PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22670058-8 2012 Metabolic stabilization of at least one such fragment, Cys-RIPK1, greatly augmented the activation of the apoptosis-inducing effector caspase-3. Cysteine 55-58 caspase 3 Homo sapiens 134-143 20615463-7 2010 This was unlikely to be due to direct oxidation of the caspase 3 active-site cysteine and suggests alternative targeting of the caspase pathway. Cysteine 77-85 caspase 3 Homo sapiens 55-64 23156805-1 2012 OBJECTIVE: To explore the expression and significance of second mitochondria derived activator of caspase (Smac), X-linked inhibitor of apoptosis protein (XIAP)and cysteine containing aspartate specific protease 3 (caspase-3) in the growth, development and carcinogenesis of the nonnasal inverted papilloma (NIP). Cysteine 164-172 caspase 3 Homo sapiens 173-224 19610597-1 2009 To provide insight of their inhibition mechanism and facilitate the design of more potent ligands, a series of 59 isatin sulfonamide analogues were docked to the X-ray structure of caspase-3, one of the important cysteine aspartyl-specific execution proteases in apoptosis, and their binding conformations were analyzed by 3D-QSAR studies. Cysteine 213-221 caspase 3 Homo sapiens 181-190 19876066-5 2010 Suppression of intracellular ROS induction using various pharmacological inhibitors or PKCdelta- or NOX4-specific RNA interference enhanced the enzymatic activity of caspase-3 by blocking the oxidative modification of its catalytic cysteine residue, resulting in marked augmentation of TRAIL-mediated cell death. Cysteine 232-240 caspase 3 Homo sapiens 166-175 18544525-8 2008 Treatment of a two-disulfide form of Trx1 with S-nitrosoglutathione resulted in nitrosylation of Cys(73), which can act as a trans-nitrosylating agent as observed by others to control caspase 3 activity (Mitchell, D. A., and Marletta, M. A. Cysteine 97-100 caspase 3 Homo sapiens 184-193 18768468-6 2008 Crystal structures of caspase-3 in complexes with isoquinoline-1,3,4-trione derivatives show that the catalytic cysteine is oxidized to sulfonic acid (-SO(3)H) and isoquinoline-1,3,4-trione derivatives are bound at the dimer interface of caspase-3. Cysteine 112-120 caspase 3 Homo sapiens 22-31 18768468-6 2008 Crystal structures of caspase-3 in complexes with isoquinoline-1,3,4-trione derivatives show that the catalytic cysteine is oxidized to sulfonic acid (-SO(3)H) and isoquinoline-1,3,4-trione derivatives are bound at the dimer interface of caspase-3. Cysteine 112-120 caspase 3 Homo sapiens 238-247 17585855-3 2007 The inhibition mechanism was investigated through NMR studies of the reaction between 11d and benzylmercaptan as a model for Cys-285 in the active site of caspase-3. Cysteine 125-128 caspase 3 Homo sapiens 155-164 16140256-8 2005 Considering that those residues could be protected by caspase-3-specific inhibitor from the inactivation, the modifiers are histidine- and cysteine-specific, respectively, and the involvement of these residues in the characteristic catalytic dyad of caspases, the results indicate that the pKa values of the catalytic histidine and cysteine residues are changed during the activation process. Cysteine 139-147 caspase 3 Homo sapiens 54-63 17459324-2 2007 The inhibition of caspase 3 by singlet oxygen appears to involve the modification of a catalytic cysteine residue, since the reactivity of the sulfhydryl with alkylating agents decreased after singlet oxygen treatment. Cysteine 97-105 caspase 3 Homo sapiens 18-27 17185628-8 2007 Cysteine-to-serine mutations (C163S, C184S, and C220S) of caspase-3 that were predicted to prevent glutathiolation showed increased cleavage compared with wild-type caspase-3. Cysteine 0-8 caspase 3 Homo sapiens 58-67 17185628-8 2007 Cysteine-to-serine mutations (C163S, C184S, and C220S) of caspase-3 that were predicted to prevent glutathiolation showed increased cleavage compared with wild-type caspase-3. Cysteine 0-8 caspase 3 Homo sapiens 165-174 17168570-4 2006 This chemical tool is capable of permeating the mammalian cell membrane, selectively transnitrosating the caspase-3 active site cysteine, and halting apoptosis in cultured human T-cells. Cysteine 128-136 caspase 3 Homo sapiens 106-115 16866351-4 2006 Unlike the clan CA cysteine proteases, the catalytic histidine in caspase-3 plays a critical role during protonation and subsequent ring opening of the epoxide moiety and facilitates the nucleophilic attack by the active site cysteine. Cysteine 19-27 caspase 3 Homo sapiens 66-75 17141888-5 2007 The results of our studies indicate that the modulation of gammaGT activity can be used to change cellular redox status, and can affect Cys- and Cys-Gly-dependent S-thiolation and caspase-3 activity. Cysteine 136-139 caspase 3 Homo sapiens 180-189 17141888-5 2007 The results of our studies indicate that the modulation of gammaGT activity can be used to change cellular redox status, and can affect Cys- and Cys-Gly-dependent S-thiolation and caspase-3 activity. Cysteine 145-148 caspase 3 Homo sapiens 180-189 17141888-6 2007 We suggest that the role of high gammaGT activity in HepG2 cells can be connected with production of reactive oxygen species and with S-thiolation with Cys and Cys-Gly that can influence activity of caspase 3. Cysteine 152-155 caspase 3 Homo sapiens 199-208 16935258-4 2006 Peroxynitrite inhibits the catalytic activity of human caspase-3 by oxidizing the Sgamma atom of the Cys catalytic residue. Cysteine 101-104 caspase 3 Homo sapiens 55-64 16514683-7 2006 The utility of the Ardec orthogonal deprotection strategy for site-specific chemical modification of peptides bearing several amino groups was illustrated firstly by the preparation of a fluorogenic substrate for caspase-3 protease containing the cyanine dyes Cy 3.0 and Cy 5.0 as FRET donor/acceptor pair, and by solid-phase synthesis of an hexapeptide bearing a single biotin reporter group. Cysteine 260-262 caspase 3 Homo sapiens 213-222 16514683-7 2006 The utility of the Ardec orthogonal deprotection strategy for site-specific chemical modification of peptides bearing several amino groups was illustrated firstly by the preparation of a fluorogenic substrate for caspase-3 protease containing the cyanine dyes Cy 3.0 and Cy 5.0 as FRET donor/acceptor pair, and by solid-phase synthesis of an hexapeptide bearing a single biotin reporter group. Cysteine 271-273 caspase 3 Homo sapiens 213-222 16040627-5 2005 Inhibition of caspase-3 activation by either aldehyde occurred despite increases in mitochondrial cytochrome c release and occurred in close association with depletion of cellular GSH and with cysteine modifications within caspase-3. Cysteine 193-201 caspase 3 Homo sapiens 14-23 16140256-8 2005 Considering that those residues could be protected by caspase-3-specific inhibitor from the inactivation, the modifiers are histidine- and cysteine-specific, respectively, and the involvement of these residues in the characteristic catalytic dyad of caspases, the results indicate that the pKa values of the catalytic histidine and cysteine residues are changed during the activation process. Cysteine 332-340 caspase 3 Homo sapiens 54-63 10213689-2 1999 Caspase-3 zymogens were found to be S-nitrosylated on their catalytic-site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway. Cysteine 75-83 caspase 3 Homo sapiens 0-9 16408020-0 2005 Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Cysteine 69-77 caspase 3 Homo sapiens 47-56 16408020-8 2005 Previous in vivo work with Casp-3 suggests that a protein-assisted process may be responsible for selective S-nitrosation of the catalytic cysteine (Cys163). Cysteine 139-147 caspase 3 Homo sapiens 27-33 16408020-9 2005 We demonstrated that a single cysteine in thioredoxin (Trx) is capable of a targeted, reversible transnitrosation reaction with Cys163 of Casp-3. Cysteine 30-38 caspase 3 Homo sapiens 138-144 12490433-6 2003 l-cysteine, reduced glutathione (GSH), and herbimycin A, a protein tyrosine kinase inhibitor, suppressed the activation of caspase-3 and apoptosis of OPMN. Cysteine 0-10 caspase 3 Homo sapiens 123-132 21782579-3 2001 The putative active site of caspase 3 contains a cysteine residue that is subject to redox control. Cysteine 49-57 caspase 3 Homo sapiens 28-37 11230124-3 2001 We propose a multi-step process, whereby catalytically active processed or unprocessed caspase-9 initially binds the Apaf-1 apoptosome in cytochrome c/dATP-activated lysates and consequently recruits caspase-3 via an interaction between the active site cysteine (C287) in caspase-9 and a critical aspartate (D175) in caspase-3. Cysteine 253-261 caspase 3 Homo sapiens 200-209 15796904-3 2005 Caspase-3 cleavage of constructs with a caspase-3 sequence near the C-terminus in the sequence between the native fluorophore and the new cysteine, located C-terminal to the caspase site, destroyed the FRET, the emitted color reverting to that of unmodified GFP. Cysteine 138-146 caspase 3 Homo sapiens 0-9 15796904-3 2005 Caspase-3 cleavage of constructs with a caspase-3 sequence near the C-terminus in the sequence between the native fluorophore and the new cysteine, located C-terminal to the caspase site, destroyed the FRET, the emitted color reverting to that of unmodified GFP. Cysteine 138-146 caspase 3 Homo sapiens 40-49 15314233-4 2004 We screened a library of 10,000 thiol-containing compounds against accessible cysteines of two members of the caspase family of proteases, caspase-3 and -7. Cysteine 78-87 caspase 3 Homo sapiens 139-155 14705865-5 2003 Subsequently, the Apaf-1/caspase-9 holoenzyme complex recruits the effector caspase-3 via an interaction between the active site cysteine in caspase-9 and the critical aspartate, which is the cleavage site for generating the large and small subunits of caspase-3 that constitute the activated form of caspase-3. Cysteine 129-137 caspase 3 Homo sapiens 76-85 14705865-5 2003 Subsequently, the Apaf-1/caspase-9 holoenzyme complex recruits the effector caspase-3 via an interaction between the active site cysteine in caspase-9 and the critical aspartate, which is the cleavage site for generating the large and small subunits of caspase-3 that constitute the activated form of caspase-3. Cysteine 129-137 caspase 3 Homo sapiens 253-262 14705865-5 2003 Subsequently, the Apaf-1/caspase-9 holoenzyme complex recruits the effector caspase-3 via an interaction between the active site cysteine in caspase-9 and the critical aspartate, which is the cleavage site for generating the large and small subunits of caspase-3 that constitute the activated form of caspase-3. Cysteine 129-137 caspase 3 Homo sapiens 253-262 14630880-5 2003 Caspases (cysteine-dependent, aspartate-specific proteases) such as caspase-3 play an important role in mediating cell death in that many of the apoptotic signaling pathways, such as the mitochondrial-mediated, receptor-mediated, and sarcoplasmic-reticulum-mediated pathways, converge at caspase-3 in the caspase cascade. Cysteine 10-18 caspase 3 Homo sapiens 68-77 14630880-5 2003 Caspases (cysteine-dependent, aspartate-specific proteases) such as caspase-3 play an important role in mediating cell death in that many of the apoptotic signaling pathways, such as the mitochondrial-mediated, receptor-mediated, and sarcoplasmic-reticulum-mediated pathways, converge at caspase-3 in the caspase cascade. Cysteine 10-18 caspase 3 Homo sapiens 288-297 12563278-4 2003 We first designed a small-molecule "extender" that irreversibly alkylates the cysteine residue of caspase-3 and also contains a thiol group. Cysteine 78-86 caspase 3 Homo sapiens 98-107 11551979-2 2001 In resting cells, a subset of caspase-3 zymogens is S-nitrosylated at the active site cysteine, inhibiting enzyme activity. Cysteine 86-94 caspase 3 Homo sapiens 30-39 10409638-9 1999 Since this S-nitrosation was not observed in a mutant form of caspase-3 lacking the active site cysteine, we conclude that NO nitrosates the active site cysteine of caspase-3 and that this modification is notably inert to fast trans-nitrosation with glutathione. Cysteine 153-161 caspase 3 Homo sapiens 165-174 10205784-6 1999 The activation of caspases can be inhibited by several molecules, including peptide aldehydes (caspase-1 and or caspase-3 inhibitors) and crmA that target the active-site cysteine of caspase family members, Bcl-2, IAP (inhibitor of apoptosis protein) and NAIP (neuronal apoptosis inhibitory protein). Cysteine 171-179 caspase 3 Homo sapiens 112-121 10066732-4 1999 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine 24-32 caspase 3 Homo sapiens 52-61 10066732-4 1999 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine 24-32 caspase 3 Homo sapiens 137-146 10066732-4 1999 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine 41-44 caspase 3 Homo sapiens 52-61 10066732-4 1999 To demonstrate that the cysteine residue Cys-163 of caspase-3 is S-nitrosated, cells were transfected with the Myc-tagged p17 subunit of caspase-3. Cysteine 41-44 caspase 3 Homo sapiens 137-146 10066732-10 1999 Thus, NO supplied by exogenous NO donors serves in vivo as an antiapoptotic regulator of caspase activity via S-nitrosation of the Cys-163 residue of caspase-3. Cysteine 131-134 caspase 3 Homo sapiens 150-159 9034139-8 1997 Inhibition of CPP-32 enzyme activity was due to specific S-nitrosylation of Cys 163, a functionally essential amino acid conserved among ICE/CPP-32-like proteases. Cysteine 76-79 caspase 3 Homo sapiens 14-20 9441900-12 1997 The inhibition of caspase-3 activity correlated with a S-nitrosylation of the reactive cysteine residue and was reversed by further addition of dithiothreitol. Cysteine 87-95 caspase 3 Homo sapiens 18-27 9034139-8 1997 Inhibition of CPP-32 enzyme activity was due to specific S-nitrosylation of Cys 163, a functionally essential amino acid conserved among ICE/CPP-32-like proteases. Cysteine 76-79 caspase 3 Homo sapiens 141-147 32041780-5 2020 We attributed the caspase-3 inhibition to persulfidation of its catalytic cysteine. Cysteine 74-82 caspase 3 Homo sapiens 18-27 32334424-8 2020 This probe was able to cross the cell membrane freely and could be converted into a dimer through the condensation reaction of 2-cyano-6-aminobenzothiazole (CBT) and cysteine in response to intracellular activated caspase-3 and glutathione (GSH). Cysteine 166-174 caspase 3 Homo sapiens 214-223 31828913-4 2020 One of the scaffolds made of 2-pyrimidinecarbonitrile and cysteine joined by a benzyl linker was applied to design fluorescent probes to image caspase-3/7 and beta-galactosidase activity in live cells. Cysteine 58-66 caspase 3 Homo sapiens 143-154 29286134-7 2018 In addition, the mRNA and protein expression levels of connective tissue growth factor and cysteine-rich angiogenic factor 61 were notably decreased, the ratio of B-cell lymphoma 2 (Bcl-2)/Bcl-2-associated X protein (Bax) was significantly reduced, and the expression levels of caspase 3 were significantly decreased within YAP-silenced DU145 cells. Cysteine 91-99 caspase 3 Homo sapiens 278-287 29514461-7 2018 Apoptosis was measured by activity of several cysteine-dependent aspartate-specific protease (abbreviated as caspase) enzymes that initiate (caspases 8 and 9) or execute (caspases 3/7) apoptosis. Cysteine 46-54 caspase 3 Homo sapiens 171-183 22768390-4 2012 For fabrication of the peptide arrays, substrate peptides of cMMP-3, caspase-3, caspase-9, and calpain-1 were functionalized with TAMRA and cysteine, and were immobilized onto amine-functionalized arrays using a heterobifunctional linker, N-[gamma-maleimidobutyloxy]succinimide ester. Cysteine 140-148 caspase 3 Homo sapiens 69-78 26921254-3 2016 Supplementation withL-cys up-regulated occludin and claudin-1 expression, reduced caspase-3 activity and enhanced proliferating cell nuclear antigen expression of jejunum and ileum relative to LPS group. Cysteine 21-25 caspase 3 Homo sapiens 82-91 25915766-7 2015 Similar to cell proliferation, GSH, NAC and L-cysteine but not D-cysteine, completely restored the processing of caspase-8 and caspase-3 to their respective subunits in z-FA-FMK-treated activated T cells. Cysteine 44-54 caspase 3 Homo sapiens 127-136 25578648-0 2015 S-nitrosylation of XIAP at Cys 213 of BIR2 domain impairs XIAP"s anti-caspase 3 activity and anti-apoptotic function. Cysteine 27-30 caspase 3 Homo sapiens 70-79 25578648-6 2015 More importantly, we found that S-nitrosylation of XIAP Cys 213 impairs the anti-caspase 3 and anti-apoptotic function of XIAP that we observed in our previous study. Cysteine 56-59 caspase 3 Homo sapiens 81-90 22785533-8 2012 Mass spectrometry-based quantitative analysis for post-translational modifications using both (16)O/(18)O- and (14)N/(15)N-labeling strategies revealed that Photofrin-PDT triggered a significant oxidation of procaspase-3-D(3)A (mainly on Met-27, -39 and -44) in a Photofrin dose-dependent manner, whereas the active site Cys-163 remained largely unmodified. Cysteine 321-324 caspase 3 Homo sapiens 208-220