PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6626500-1 1983 Kinetic evidence for involvement of aspartic acid at position P10. Aspartic Acid 36-49 S100 calcium binding protein A10 Homo sapiens 62-65 12506111-7 2003 We have found that cleavage of procaspase-9 at Asp(330) to generate p35, p10 or p37, p10 forms resulted in a significant increase (up to 8-fold) in apoptosome activity compared with p35/p12. Aspartic Acid 47-50 S100 calcium binding protein A10 Homo sapiens 73-76 12506111-7 2003 We have found that cleavage of procaspase-9 at Asp(330) to generate p35, p10 or p37, p10 forms resulted in a significant increase (up to 8-fold) in apoptosome activity compared with p35/p12. Aspartic Acid 47-50 S100 calcium binding protein A10 Homo sapiens 85-88 12506111-9 2003 In addition, cleavage at Asp(330) exposed a novel p10 NH(2)-terminal peptide motif (AISS) that retained the ability to mediate XIAP inhibition of caspase-9. Aspartic Acid 25-28 S100 calcium binding protein A10 Homo sapiens 50-53 18258633-8 2008 The replacement of the residues of aspartic acid in position 5 or those of alanine in position 6 in the sequence of p10mer resulted in peptides with no activity in the activation experiments. Aspartic Acid 35-48 S100 calcium binding protein A10 Homo sapiens 116-119