A. Barrett

Publications278
h-index87
Citations29,692
Highly Influential Citations1,090
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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
TLDR
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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Cathepsin B, Cathepsin H, and cathepsin L.
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Handbook of proteolytic enzymes
(Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of Clan…
MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
TLDR
The MEROPS database has been expanded to include proteolytic enzymes other than peptidases, and the inclusion of small-molecule inhibitors in the tables of peptidase–inhibitor interactions is included.
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The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database
TLDR
Insight is given into the origins and evolution of peptidase families, including an expansion in the number of proteasome components in Asgard archaeotes and as organisms increase in complexity.
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Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors
The MEROPS database (http://merops.sanger.ac.uk) is an integrated source of information about peptidases, their substrates and inhibitors, which are of great relevance to biology, medicine and…
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[41] Cathepsin B, cathepsin H, and cathepsin L
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L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.
TLDR
It was shown that the rapid stoichiometric reaction of the cysteine proteinases related to papain can be used to determine the operational molarity of solutions of the enzymes and thus to calibrate rate assays.
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Cloning, Isolation, and Characterization of Mammalian Legumain, an Asparaginyl Endopeptidase*
TLDR
The mammalian sequences are clearly homologous with legumains from non-mammalian species and the significance of the discovery of a cysteine endopeptidase of a new family and distinctive specificity in man and other mammals is discussed.
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Evolutionary families of metallopeptidases.
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