PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21179168-8 2010 Cysteine residues are critical for the maintenance of eNOS function; we therefore speculated that oxidative stress could alter eNOS activity through S-glutathionylation. Cysteine 0-8 nitric oxide synthase 3 Homo sapiens 54-58 21666221-7 2011 Mutagenesis of this key cysteine to alanine abolished eNOS thiyl radical formation and uncoupled eNOS, leading to increased superoxide generation. Cysteine 24-32 nitric oxide synthase 3 Homo sapiens 54-58 21666221-7 2011 Mutagenesis of this key cysteine to alanine abolished eNOS thiyl radical formation and uncoupled eNOS, leading to increased superoxide generation. Cysteine 24-32 nitric oxide synthase 3 Homo sapiens 97-101 21666221-8 2011 Protein thiyl radical formation leads to oxidation or modification of cysteine with either disulfide bond formation or S-glutathionylation, which induces eNOS uncoupling. Cysteine 70-78 nitric oxide synthase 3 Homo sapiens 154-158 33934624-8 2021 Overexpression of FXYD1 in HEK293 cells revealed a possible mechanism, where FXYD1 protected against redox modification of eNOS cysteines. Cysteine 128-137 nitric oxide synthase 3 Homo sapiens 123-127 21179168-8 2010 Cysteine residues are critical for the maintenance of eNOS function; we therefore speculated that oxidative stress could alter eNOS activity through S-glutathionylation. Cysteine 0-8 nitric oxide synthase 3 Homo sapiens 127-131 21179168-9 2010 Here we show that S-glutathionylation of eNOS reversibly decreases NOS activity with an increase in O(2)( -) generation primarily from the reductase, in which two highly conserved cysteine residues are identified as sites of S-glutathionylation and found to be critical for redox-regulation of eNOS function. Cysteine 180-188 nitric oxide synthase 3 Homo sapiens 41-45 21179168-9 2010 Here we show that S-glutathionylation of eNOS reversibly decreases NOS activity with an increase in O(2)( -) generation primarily from the reductase, in which two highly conserved cysteine residues are identified as sites of S-glutathionylation and found to be critical for redox-regulation of eNOS function. Cysteine 180-188 nitric oxide synthase 3 Homo sapiens 294-298 17941803-8 2008 All these cysteine residues identified were found to be located on the surface of the protein according to the available X-ray structure of the oxygenase domain of eNOS. Cysteine 10-18 nitric oxide synthase 3 Homo sapiens 164-168 18641128-7 2008 We further show that activation of N-Ras involves eNOS-dependent S-nitrosylation on Cys(118), suggesting that upon TCR engagement, eNOS-derived NO directly activates N-Ras on the Golgi. Cysteine 84-87 nitric oxide synthase 3 Homo sapiens 50-54 18641128-7 2008 We further show that activation of N-Ras involves eNOS-dependent S-nitrosylation on Cys(118), suggesting that upon TCR engagement, eNOS-derived NO directly activates N-Ras on the Golgi. Cysteine 84-87 nitric oxide synthase 3 Homo sapiens 131-135 17941803-0 2008 Identification of the cysteine nitrosylation sites in human endothelial nitric oxide synthase. Cysteine 22-30 nitric oxide synthase 3 Homo sapiens 60-93 17941803-2 2008 In our previous work we have shown that S-nitrosylation is involved in the disruption of the endothelial nitric oxide synthase (eNOS) dimer and that this involves the disruption of the zinc (Zn) tetrathiolate cluster due to the S-nitrosylation of Cysteine 98. Cysteine 247-255 nitric oxide synthase 3 Homo sapiens 93-126 17941803-2 2008 In our previous work we have shown that S-nitrosylation is involved in the disruption of the endothelial nitric oxide synthase (eNOS) dimer and that this involves the disruption of the zinc (Zn) tetrathiolate cluster due to the S-nitrosylation of Cysteine 98. Cysteine 247-255 nitric oxide synthase 3 Homo sapiens 128-132 17941803-3 2008 However, human eNOS contains 28 other cysteine residues whose potential to undergo S-nitrosylation has not been determined. Cysteine 38-46 nitric oxide synthase 3 Homo sapiens 15-19 17941803-4 2008 Thus, the goal of this study was to identify the cysteine residues within eNOS that are susceptible to S-nitrosylation in vitro. Cysteine 49-57 nitric oxide synthase 3 Homo sapiens 74-78 17941803-9 2008 Among those identified were Cys 93 and 98, the residues involved in the formation of the eNOS dimer through a Zn tetrathiolate cluster. Cysteine 28-31 nitric oxide synthase 3 Homo sapiens 89-93 17941803-14 2008 These cysteines are located in regions of eNOS that have not been implicated in any known biochemical functions and the significance of their S-nitrosylation is not clear from this study. Cysteine 6-15 nitric oxide synthase 3 Homo sapiens 42-46 10409685-4 1999 In the zinc-bound state, these same two cysteine residues form part of a zinc-tetrathiolate (ZnS(4)) center indistinguishable from that observed in the endothelial isoform (NOS-3). Cysteine 40-48 nitric oxide synthase 3 Homo sapiens 173-178 15937123-3 2005 In this work, we show by a variety of methods (ozone chemiluminescence, biotin switch, and mass spectrometry) that the molecular chaperone Hsp90 is a target of S-nitrosylation and identify a susceptible cysteine residue in the region of the C-terminal domain that interacts with endothelial nitric oxide synthase (eNOS). Cysteine 203-211 nitric oxide synthase 3 Homo sapiens 279-312 7523378-0 1994 Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity. Cysteine 0-8 nitric oxide synthase 3 Homo sapiens 16-49 8873592-1 1996 Endothelial nitric oxide synthase (eNOS) is dually acylated by N-myristoylation and cysteine palmitoylation and resides in Golgi and caveolae membranes. Cysteine 84-92 nitric oxide synthase 3 Homo sapiens 0-33 8873592-1 1996 Endothelial nitric oxide synthase (eNOS) is dually acylated by N-myristoylation and cysteine palmitoylation and resides in Golgi and caveolae membranes. Cysteine 84-92 nitric oxide synthase 3 Homo sapiens 35-39 9852077-1 1998 Eight polar amino acid residues in the putative substrate-binding region from Thr-360 to Val-379 in human endothelial nitric-oxide synthase (eNOS) (Thr-360, Arg-365, Cys-368, Asp-369, Arg-372, Tyr-373, Glu-377, and Asp-378) were individually mutated. Cysteine 166-169 nitric oxide synthase 3 Homo sapiens 106-139 8806629-1 1996 We examined whether highly conserved cysteine residues in the reductase domain of the constitutive isoform of nitric oxide synthase in human endothelial cells (ecNOS) are crucial for catalytic activity of the enzyme. Cysteine 37-45 nitric oxide synthase 3 Homo sapiens 160-165 8806629-3 1996 The specific activity of ecNOS was > 7-fold increased in wild-type and in mutants Cys-976 and Cys-991, but not in mutants Cys-1048 and Cys-1114. Cysteine 85-88 nitric oxide synthase 3 Homo sapiens 25-30 8806629-3 1996 The specific activity of ecNOS was > 7-fold increased in wild-type and in mutants Cys-976 and Cys-991, but not in mutants Cys-1048 and Cys-1114. Cysteine 97-100 nitric oxide synthase 3 Homo sapiens 25-30 8806629-3 1996 The specific activity of ecNOS was > 7-fold increased in wild-type and in mutants Cys-976 and Cys-991, but not in mutants Cys-1048 and Cys-1114. Cysteine 97-100 nitric oxide synthase 3 Homo sapiens 25-30 8806629-3 1996 The specific activity of ecNOS was > 7-fold increased in wild-type and in mutants Cys-976 and Cys-991, but not in mutants Cys-1048 and Cys-1114. Cysteine 97-100 nitric oxide synthase 3 Homo sapiens 25-30 8806629-7 1996 These results indicate that Cys-1048 and Cys-1114 residues in the NADPH binding site of the reductase domain are critical for human ecNOS activity. Cysteine 28-31 nitric oxide synthase 3 Homo sapiens 132-137 8806629-7 1996 These results indicate that Cys-1048 and Cys-1114 residues in the NADPH binding site of the reductase domain are critical for human ecNOS activity. Cysteine 41-44 nitric oxide synthase 3 Homo sapiens 132-137 8806629-8 1996 The lack of utilization of NADPH in L-arginine metabolism and in cytochrome c reduction suggests that these active site cysteine residues may be responsible for binding of NADPH and/or for electron transfer in human ecNOS. Cysteine 120-128 nitric oxide synthase 3 Homo sapiens 216-221 8524847-7 1995 Immunoprecipitation of ecNOS mutants following cDNA transfection and biosynthetic labeling with [3H]palmitate revealed that mutagenesis of either cysteine residue attenuated palmitoylation, whereas replacement of both residues completely eliminated palmitoylation. Cysteine 146-154 nitric oxide synthase 3 Homo sapiens 23-28 8524847-8 1995 Analysis of N-terminal deletion mutations of ecNOS demonstrated that the region containing these two cysteine residues is both necessary and sufficient for enzyme palmitoylation. Cysteine 101-109 nitric oxide synthase 3 Homo sapiens 45-50 8524847-9 1995 The cysteines thus identified as the palmitoylation sites for ecNOS are separated by an unusual (Gly-Leu)5 sequence and appear to define a sequence motif for dual acylation. Cysteine 4-13 nitric oxide synthase 3 Homo sapiens 62-67 7488039-0 1995 Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity. Cysteine 0-8 nitric oxide synthase 3 Homo sapiens 15-48 7488039-0 1995 Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity. Cysteine 0-8 nitric oxide synthase 3 Homo sapiens 50-57 7488039-3 1995 Here, we demonstrated that cys-99 of human endothelial NOS (ecNOS) is critical for BH4 involvement in NOS catalytic activity and stability. Cysteine 27-30 nitric oxide synthase 3 Homo sapiens 43-58 7488039-3 1995 Here, we demonstrated that cys-99 of human endothelial NOS (ecNOS) is critical for BH4 involvement in NOS catalytic activity and stability. Cysteine 27-30 nitric oxide synthase 3 Homo sapiens 60-65 7488039-4 1995 Mutation of cys-99 to alanine in ecNOS resulted in loss of catalytic activity which could be restored to the level of wild type by adding a high concentration of exogenous BH4 to the crude extract. Cysteine 12-15 nitric oxide synthase 3 Homo sapiens 33-38 7523378-3 1994 To locate this specific cysteine, we altered three potential cysteine residues (Cys-99, Cys-184, and Cys-441) to alanine residues in human endothelial nitric oxide synthase (eNOS) by oligonucleotide-directed mutagenesis and expressed the wild-type and mutant eNOSs in COS-1 and the baculovirus expression system. Cysteine 24-32 nitric oxide synthase 3 Homo sapiens 139-172 7523378-3 1994 To locate this specific cysteine, we altered three potential cysteine residues (Cys-99, Cys-184, and Cys-441) to alanine residues in human endothelial nitric oxide synthase (eNOS) by oligonucleotide-directed mutagenesis and expressed the wild-type and mutant eNOSs in COS-1 and the baculovirus expression system. Cysteine 24-32 nitric oxide synthase 3 Homo sapiens 174-178 7523378-3 1994 To locate this specific cysteine, we altered three potential cysteine residues (Cys-99, Cys-184, and Cys-441) to alanine residues in human endothelial nitric oxide synthase (eNOS) by oligonucleotide-directed mutagenesis and expressed the wild-type and mutant eNOSs in COS-1 and the baculovirus expression system. Cysteine 61-69 nitric oxide synthase 3 Homo sapiens 139-172 7523378-3 1994 To locate this specific cysteine, we altered three potential cysteine residues (Cys-99, Cys-184, and Cys-441) to alanine residues in human endothelial nitric oxide synthase (eNOS) by oligonucleotide-directed mutagenesis and expressed the wild-type and mutant eNOSs in COS-1 and the baculovirus expression system. Cysteine 80-83 nitric oxide synthase 3 Homo sapiens 139-172 7523378-3 1994 To locate this specific cysteine, we altered three potential cysteine residues (Cys-99, Cys-184, and Cys-441) to alanine residues in human endothelial nitric oxide synthase (eNOS) by oligonucleotide-directed mutagenesis and expressed the wild-type and mutant eNOSs in COS-1 and the baculovirus expression system. Cysteine 88-91 nitric oxide synthase 3 Homo sapiens 139-172 7523378-5 1994 Mutation of Cys-184 resulted in a complete loss of NOS catalytic activity and abrogation of the formation of carbon monoxide (CO)-heme ferrous complex, which was detected on CO difference spectra as a distinct peak centered on 444-446 nm, without reduction in the quantity of eNOS protein. Cysteine 12-15 nitric oxide synthase 3 Homo sapiens 276-280 7523378-8 1994 These results indicate that the cysteine 184 of human eNOS is most likely the proximal heme ligand. Cysteine 32-40 nitric oxide synthase 3 Homo sapiens 54-58