MEROPS: the peptidase database
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TLDR
The MEROPS database has added an analysis tool to the relevant species pages to show significant gains and losses of peptidase genes relative to related species, and has collected over 39 000 known cleavage sites in proteins, peptides and synthetic substrates.Abstract:
Peptidases (proteolytic enzymes) are of great relevance to biology, medicine and biotechnology. This practical importance creates a need for an integrated source of information about them, and also about their natural inhibitors. The MEROPS database (http://merops.sanger.ac.uk) aims to fill this need. The organizational principle of the database is a hierarchical classification in which homologous sets of the proteins of interest are grouped in families and the homologous families are grouped in clans. Each peptidase, family and clan has a unique identifier. The database has recently been expanded to include the protein inhibitors of peptidases, and these are classified in much the same way as the peptidases. Forms of information recently added include new links to other databases, summary alignments for peptidase clans, displays to show the distribution of peptidases and inhibitors among organisms, substrate cleavage sites and indexes for expressed sequence tag libraries containing peptidases. A new way of making hyperlinks to the database has been devised and a BlastP search of our library of peptidase and inhibitor sequences has been added.read more
Citations
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Systems biology-opportunities and challenges: the application of proteomics to study the cardiovascular extracellular matrix.
TL;DR: This review discusses decellularization-based methods that enrich for ECM proteins in cardiac tissue, and how targeted MS allows for accurate protein quantification and on the release of matrix fragments with biological activity (matrikines), all of which can be interrogated by proteomic techniques.
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Genome analysis reveals evolutionary mechanisms of adaptation in systemic dimorphic fungi.
TL;DR: Comparisons of genomes of classic systemic, opportunistic, and non-pathogenic species revealed that independent changes in nutrient acquisition capacity have occurred in the Onygenaceae and Ajellomycetaceae, and underlie how the dimorphic pathogens have adapted to the human host and decreased their capacity for growth in environmental niches.
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Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts
Stefan Tholen,Martin L. Biniossek,Anna-Lena Gessler,Sebastian Müller,Juliane Weisser,Jayachandran N. Kizhakkedathu,Thomas Reinheckel,Oliver Schilling +7 more
TL;DR: Quantitative proteomic comparison of cell conditioned media indicated that cathepsin L deficiency affects, albeit in a limited manner, the abundances of extracellular matrix (ECM) components, signaling proteins, and further proteases as well as endogenous protease inhibitors.
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N-acetylamino acid utilization by kidney aminoacylase-1.
TL;DR: Detailed N-acetylamino acid specificity profiles for human and porcine Acy1 are reported and uptake and utilization of N-acteylleucine and -methionine in replacement of the free amino acid, respectively, in cultured epithelial cells are demonstrated.
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Colocalization of a carnosine-splitting enzyme, tissue carnosinase (CN2)/cytosolic non-specific dipeptidase 2 (CNDP2), with histidine decarboxylase in the tuberomammillary nucleus of the hypothalamus.
TL;DR: Investigation of the immunohistochemical localization of CN2 in the hypothalamus suggests that CN2 is highly expressed in the histaminergic neurons in the tuberomammillary nucleus, implying that it may supply histidine to histamine neurons for histamine synthesis.
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