1347452 , PMC148173 , PMC102440 , PMC308805
Peptidases (proteolytic enzymes) and their natural, protein inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these proteins. The organizational principle of the database is a hierarchical classification in which homologous sets of proteins of interest are grouped into families and the homologous families are grouped in clans. The most important addition to the database has been newly written, concise text annotations for each peptidase family. Other forms of information recently added include highlighting of active site residues (or the replacements that render some homologues inactive) in the sequence displays and BlastP search results, dynamically generated alignments and trees at the peptidase or inhibitor level, and a curated list of human and mouse homologues that have been experimentally characterized as active. A new way to display information at taxonomic levels higher than species has been devised. In the Literature pages, references have been flagged to draw attention to particularly 'hot' topics.
Databases, Factual, Protein Conformation, Molecular Sequence Data, Information Storage and Retrieval, Saccharomyces cerevisiae, Article, Substrate Specificity, Evolution, Molecular, Mice, User-Computer Interface, Sequence Analysis, Protein, Terminology as Topic, Animals, Humans, Protease Inhibitors, Amino Acid Sequence, Databases, Protein, Phylogeny, Expressed Sequence Tags, Internet, Genome, Binding Sites, Bacteria, Sequence Homology, Amino Acid, Computational Biology, Archaea, Pepsin A, Protein Structure, Tertiary, Sequence Alignment, Peptide Hydrolases
Databases, Factual, Protein Conformation, Molecular Sequence Data, Information Storage and Retrieval, Saccharomyces cerevisiae, Article, Substrate Specificity, Evolution, Molecular, Mice, User-Computer Interface, Sequence Analysis, Protein, Terminology as Topic, Animals, Humans, Protease Inhibitors, Amino Acid Sequence, Databases, Protein, Phylogeny, Expressed Sequence Tags, Internet, Genome, Binding Sites, Bacteria, Sequence Homology, Amino Acid, Computational Biology, Archaea, Pepsin A, Protein Structure, Tertiary, Sequence Alignment, Peptide Hydrolases
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 1K | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 0.1% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 0.1% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 1% |
