PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31910706-5 2020 Caspases (cysteine aspartic proteases and cysteine aspartases) are cysteine dependent aspartate-specific proteases. Aspartic Acid 86-95 caspase 8 Homo sapiens 0-8 20202478-7 2010 Several distinctive features of sea bass caspase-8 were identified, which include two death effector domains, the caspase family domains p20 and p10, the caspase-8 active-site pentapeptide and potential aspartic acid cleavage sites. Aspartic Acid 203-216 caspase 8 Homo sapiens 41-50 24249517-0 2015 Osteopontin mediates tumorigenic transformation of a preneoplastic murine cell line by suppressing anoikis: an Arg-Gly-Asp-dependent-focal adhesion kinase-caspase-8 axis. Aspartic Acid 119-122 caspase 8 Homo sapiens 155-164 22037414-9 2011 A CYLD substitution mutation at Asp 215 that cannot be cleaved by caspase 8 switches cell survival to necrotic cell death in response to TNF. Aspartic Acid 32-35 caspase 8 Homo sapiens 66-75 25553350-2 2014 CASP8 D302H (rs1045485) (D, Aspartate; H, Histidine) and CASP8 -652 6N del (rs3834129) polymorphisms have been reported to be associated with Cancer susceptibility. Aspartic Acid 28-37 caspase 8 Homo sapiens 0-5 23754197-4 2013 We demonstrated that Asp induced cell death through the activation of TRAIL DR4/DR5 death receptors leading to the activation of caspase-8 and caspase-3 and to cell apoptosis. Aspartic Acid 21-24 caspase 8 Homo sapiens 129-138 20202478-7 2010 Several distinctive features of sea bass caspase-8 were identified, which include two death effector domains, the caspase family domains p20 and p10, the caspase-8 active-site pentapeptide and potential aspartic acid cleavage sites. Aspartic Acid 203-216 caspase 8 Homo sapiens 41-48 19665028-7 2009 By site-directed mutagenesis of bovSERPINA3-3, we identified Asp(371) as the potential P1 residue for caspases. Aspartic Acid 61-64 caspase 8 Homo sapiens 102-110 19706414-3 2009 In vitro cleavage assays demonstrate that OPN is cleaved at Asp-135 and Asp-157 by caspase-8. Aspartic Acid 60-63 caspase 8 Homo sapiens 83-92 19706414-3 2009 In vitro cleavage assays demonstrate that OPN is cleaved at Asp-135 and Asp-157 by caspase-8. Aspartic Acid 72-75 caspase 8 Homo sapiens 83-92 16741989-8 2006 In the type I H9 and SKW6.4 cells and type II Jurkat cells, the caspase-8 inhibitor Z-Ile-Glu(OMe)-Thr-Asp(OMe)-CH2F (IETD) prevented the cell killing. Aspartic Acid 103-106 caspase 8 Homo sapiens 64-73 19278658-1 2009 Caspases are proteases with an active-site cysteine and aspartate specificity in their substrates. Aspartic Acid 56-65 caspase 8 Homo sapiens 0-8 11790791-2 2002 The caspase-8 inhibitor benzyloxycarbonyl-Ile-Glu(OMe)-Thr-Asp(OMe)-CH(2)F (IETD) prevented the cleavage of Bid and the loss of viability. Aspartic Acid 59-62 caspase 8 Homo sapiens 4-13 15117953-4 2004 Bid is not transcriptionally up-regulated in response to these stimuli but is activated by cleavage on aspartate residues 60 and/or 75, which are the targets of caspase-8 and granzyme B. Aspartic Acid 103-112 caspase 8 Homo sapiens 161-170 15252032-6 2004 The late phase of TRAIL-induced NF-kappaB activation involves caspase mediated cleavage of IkappaBalpha between Asp(31) and Ser(32) residues to generate an N-terminal truncated fragment that is degraded by the proteasome via the N-end rule pathway. Aspartic Acid 112-115 caspase 8 Homo sapiens 62-69 11178964-2 2001 Caspases, the major effectors of apoptosis, are cysteine proteases that cleave crucial substrate proteins exclusively after aspartate residues. Aspartic Acid 124-133 caspase 8 Homo sapiens 0-8 11437602-4 2001 Amino-terminal sequence analysis of the caspase 3 polypeptides proved that caspase 8 had specifically cleaved the Asp(175)-Ser(176) bond to yield the expected p18 and p12 subunits, with partial cleavage at the Asp(28)-Ser(29) bond to release the prosegment. Aspartic Acid 114-117 caspase 8 Homo sapiens 75-84 11437602-4 2001 Amino-terminal sequence analysis of the caspase 3 polypeptides proved that caspase 8 had specifically cleaved the Asp(175)-Ser(176) bond to yield the expected p18 and p12 subunits, with partial cleavage at the Asp(28)-Ser(29) bond to release the prosegment. Aspartic Acid 210-213 caspase 8 Homo sapiens 75-84 11402050-2 2001 Upon caspase cleavage at Asp-87, the 10- and 25-kDa cleavage products of P35 remain tightly associated with the inhibited caspase. Aspartic Acid 25-28 caspase 8 Homo sapiens 5-12 11402050-2 2001 Upon caspase cleavage at Asp-87, the 10- and 25-kDa cleavage products of P35 remain tightly associated with the inhibited caspase. Aspartic Acid 25-28 caspase 8 Homo sapiens 122-129 9694885-3 1998 Both pathways involve the activation of a family of cysteine proteinases, the caspases, that cleave substrates at aspartic acid and are themselves activated by cleavage at internal aspartate residues. Aspartic Acid 114-127 caspase 8 Homo sapiens 78-86 10964557-2 2000 Caspases are cysteine proteases that are specific for substrates with an aspartic acid residue at the P(1) position and have an optimal recognition motif that incorporates four amino acid residues N-terminal to the cleavage site. Aspartic Acid 73-86 caspase 8 Homo sapiens 0-8 10964557-7 2000 In view of this finding, the original classification of caspases into three specificity groups needs to be modified, at least for caspase-8, which tolerates small hydrophobic residues as well as the acidic residue Asp in subsite S(4). Aspartic Acid 214-217 caspase 8 Homo sapiens 56-64 10964557-7 2000 In view of this finding, the original classification of caspases into three specificity groups needs to be modified, at least for caspase-8, which tolerates small hydrophobic residues as well as the acidic residue Asp in subsite S(4). Aspartic Acid 214-217 caspase 8 Homo sapiens 130-139 10891503-5 2000 Plectin was quantitatively cleaved by caspase 8 at Asp 2395 in the center of the molecule in all cells tested. Aspartic Acid 51-54 caspase 8 Homo sapiens 38-47 9694885-3 1998 Both pathways involve the activation of a family of cysteine proteinases, the caspases, that cleave substrates at aspartic acid and are themselves activated by cleavage at internal aspartate residues. Aspartic Acid 181-190 caspase 8 Homo sapiens 78-86