PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 107-110 tumor protein p53 Homo sapiens 15-18 33357454-3 2021 Here we report the identification of small molecules, including arsenic trioxide (ATO), an established agent in treating acute promyelocytic leukemia, as cysteine-reactive compounds that rescue structural p53 mutations. Cysteine 154-162 tumor protein p53 Homo sapiens 205-208 33357454-4 2021 Crystal structures of arsenic-bound p53 mutants reveal a cryptic allosteric site involving three arsenic-coordinating cysteines within the DNA-binding domain, distal to the zinc-binding site. Cysteine 118-127 tumor protein p53 Homo sapiens 36-39 33372419-0 2021 Association of hOGG1-Cys variants with occurrence of p53 and EGFR deletion mutations in non-small cell lung cancer. Cysteine 21-24 tumor protein p53 Homo sapiens 53-56 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 101-104 tumor protein p53 Homo sapiens 15-18 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 107-110 tumor protein p53 Homo sapiens 15-18 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 107-110 tumor protein p53 Homo sapiens 15-18 33372419-12 2021 KEY POINTS: SIGNIFICANT FINDINGS OF THE STUDY: NSCLC patients with hOGG1-Cys variants may have a higher risk of p53 and EGFR deletion mutations than with hOGG1 Ser/Ser genotype. Cysteine 73-76 tumor protein p53 Homo sapiens 112-115 27479485-4 2016 The modified DNA efficiently cross-linked with p53 protein through alkylation of cysteine and showed potential for cross-linking with histidine (in C277H mutant of p53). Cysteine 81-89 tumor protein p53 Homo sapiens 47-50 32801360-5 2020 Then, autophagy improves intracellular H2O2 via promoting p53-mediated depletion of GSH and cysteine and downregulation of xCT. Cysteine 92-100 tumor protein p53 Homo sapiens 58-61 31601779-0 2019 Correction: APR-246 reactivates mutant p53 by targeting cysteines 124 and 277. Cysteine 56-65 tumor protein p53 Homo sapiens 39-42 30892598-6 2019 The DNA-binding core domain of p53 has 10 cysteine residues, three of which participate in holding a zinc atom that is critical for p53 structure and function. Cysteine 42-50 tumor protein p53 Homo sapiens 31-34 30892598-6 2019 The DNA-binding core domain of p53 has 10 cysteine residues, three of which participate in holding a zinc atom that is critical for p53 structure and function. Cysteine 42-50 tumor protein p53 Homo sapiens 132-135 30892598-7 2019 Several novel compounds that refold and reactivate missense mutant p53 bind to specific p53 cysteine residues. Cysteine 92-100 tumor protein p53 Homo sapiens 67-70 30892598-7 2019 Several novel compounds that refold and reactivate missense mutant p53 bind to specific p53 cysteine residues. Cysteine 92-100 tumor protein p53 Homo sapiens 88-91 29670092-0 2018 APR-246 reactivates mutant p53 by targeting cysteines 124 and 277. Cysteine 44-53 tumor protein p53 Homo sapiens 27-30 29670092-6 2018 We identified cysteine 277 as a prime binding target for MQ in p53. Cysteine 14-22 tumor protein p53 Homo sapiens 63-66 33111621-7 2022 Cmpd-4 and Cmpd-8 demonstrated binding with mutated p53 at cysteine 124, similar to the mutant p53 reactivating compound APR-246 (PRIMA-1Met) for functional restoration of the mutant p53. Cysteine 59-67 tumor protein p53 Homo sapiens 52-55 31945496-11 2020 Interestingly, mutation of redox sensitive cysteine residues at 124, 141 and 182 position in p53 significantly reduces mal C plus NAC mediated sensitization of cancer cells. Cysteine 43-51 tumor protein p53 Homo sapiens 93-96 30728290-6 2019 We show by coimmunoprecipitation and mass spectrometry that the redox-regulated pyruvate kinase muscle 2 (PKM2) directly binds with p53 and that the redox status of cysteine-423 of tetrameric (but not monomeric) PKM2 is critical for the differential regulation of p53 transcriptional activity. Cysteine 165-173 tumor protein p53 Homo sapiens 132-135 30728290-6 2019 We show by coimmunoprecipitation and mass spectrometry that the redox-regulated pyruvate kinase muscle 2 (PKM2) directly binds with p53 and that the redox status of cysteine-423 of tetrameric (but not monomeric) PKM2 is critical for the differential regulation of p53 transcriptional activity. Cysteine 165-173 tumor protein p53 Homo sapiens 264-267 26870698-7 2016 One of these molecules, APR-246, is a prodrug that is converted to the Michael acceptor methylene quinuclidinone (MQ) that binds covalently to cysteines in p53, leading to refolding and restoration of wild type p53 function. Cysteine 143-152 tumor protein p53 Homo sapiens 156-159 27551077-5 2016 PK11007 stabilized p53 in vitro via selective alkylation of two surface-exposed cysteines without compromising its DNA binding activity. Cysteine 80-89 tumor protein p53 Homo sapiens 19-22 26870698-7 2016 One of these molecules, APR-246, is a prodrug that is converted to the Michael acceptor methylene quinuclidinone (MQ) that binds covalently to cysteines in p53, leading to refolding and restoration of wild type p53 function. Cysteine 143-152 tumor protein p53 Homo sapiens 211-214 23038158-0 2012 The APE1 Asp/Asp genotype and the combination of APE1 Asp/Asp and hOGG1-Cys variants are associated with increased p53 mutation in non-small cell lung cancer. Cysteine 72-75 tumor protein p53 Homo sapiens 115-118 26086967-4 2015 APR-246 is a prodrug that is converted to the active compound methylene quinuclidinone (MQ), a Michael acceptor that binds to cysteine residues in mutant p53 and restores its wild-type conformation. Cysteine 126-134 tumor protein p53 Homo sapiens 154-157 26086967-7 2015 We propose that this unique ability of APR-246/MQ to bind to cysteines in both mutant p53 and glutathione has a key role in the resensitization as well as in the outstanding synergistic effects observed with APR-246 in combination with platinum compounds in ovarian cancer cell lines and primary cancer cells. Cysteine 61-70 tumor protein p53 Homo sapiens 86-89 25584637-6 2015 Differential thiol labeling was used to determine the oxidation states of cysteine residues within p53 after DNA-mediated oxidation. Cysteine 74-82 tumor protein p53 Homo sapiens 99-102 25584637-9 2015 A distinct shift in peptide labeling toward (13)C2D2-iodoacetamide-labeled cysteines is observed in oxidized samples, confirming that chemical oxidation of p53 occurs at long range. Cysteine 75-84 tumor protein p53 Homo sapiens 156-159 25025378-8 2014 Moreover, combined positive expression of p53 and pAkt led to significantly increased PFS in subgroups carrying the XRCC1 Gln allele (HR 7.057; 95% CI 2.073-24.021; P = 0.002) or the ERCC1 Cys allele (HR 2.568; 95% CI 1.056-6.248; P = 0.038). Cysteine 189-192 tumor protein p53 Homo sapiens 42-45 24446736-0 2014 Induction of lung cancer cell apoptosis through a p53 pathway by [6]-shogaol and its cysteine-conjugated metabolite M2. Cysteine 85-93 tumor protein p53 Homo sapiens 50-53 23863845-1 2013 A p53 hot-spot mutation found frequently in human cancer is the replacement of R273 by histidine or cysteine residues resulting in p53 loss of function as a tumor suppressor. Cysteine 100-108 tumor protein p53 Homo sapiens 2-5 23863845-1 2013 A p53 hot-spot mutation found frequently in human cancer is the replacement of R273 by histidine or cysteine residues resulting in p53 loss of function as a tumor suppressor. Cysteine 100-108 tumor protein p53 Homo sapiens 131-134 23038158-11 2012 CONCLUSIONS: These results suggest that the APE1 Asp/Asp genotype and the combination of the APE1 Asp/Asp and hOGG1-Cys variants are associated with increased risk of p53 mutation in non-small cell lung cancer. Cysteine 116-119 tumor protein p53 Homo sapiens 167-170 23501101-1 2013 Cysteine oxidation and covalent modification of redox sensitive transcription factors including p53 are known, among others, as important events in cell response to oxidative stress. Cysteine 0-8 tumor protein p53 Homo sapiens 96-99 23038158-10 2012 The risk of p53 mutation was also higher in participants with APE1 Asp/Asp plus hOGG1-Cys than in those with APE1-Glu plus hOGG1 Ser/Ser (OR, 3.72; 95% CI, 1.33-10.40; P = 0.012). Cysteine 86-89 tumor protein p53 Homo sapiens 12-15 20878668-0 2010 Stabilization of mutant p53 via alkylation of cysteines and effects on DNA binding. Cysteine 46-55 tumor protein p53 Homo sapiens 24-27 21472523-0 2011 Identification of two reactive cysteine residues in the tumor suppressor protein p53 using top-down FTICR mass spectrometry. Cysteine 31-39 tumor protein p53 Homo sapiens 81-84 21472523-2 2011 The discovery of cysteine-targeting compounds that cause re-activation of mutant p53 and the death of tumor cells in vivo has emphasized the functional importance of p53 thiols. Cysteine 17-25 tumor protein p53 Homo sapiens 81-84 21472523-2 2011 The discovery of cysteine-targeting compounds that cause re-activation of mutant p53 and the death of tumor cells in vivo has emphasized the functional importance of p53 thiols. Cysteine 17-25 tumor protein p53 Homo sapiens 166-169 21472523-3 2011 Using a combination of top-down and middle-down FTICR mass spectrometry, we show that of the 10 Cys residues in the core domain of wild-type p53, Cys182 and Cys277 exhibit a remarkable preference for modification by the alkylating reagent N-ethylmaleimide. Cysteine 96-99 tumor protein p53 Homo sapiens 141-144 21472523-5 2011 Further alkylation of p53 beyond Cys182 and Cys277 was found to trigger co-operative modification of the remaining seven Cys residues and protein unfolding. Cysteine 33-36 tumor protein p53 Homo sapiens 22-25 21465572-2 2011 In response to oxidative, nitrosative, and electrophilic insults, p53 undergoes post-translational modifications, such as oxidation and covalent modification of cysteines, nitration of tyrosines, acetylation of lysines, phosphorylation of serine/threonine residues, etc. Cysteine 161-170 tumor protein p53 Homo sapiens 66-69 20878668-3 2010 We have discovered ligands containing an alpha,beta-unsaturated double bond, characteristic of Michael acceptors, that bind covalently to generic cysteine sites in the p53 core domain. Cysteine 146-154 tumor protein p53 Homo sapiens 168-171 19101993-3 2009 Genetic analysis showed a germline TP53 mutation in codon 220 exon 6, which changed TAT --> TGT and resulted in a tyrosine-to-cysteine amino acid substitution (Tyr220Cys). Cysteine 126-134 tumor protein p53 Homo sapiens 35-39 20233844-4 2010 Using this approach, we quantified the site-specific cysteine oxidation status of endogenous p53 for the first time and found that Cys182 at the dimerization interface of the DNA binding domain is particularly susceptible to diamide oxidation intracellularly. Cysteine 53-61 tumor protein p53 Homo sapiens 93-96 20600834-0 2010 Cys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines. Cysteine 0-3 tumor protein p53 Homo sapiens 35-38 20600834-1 2010 Previously, we reported that human p53 is functionally inactivated by S-glutathionylation at Cys-141 during oxidative and DNA-damaging treatments. Cysteine 93-96 tumor protein p53 Homo sapiens 35-38 20459757-5 2010 Oxygen tension also affects many mammalian transactivators including AP-1, NFkB, and p53 by affecting the reduced state of critical cysteines in these proteins. Cysteine 132-141 tumor protein p53 Homo sapiens 85-88 20208557-0 2010 15-Deoxy-Delta(12,14)-prostaglandin J(2) stabilizes, but functionally inactivates p53 by binding to the cysteine 277 residue. Cysteine 104-112 tumor protein p53 Homo sapiens 82-85 20208557-6 2010 Moreover, by conducting an in vitro [(35)S]-labeled p53 translation assay, we identified cysteine 277 as a putative site of p53 modification by 15d-PGJ(2). Cysteine 89-97 tumor protein p53 Homo sapiens 52-55 20208557-6 2010 Moreover, by conducting an in vitro [(35)S]-labeled p53 translation assay, we identified cysteine 277 as a putative site of p53 modification by 15d-PGJ(2). Cysteine 89-97 tumor protein p53 Homo sapiens 124-127 20208557-10 2010 In conclusion, 15d-PGJ(2) can undergo nucleophilic addition to p53, presumably at the cysteine 277 residue, rendering this tumor suppressor less susceptible to proteasomal degradation. Cysteine 86-94 tumor protein p53 Homo sapiens 63-66 19681600-0 2009 Effect of thioredoxin deletion and p53 cysteine replacement on human p53 activity in wild-type and thioredoxin reductase null yeast. Cysteine 39-47 tumor protein p53 Homo sapiens 69-72 19681600-7 2009 Substitutions at Zn-coordinating cysteines C176, C238, or C242 resulted in p53 inactivation. Cysteine 33-42 tumor protein p53 Homo sapiens 75-78 19681600-8 2009 Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. Cysteine 30-38 tumor protein p53 Homo sapiens 61-64 19681600-8 2009 Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. Cysteine 30-38 tumor protein p53 Homo sapiens 152-155 19681600-8 2009 Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. Cysteine 123-131 tumor protein p53 Homo sapiens 61-64 19681600-8 2009 Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. Cysteine 123-131 tumor protein p53 Homo sapiens 152-155 19681600-9 2009 Cysteine substitutions at six positions (C124, C135, C141, C182, C229, and C277) neither inactivated p53 nor relieved the requirement for thioredoxin reductase. Cysteine 0-8 tumor protein p53 Homo sapiens 101-104 19681600-11 2009 The results suggested that p53 dependence on thioredoxin reductase either was indirect, perhaps mediated by an upstream activator of p53, or was due to oxidation of one or more of the four essential cysteines. Cysteine 199-208 tumor protein p53 Homo sapiens 27-30 18586825-2 2008 APE1/Ref-1 has redox activity and AP endonuclease activity, and is able to enhance DNA-binding activity of several transcription factors, including NF-kappaB, AP-1 and p53, through reduction of their critical cysteine residues. Cysteine 209-217 tumor protein p53 Homo sapiens 168-171 17916563-4 2007 The use of NM23-H1 and STRAP mutants revealed that Cys(145) of NM23-H1 and Cys(152) (or Cys(270)) of STRAP were responsible for p53 binding. Cysteine 51-54 tumor protein p53 Homo sapiens 128-131 18502749-0 2008 Critical role of cysteine residue 81 of macrophage migration inhibitory factor (MIF) in MIF-induced inhibition of p53 activity. Cysteine 17-25 tumor protein p53 Homo sapiens 114-117 18502749-3 2008 This association was significantly reduced by a C81S mutation but not C57S or C60S mutations, suggesting that Cys(81) is essential for the in vivo association between MIF and p53. Cysteine 110-113 tumor protein p53 Homo sapiens 175-178 18502749-4 2008 This association also depended on Cys(242) (and, to some extent, on Cys(238)) within the central DNA binding domain of p53. Cysteine 34-37 tumor protein p53 Homo sapiens 119-122 18502749-4 2008 This association also depended on Cys(242) (and, to some extent, on Cys(238)) within the central DNA binding domain of p53. Cysteine 68-71 tumor protein p53 Homo sapiens 119-122 18179182-5 2008 The cysteine residues on the exterior of the p53 molecule were derivatized for the attachment of gold nanoparticle/streptavidin conjugates capped with multiple ferrocene (Fc) groups. Cysteine 4-12 tumor protein p53 Homo sapiens 45-48 17916563-4 2007 The use of NM23-H1 and STRAP mutants revealed that Cys(145) of NM23-H1 and Cys(152) (or Cys(270)) of STRAP were responsible for p53 binding. Cysteine 75-78 tumor protein p53 Homo sapiens 128-131 17916563-4 2007 The use of NM23-H1 and STRAP mutants revealed that Cys(145) of NM23-H1 and Cys(152) (or Cys(270)) of STRAP were responsible for p53 binding. Cysteine 75-78 tumor protein p53 Homo sapiens 128-131 17916563-5 2007 Furthermore, Cys(176) and Cys(135) of p53 were required to bind NM23-H1 and STRAP, respectively. Cysteine 13-16 tumor protein p53 Homo sapiens 38-41 17916563-5 2007 Furthermore, Cys(176) and Cys(135) of p53 were required to bind NM23-H1 and STRAP, respectively. Cysteine 26-29 tumor protein p53 Homo sapiens 38-41 17555331-0 2007 Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress. Cysteine 47-56 tumor protein p53 Homo sapiens 6-9 17070096-7 2007 Mutational analysis of p53 gene revealed an A-->G transition at the second base of codon 220, resulting in amino acid substitution from tyrosine to cysteine in the protein. Cysteine 151-159 tumor protein p53 Homo sapiens 23-26 17555331-8 2007 Mass spectrometry of GSH-modified p53 protein identified cysteines 124, 141, and 182, all present in the proximal DNA-binding domain, as the sites of glutathionylation. Cysteine 57-66 tumor protein p53 Homo sapiens 34-37 17555331-9 2007 Biotinylated maleimide also reacted rapidly with Cys141, implying that this is the most reactive cysteine on the p53 surface. Cysteine 97-105 tumor protein p53 Homo sapiens 113-116 17555331-10 2007 The glutathionylatable cysteines were found to exist in a negatively charged microenvironment in cellular p53. Cysteine 23-32 tumor protein p53 Homo sapiens 106-109 17555331-12 2007 These results show for the first time that shielding of reactive cysteines contributes to a negative regulation for human p53 and imply that such an inactivation of the transcription factor may represent an acute defensive response with significant consequences for oncogenesis. Cysteine 65-74 tumor protein p53 Homo sapiens 122-125 17575104-6 2007 Furthermore, the antibody-mediated p53 response was dramatically increased when a peptide corresponding to the 4C6 epitope and bearing a COOH-terminal cysteine residue was added to the transduction mixture. Cysteine 151-159 tumor protein p53 Homo sapiens 35-38 15888975-8 2005 This mutation causes an amino-acid replacement (Tyr to Cys), which was previously proven to attenuate p53 function. Cysteine 55-58 tumor protein p53 Homo sapiens 102-105 16300733-5 2006 Oxidation of cysteine residues within the CD of posttranslationally unmodified full length p53 did not affect its ability to recognize cisPt-DNA. Cysteine 13-21 tumor protein p53 Homo sapiens 91-94 15551330-9 2005 p53 mutations were significantly (p = 0.04) less common in NSCLC from patients with codon 326 Ser/Cys or Cys/Cys genotypes (21 of 51; 41%) than in NSCLC from Ser/Ser homozygotes (53 of 90; 59%). Cysteine 98-101 tumor protein p53 Homo sapiens 0-3 15551330-9 2005 p53 mutations were significantly (p = 0.04) less common in NSCLC from patients with codon 326 Ser/Cys or Cys/Cys genotypes (21 of 51; 41%) than in NSCLC from Ser/Ser homozygotes (53 of 90; 59%). Cysteine 105-108 tumor protein p53 Homo sapiens 0-3 15551330-9 2005 p53 mutations were significantly (p = 0.04) less common in NSCLC from patients with codon 326 Ser/Cys or Cys/Cys genotypes (21 of 51; 41%) than in NSCLC from Ser/Ser homozygotes (53 of 90; 59%). Cysteine 105-108 tumor protein p53 Homo sapiens 0-3 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 61-64 tumor protein p53 Homo sapiens 16-19 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 137-140 tumor protein p53 Homo sapiens 16-19 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 137-140 tumor protein p53 Homo sapiens 16-19 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 137-140 tumor protein p53 Homo sapiens 16-19 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 137-140 tumor protein p53 Homo sapiens 16-19 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 137-140 tumor protein p53 Homo sapiens 16-19 15551330-10 2005 The decrease in p53 mutation frequency among carriers of the Cys allele was more evident in lung squamous cell cancer [7 of 17 (41%) for Cys/Cys and Ser/Cys vs. 27 of 38 (71%) for Ser/Ser; p = 0.04] than in nonbronchoalveolar adenocarcinoma [11 of 26 (42%) for Cys/Cys and Ser/Cys vs. 20 of 35 (57%) for Ser/Ser; p = 0.25]. Cysteine 137-140 tumor protein p53 Homo sapiens 16-19 15551330-12 2005 In summary, the hOGG1 codon 326 Cys allele was associated with a decrease in p53 mutations and no effect on G:C-to-T:A transversions in NSCLC. Cysteine 32-35 tumor protein p53 Homo sapiens 77-80 15105503-2 2004 We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing Cys-SO(2)H, thus reestablishing the antioxidant firewall. Cysteine 131-134 tumor protein p53 Homo sapiens 77-80 15274301-3 2004 The main dietary form is selenomethionine, which we showed modulated p53 activity by causing redox regulation of key p53 cysteine residues. Cysteine 121-129 tumor protein p53 Homo sapiens 69-72 15274301-3 2004 The main dietary form is selenomethionine, which we showed modulated p53 activity by causing redox regulation of key p53 cysteine residues. Cysteine 121-129 tumor protein p53 Homo sapiens 117-120 15154850-3 2004 Direct protein-protein interaction between a central domain of MDM2 and the TAZ1 (transcriptional adaptor zinc-binding domain) [C/H1 (cysteine/histidine-rich region 1)] domain of p300 and subsequent formation of a ternary complex including p53 have been reported previously. Cysteine 134-142 tumor protein p53 Homo sapiens 240-243 14580323-2 2003 The goal of the current research was to determine the nature of the cysteine residue thiol oxidation that prevents p53 from binding its DNA target and its effect on p53 structure. Cysteine 68-76 tumor protein p53 Homo sapiens 115-118 14981901-6 2003 Only one tumour, which previously had shown expression and mutation in the p53, had a point mutation at codon 117 of exon 2 of the p21 gene with a resulting Cys-->Tyr amino acid substitution. Cysteine 157-160 tumor protein p53 Homo sapiens 75-78 14580323-2 2003 The goal of the current research was to determine the nature of the cysteine residue thiol oxidation that prevents p53 from binding its DNA target and its effect on p53 structure. Cysteine 68-76 tumor protein p53 Homo sapiens 165-168 11554448-3 2001 p53 is a zinc-binding protein containing several reactive cysteines, and its key biochemical property, sequence-specific DNA binding, is dependent upon metal and redox regulation in vitro. Cysteine 58-67 tumor protein p53 Homo sapiens 0-3 12427017-7 2002 Finally, we have identified a critical cysteine residue that nitric oxide modifies to disrupt Hdm2-p53 binding. Cysteine 39-47 tumor protein p53 Homo sapiens 99-102 11964141-10 2002 These results suggest that p53 is vulnerable to free radical-mediated oxidation at cysteine residues. Cysteine 83-91 tumor protein p53 Homo sapiens 27-30 12663048-7 2003 Direct reduction by WR1065 of key cysteines in p53 may play an important role in this alternative pathway, as shown by the fact that WR1065 activated the redox-dependent, DNA-binding activity of p53 in vitro. Cysteine 34-43 tumor protein p53 Homo sapiens 47-50 12663048-7 2003 Direct reduction by WR1065 of key cysteines in p53 may play an important role in this alternative pathway, as shown by the fact that WR1065 activated the redox-dependent, DNA-binding activity of p53 in vitro. Cysteine 34-43 tumor protein p53 Homo sapiens 195-198 12034820-0 2002 Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277. Cysteine 104-112 tumor protein p53 Homo sapiens 32-35 10747932-6 2000 These analyses identified a subset of cysteine and histidine residues required for stimulation of late gene expression, physical interaction with E1b 55k, and p53 destabilization. Cysteine 38-46 tumor protein p53 Homo sapiens 159-162 10998350-2 2000 Methoxy-polyethylene glycol-maleimide MW 2000 (MAL-PEG) was used to covalently tag p53 protein that was oxidized at cysteine residues in cultured cells. Cysteine 116-124 tumor protein p53 Homo sapiens 83-86 10998350-4 2000 The oxidized p53 had an average of one cysteine residue oxidized per p53 protein molecule. Cysteine 39-47 tumor protein p53 Homo sapiens 13-16 10998350-4 2000 The oxidized p53 had an average of one cysteine residue oxidized per p53 protein molecule. Cysteine 39-47 tumor protein p53 Homo sapiens 69-72 10998350-9 2000 The data indicate that an average of one cysteine residue per p53 protein molecule is highly sensitive to oxidation and that p53 can be efficiently oxidized by PDTC in cultured cells. Cysteine 41-49 tumor protein p53 Homo sapiens 62-65 11273008-4 2001 The second glioblastoma also contained multiple, but different mutations: p53 mutations in codons 158 (CGC-->CAC, Arg-->His) and 273 (CGT-->TGT, Arg-->Cys), and a PTEN mutation in codon 233 (CGA-->TGA, Arg-->Stop). Cysteine 163-166 tumor protein p53 Homo sapiens 74-77 10825467-1 2000 The dietary isothiocyanates and cancer chemopreventive agents phenethyl isothiocyanate and allyl isothiocyanate and their cysteine conjugates inhibited the growth and induced apoptosis of human leukaemia HL60 (p53-) and human myeloblastic leukaemia-1 cells (p53+) in vitro. Cysteine 122-130 tumor protein p53 Homo sapiens 210-213 10825467-1 2000 The dietary isothiocyanates and cancer chemopreventive agents phenethyl isothiocyanate and allyl isothiocyanate and their cysteine conjugates inhibited the growth and induced apoptosis of human leukaemia HL60 (p53-) and human myeloblastic leukaemia-1 cells (p53+) in vitro. Cysteine 122-130 tumor protein p53 Homo sapiens 258-261 10723139-7 2000 When we mutated the seven cysteine residues of RING finger domain of MDM2 in the carboxyl terminus, the disruption of each residue in the RING finger completely diminished the ubiquitin ligase activity of MDM2 toward MDM2 itself and toward tumor suppressor p53. Cysteine 26-34 tumor protein p53 Homo sapiens 257-260 11023067-7 2000 Mutations of p53 were present in 3 of 38 HPV-positive samples: one with an ATG-->TTG transversion (Met-->Leu) in codon 237 of exon 7; and the others with a TGC-->TGG transversion (Cys-->Trp) in codon 242 of exon 7, and a CGT-->CCT transversion (Arg-->Pro) in codon 273 of exon 8, respectively. Cysteine 189-192 tumor protein p53 Homo sapiens 13-16 10605931-4 2000 Second, they regulate the DNA-binding activity of p53 by modulating the redox status of a critical set of cysteines in the DNA-binding domain, which are also involved in the coordination of zinc. Cysteine 106-115 tumor protein p53 Homo sapiens 50-53 10531375-1 1999 The p53 tumor suppressor protein is a transcription factor that binds DNA in a sequence-specific manner through a protein domain stabilized by the coordination of zinc within a tetrahedral cluster of three cysteine residues and one histidine residue. Cysteine 206-214 tumor protein p53 Homo sapiens 4-7 22607421-14 2000 We suggested that the irreversibility of p53 oxidation was due, at least in part, to the removal of intrinsic zinc from its position in the DNA binding domain (after oxidation of the three cysteines to which the zinc ion is coordinated in the reduced protein) accompanied by a change in the p53 conformation. Cysteine 189-198 tumor protein p53 Homo sapiens 41-44 10464313-8 1999 We conclude that the irreversibility of p53 oxidation is due, at least in part, to the removal of intrinsic zinc from its position in the DNA binding domain accompanied by a conformational change of the p53 molecule after oxidation of the three cysteines to which the zinc ion is coordinated in the reduced protein. Cysteine 245-254 tumor protein p53 Homo sapiens 40-43 10486243-3 1999 These two bases make contact with cysteine-277 of the human p53. Cysteine 34-42 tumor protein p53 Homo sapiens 60-63 10464313-8 1999 We conclude that the irreversibility of p53 oxidation is due, at least in part, to the removal of intrinsic zinc from its position in the DNA binding domain accompanied by a conformational change of the p53 molecule after oxidation of the three cysteines to which the zinc ion is coordinated in the reduced protein. Cysteine 245-254 tumor protein p53 Homo sapiens 203-206 9668066-0 1998 Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation. Cysteine 69-77 tumor protein p53 Homo sapiens 65-68 10628393-5 1999 In contrast to previous studies showing p53-dependent GML expression, of the 3 cell lines expressing GML mRNA, one had a p53 gene mutation (codon 245: Gly to Cys). Cysteine 158-161 tumor protein p53 Homo sapiens 121-124 10334492-7 1999 A p53 mutation in codon 273 (CGT-->TGT, Arg-->Cys) was identified in the first biopsy and persisted throughout the course of the disease. Cysteine 52-55 tumor protein p53 Homo sapiens 2-5 9796399-8 1998 Analysis of the p53 gene by the polymerase chain reaction-single strand conformation polymorphism method showed one base transposition, from TAT to TGT (Tyr to Cys), at codon 220 of exon 6. Cysteine 160-163 tumor protein p53 Homo sapiens 16-19 9668066-9 1998 We found that PDTC increased p53 cysteine residue oxidation in vivo. Cysteine 33-41 tumor protein p53 Homo sapiens 29-32 9187098-5 1997 Among p53 mutations at various sites, mutation at codon 242 (C TGC --> C CGC; Cys --> Arg) was specifically observed in both skin cancers and actinic keratoses. Cysteine 81-84 tumor protein p53 Homo sapiens 6-9 8110876-4 1994 p53 mutations were restricted to one case of myeloid blast crisis, showing a CGC-->TGC (Arg-->Cys) mutation at codon 283; two additional cases displayed LOH at 17p13 in the absence of p53 mutations. Cysteine 100-103 tumor protein p53 Homo sapiens 0-3 9042396-9 1997 The mutation in codon 170 is adjacent to a mutation hotspot of the human p53 gene (codon 175) and eliminates a critical zinc-coordinating cysteine residue such that the mutant protein is likely to be denatured and have a dominant negative effect on normal p53 function. Cysteine 138-146 tumor protein p53 Homo sapiens 73-76 9042396-9 1997 The mutation in codon 170 is adjacent to a mutation hotspot of the human p53 gene (codon 175) and eliminates a critical zinc-coordinating cysteine residue such that the mutant protein is likely to be denatured and have a dominant negative effect on normal p53 function. Cysteine 138-146 tumor protein p53 Homo sapiens 256-259 18726304-2 1997 It was confirmed that the mt-p53 cDNA contained the complete coding sequence of p53 gene but mutated at codon 245 (G-->T) and resulted in glycine to cysteine by sequencing analysis. Cysteine 152-160 tumor protein p53 Homo sapiens 29-32 8055938-1 1994 Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding. Cysteine 66-74 tumor protein p53 Homo sapiens 94-97 8055938-8 1994 Further characterization of the purified p53 revealed that the protein possesses highly reactive cysteine residues. Cysteine 97-105 tumor protein p53 Homo sapiens 41-44 8055938-12 1994 The oxidation of the p53 cysteine residues was also observed for nuclear p53 in baculovirus-infected insect cells. Cysteine 25-33 tumor protein p53 Homo sapiens 21-24 8055938-12 1994 The oxidation of the p53 cysteine residues was also observed for nuclear p53 in baculovirus-infected insect cells. Cysteine 25-33 tumor protein p53 Homo sapiens 73-76 8055938-13 1994 The redox status of the nuclear p53 regulates its DNA-binding activity in vitro confirming the essential role of the reduced state of cysteine residues in p53 for detectable DNA-binding activity. Cysteine 134-142 tumor protein p53 Homo sapiens 32-35 8055938-13 1994 The redox status of the nuclear p53 regulates its DNA-binding activity in vitro confirming the essential role of the reduced state of cysteine residues in p53 for detectable DNA-binding activity. Cysteine 134-142 tumor protein p53 Homo sapiens 155-158 9038605-4 1996 In 4 cases, the mutations lead to distinct changes in the primary or secondary structure of the protein (cysteine-->tyrosine, proline-->leucine) and were associated with marked accumulation of p53 protein. Cysteine 105-113 tumor protein p53 Homo sapiens 199-202 9182295-5 1996 Single strand conformation polymorphism analysis (SSCP-PCR) from DNA obtained by microdissection demonstrated the presence of a mutation (TAT-->TGT; Tyr-->Cys) in codon 220, exon six of the p53 gene in the anaplastic component, that was absent in the well-differentiated follicular areas. Cysteine 161-164 tumor protein p53 Homo sapiens 196-199 8290256-5 1994 Two mutations were identified in the p53 cDNA from HC11 cells: a missense mutation at codon 138, substituting Trp for Cys, and a microdeletion, codon 123 to 130, of exon 5. Cysteine 118-121 tumor protein p53 Homo sapiens 37-40 34862374-3 2021 PRIMA-1 and eprenetapopt (APR-246/PRIMA-1MET) are small molecules that are converted into the biologically active compound, methylene quinuclidinone (MQ), shown to reactivate mutant p53 by binding covalently to cysteine residues. Cysteine 211-219 tumor protein p53 Homo sapiens 182-185 1549103-4 1992 A new dominant mutation of p53, resulting in the change of a cysteine to an arginine at amino acid residue 141, was identified. Cysteine 61-69 tumor protein p53 Homo sapiens 27-30 1737852-7 1992 The other two nonhereditary p53 mutations included a T to G transversion at codon 270 (phenylalanine to cysteine) and a G to C transversion at codon 248 (arginine to proline). Cysteine 104-112 tumor protein p53 Homo sapiens 28-31 8221663-2 1993 Mutations of the p53 gene were found in six of seven ES cell lines: a missense mutation of TGC (Cys)-->TAC (Try) at codon 141 in one, a missense mutation of CGT (Arg)-->TGT (Cys) at codon 273 in one, a missense mutation of TGC (Cys)-->TTC (Phe) at codon 176 in three, and one base deletion of CGC-->CG at codon 283 in one. Cysteine 96-99 tumor protein p53 Homo sapiens 17-20 8221663-2 1993 Mutations of the p53 gene were found in six of seven ES cell lines: a missense mutation of TGC (Cys)-->TAC (Try) at codon 141 in one, a missense mutation of CGT (Arg)-->TGT (Cys) at codon 273 in one, a missense mutation of TGC (Cys)-->TTC (Phe) at codon 176 in three, and one base deletion of CGC-->CG at codon 283 in one. Cysteine 180-183 tumor protein p53 Homo sapiens 17-20 8221663-2 1993 Mutations of the p53 gene were found in six of seven ES cell lines: a missense mutation of TGC (Cys)-->TAC (Try) at codon 141 in one, a missense mutation of CGT (Arg)-->TGT (Cys) at codon 273 in one, a missense mutation of TGC (Cys)-->TTC (Phe) at codon 176 in three, and one base deletion of CGC-->CG at codon 283 in one. Cysteine 180-183 tumor protein p53 Homo sapiens 17-20 21573446-8 1993 The point mutation of p53 gene was found at codon 181 contained C to T transversions (Amino acid switch: Arg --> Cys) in ES-4 esophageal cancer. Cysteine 116-119 tumor protein p53 Homo sapiens 22-25 8389256-6 1993 The p53 point mutations in the three HCC cell lines from Japan resulted in the amino acid changes of cysteine for tyrosine in cell line HuH 7 at codon 220 (A:T-->G:C), alanine for glycine in cell line HLF at codon 244 (G:C-->C:G), and serine for arginine in cell line HLE at codon 249 (G:C-->C:G). Cysteine 101-109 tumor protein p53 Homo sapiens 4-7 1918170-4 1991 We previously identified a case of human acute myelogenous leukemia (AML) in which both alleles of the p53 gene had undergone independent missense mutations (at codons 135 cys to ser and 246 met to val). Cysteine 172-175 tumor protein p53 Homo sapiens 103-106 2254323-7 1990 N alpha-Acetyl[D-Phe45, Arg47] hirudin45-65 (P53) emerged as a pure competitive inhibitor with a Ki = 2.8 +/- 0.9 nM and IC50 = 4.0 +/- 0.8 nM (human alpha-thrombin) and is designated as a "bifunctional" inhibitor. Cysteine 7-14 tumor protein p53 Homo sapiens 45-48 34831372-0 2021 Redox Sensitive Cysteine Residues as Crucial Regulators of Wild-Type and Mutant p53 Isoforms. Cysteine 16-24 tumor protein p53 Homo sapiens 80-83 34831372-7 2021 We will also discuss therapeutic opportunities using small molecules targeting cysteines capable of modifying the structure and function of the p53 mutant isoforms in view of possible anticancer therapies for patients possessing the mutation in the TP53 gene. Cysteine 79-88 tumor protein p53 Homo sapiens 144-147 34386946-6 2021 Conjugation of the p53 short-chain peptide of 25 amino acids occurs through a combination of electrostatic interactions and covalent bonds between cysteine residues at the N-terminal of the peptide and the surface of the AuNPs. Cysteine 147-155 tumor protein p53 Homo sapiens 19-22 34679713-0 2021 p53 Forms Redox-Dependent Protein-Protein Interactions through Cysteine 277. Cysteine 63-71 tumor protein p53 Homo sapiens 0-3 34679713-4 2021 In the past few decades, p53 has been shown to be a redox-sensitive protein, and undergoes reversible cysteine oxidation both in vitro and in vivo. Cysteine 102-110 tumor protein p53 Homo sapiens 25-28 34679713-7 2021 Cysteine 277 is required for most of the disulfide-dependent interactions of p53, including those with 14-3-3theta and 53BP1. Cysteine 0-8 tumor protein p53 Homo sapiens 77-80 34683888-8 2021 The docking results confirmed the ability of both NPs to bind to the p53 gene with relevant potency in binding to other tested gens and participation of cysteine SH-functional group in such interaction. Cysteine 153-161 tumor protein p53 Homo sapiens 69-72 35204825-8 2022 The p53 complexes with SIRT2, MUL1, USP7, TXN, PIN1 and PPIF control regulation of p53 function through post-translational modifications, such as lysine acetylation or ubiquitination, cysteine/cystine redox transformation and peptidyl-prolyl cis-trans isomerization. Cysteine 184-192 tumor protein p53 Homo sapiens 4-7 35487360-11 2022 The metal ions with weak hydrolysis constants and strong polarization forces could readily interact with N-containing histidine and S-containing cysteine of p53 DBD, which resulted in high Ka values. Cysteine 145-153 tumor protein p53 Homo sapiens 157-160 35312310-10 2022 Dithiothreitol-reduced protein was more efficiently cross-linked indicating that p53 cysteine residues play a key role in protein modification. Cysteine 85-93 tumor protein p53 Homo sapiens 81-84 35312310-12 2022 The formation of intermolecular complexes was a consequence of HN2 cross-linked cysteine residues between two molecules of p53. Cysteine 80-88 tumor protein p53 Homo sapiens 123-126 35204825-8 2022 The p53 complexes with SIRT2, MUL1, USP7, TXN, PIN1 and PPIF control regulation of p53 function through post-translational modifications, such as lysine acetylation or ubiquitination, cysteine/cystine redox transformation and peptidyl-prolyl cis-trans isomerization. Cysteine 184-192 tumor protein p53 Homo sapiens 83-86