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- aggregation classification "A1".
- aggregation creator B191848.
- aggregation creator B191849.
- aggregation creator B191850.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2010".
- aggregation format "application/pdf".
- aggregation hasFormat 1064461.bibtex.
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- aggregation isPartOf urn:issn:1431-6730.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "The substrate specificity profile of human granzyme A".
- aggregation abstract "The exact biological function of granzyme A, a granule-associated serine protease belonging to the tryptase family of proteases, is still a matter of debate because conflicting roles have been suggested, such as initiation of caspase-independent apoptosis-like cell death and endogenous modulation of inflammatory processes. In contrast to its well-studied family member, granzyme B, far less is known about the physiological targets of granzyme A. Using an N-terminal peptide-centric proteomics technology, the substrate specificity of human granzyme A was extensively characterized at the level of macromolecular protein substrates. Overall, more than 260 cleavage sites, almost exclusively favoring basic residues at the P1 position, in approximately 200 unique protein substrates, including the well-known in vitro substrates APEX-endonuclease 1 and different histones, were identified. Further substrate characterization was used to delineate physical properties in the substrate specificity profiles, which further highlights important aspects in protease/substrate biology.".
- aggregation authorList BK451768.
- aggregation endPage "997".
- aggregation issue "8".
- aggregation startPage "983".
- aggregation volume "391".
- aggregation aggregates 3112383.
- aggregation isDescribedBy 1064461.
- aggregation similarTo BC.2010.096.
- aggregation similarTo LU-1064461.