PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24269899-10 2014 Further studies demonstrated a significant increase in posttranslational modifications of tyrosine and lysine residues in MnSOD protein and oxidation of Cys at the active site (Cys32 and Cys35) and the regulatory site (Cys62 and Cys69) of Trx1 in high-grade PCa compared to BN tissues. Tyrosine 90-98 superoxide dismutase 2 Homo sapiens 122-127 9537987-0 1998 Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Tyrosine 111-119 superoxide dismutase 2 Homo sapiens 53-83 9537987-2 1998 We have prepared the mutant containing the replacement Tyr 34 --> Phe (Y34F) in human manganese superoxide dismutase (hMnSOD) and crystallized it in two different crystal forms, orthorhombic and hexagonal. Tyrosine 55-58 superoxide dismutase 2 Homo sapiens 89-119 9537987-2 1998 We have prepared the mutant containing the replacement Tyr 34 --> Phe (Y34F) in human manganese superoxide dismutase (hMnSOD) and crystallized it in two different crystal forms, orthorhombic and hexagonal. Tyrosine 55-58 superoxide dismutase 2 Homo sapiens 121-127 9537987-4 1998 Both crystal forms give structures that are closely superimposable with that of wild-type hMnSOD, with the phenyl rings of Tyr 34 in the wild type and Phe 34 in the mutant very similar in orientation. Tyrosine 123-126 superoxide dismutase 2 Homo sapiens 90-96 9537987-7 1998 The functional role of the side chain hydroxyl of Tyr 34 can be evaluated by comparison of the Y34F mutant with the wild-type hMnSOD. Tyrosine 50-53 superoxide dismutase 2 Homo sapiens 126-132 8876227-6 1996 Immunoprecipitation and amino acid sequencing techniques identified manganese superoxide dismutase, the major antioxidant enzyme in mitochondria, as one of the targets of tyrosine nitration. Tyrosine 171-179 superoxide dismutase 2 Homo sapiens 68-98 8876227-8 1996 Exposure of recombinant human manganese superoxide dismutase to peroxynitrite resulted in a dose-dependent (IC50 = 10 microM) decrease in enzymatic activity and concomitant increase in tyrosine nitration. Tyrosine 185-193 superoxide dismutase 2 Homo sapiens 30-60 28165386-5 2017 Markedly, oxidative modifications of MNSOD were identified at histidine (H54 and H55), tyrosine (Y58), tryptophan (W147, W149, W205 and W210) and asparagine (N206 and N209) residues additional to methionine. Tyrosine 87-95 superoxide dismutase 2 Homo sapiens 37-42 27227512-0 2016 Mechanism of the Reaction of Human Manganese Superoxide Dismutase with Peroxynitrite: Nitration of Critical Tyrosine 34. Tyrosine 108-116 superoxide dismutase 2 Homo sapiens 35-65 24437351-6 2014 Elevated ROS derived from NOX1 activation and downregulation of SOD in NIH3T3RET-MEN2A and NIH3T3RET-MEN 2B cells may be involved in RET constitutive tyrosine auto-phosphorylation, and scavengers of ROS such as catalase and blocking NOX1 are useful for targeting RET tyrosine kinase activation in cancer. Tyrosine 150-158 superoxide dismutase 2 Homo sapiens 64-67 9603906-0 1998 Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine. Tyrosine 106-114 superoxide dismutase 2 Homo sapiens 22-52 9603906-3 1998 This study proposes that nitration of a specific tyrosine residue is responsible for inactivation of recombinant human mitochondrial manganese-superoxide dismutase (Mn-SOD) by peroxynitrite. Tyrosine 49-57 superoxide dismutase 2 Homo sapiens 133-163 9603906-3 1998 This study proposes that nitration of a specific tyrosine residue is responsible for inactivation of recombinant human mitochondrial manganese-superoxide dismutase (Mn-SOD) by peroxynitrite. Tyrosine 49-57 superoxide dismutase 2 Homo sapiens 165-171 9603906-4 1998 Mass spectroscopic analysis of the peroxynitrite-inactivated Mn-SOD showed an increased molecular mass because of a single nitro group substituted onto a tyrosine residue. Tyrosine 154-162 superoxide dismutase 2 Homo sapiens 61-67 29737331-0 2018 Human Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivo. Tyrosine 91-99 superoxide dismutase 2 Homo sapiens 6-29 29737331-3 2018 Then, peroxynitrite can promote the regio-specific nitration of MnSOD at active site tyrosine 34, which turns the enzyme inactive. Tyrosine 85-93 superoxide dismutase 2 Homo sapiens 64-69 29737331-7 2018 Herein, kinetic, molecular, structural biology and computational studies are integrated to rationalize the specificity and impact of peroxynitrite-dependent MnSOD tyrosine nitration in vitro and in vivo from both functional and structural perspectives. Tyrosine 163-171 superoxide dismutase 2 Homo sapiens 157-162 21080654-0 2010 Peroxynitrite mediates active site tyrosine nitration in manganese superoxide dismutase. Tyrosine 35-43 superoxide dismutase 2 Homo sapiens 57-87 23880762-6 2013 We report that overexpression of Mn-SOD enhances tyrosine phosphorylation of TCR-associated membrane proximal signal transduction molecules Lck, LAT, ZAP70, PLCgamma1, and SLP76 within 1 min of TCR cross-linking. Tyrosine 49-57 superoxide dismutase 2 Homo sapiens 33-39 21167124-0 2011 Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration. Tyrosine 95-103 superoxide dismutase 2 Homo sapiens 39-69 21167124-6 2011 However, the molecular basis about MnSOD tyrosine nitration affects the protein catalytic function is mostly unknown. Tyrosine 41-49 superoxide dismutase 2 Homo sapiens 35-40 21080654-9 2010 Distinctive patterns of tyrosine nitration within MnSOD by various reagents were revealed and quantified by MS/MS analysis of MnSOD trypsin digest peptides. Tyrosine 24-32 superoxide dismutase 2 Homo sapiens 50-55 21080654-9 2010 Distinctive patterns of tyrosine nitration within MnSOD by various reagents were revealed and quantified by MS/MS analysis of MnSOD trypsin digest peptides. Tyrosine 24-32 superoxide dismutase 2 Homo sapiens 126-131 21080654-10 2010 These analyses showed that three of the seven tyrosine residues of MnSOD (Tyr34, Tyr9, and Tyr11) were the most susceptible to nitration and that the relative amounts of nitration of these residues varied widely depending upon the nature of the nitrating agent. Tyrosine 46-54 superoxide dismutase 2 Homo sapiens 67-72 21080654-13 2010 These kinetics and the 20-fold increase in the efficiency of tyrosine nitration in the presence of CO2 suggest a specific role for the carbonate radical anion ( CO3(-)) in MnSOD nitration by PN. Tyrosine 61-69 superoxide dismutase 2 Homo sapiens 172-177 17395009-4 2007 The formation of protein radicals was followed by tyrosine nitration in the case of MnSOD. Tyrosine 50-58 superoxide dismutase 2 Homo sapiens 84-89 19837190-6 2010 On the other hand, tyrosine 34 of human MnSOD was exclusively nitrated to 3-nitrotyrosine and almost completely inactivated by the reaction with peroxynitrite. Tyrosine 19-27 superoxide dismutase 2 Homo sapiens 40-45 19265433-0 2009 Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis. Tyrosine 53-61 superoxide dismutase 2 Homo sapiens 22-52 17395009-7 2007 The data are consistent with the direct reaction of peroxynitrite with the Mn center and a metal-catalyzed nitration of Tyr-34 in MnSOD. Tyrosine 120-123 superoxide dismutase 2 Homo sapiens 130-135 17395009-9 2007 Our results help to rationalize MnSOD tyrosine nitration observed in inflammatory conditions in vivo in the presence of low molecular weight scavengers such as glutathione that otherwise would completely consume nitrogen dioxide and prevent nitration reactions. Tyrosine 38-46 superoxide dismutase 2 Homo sapiens 32-37 16819819-3 2006 Human MnSOD was prepared in which all nine tyrosine residues in each subunit are replaced with 3-fluorotyrosine. Tyrosine 43-51 superoxide dismutase 2 Homo sapiens 6-11 16214029-5 2005 A time course study demonstrated that increases in MnSOD activity prior to the onset of apoptosis correlated with alterations in the levels of nitration of tyrosine residue(s) of MnSOD protein. Tyrosine 156-164 superoxide dismutase 2 Homo sapiens 51-56 16150974-3 2005 Each of the nine tyrosine residues in each of the four subunits of the homotetramer of human MnSOD was replaced with 3-fluorotyrosine. Tyrosine 17-25 superoxide dismutase 2 Homo sapiens 93-98 16214029-5 2005 A time course study demonstrated that increases in MnSOD activity prior to the onset of apoptosis correlated with alterations in the levels of nitration of tyrosine residue(s) of MnSOD protein. Tyrosine 156-164 superoxide dismutase 2 Homo sapiens 179-184 15884106-5 2005 Expression of Cu, ZnSOD, MnSOD and tyrosine-nitrated MnSOD were analyzed by Western blot and/or immunohistochemistry. Tyrosine 35-43 superoxide dismutase 2 Homo sapiens 53-58 12646264-1 2003 Endogenous tyrosine nitration and inactivation of manganese superoxide dismutase (MnSOD) has previously been shown to occur in both human and rat chronic renal allograft rejection. Tyrosine 11-19 superoxide dismutase 2 Homo sapiens 50-80 14656937-9 2004 Co-localization studies established that the mitochondria are a primary site for 3-nitrotyrosine localization and immunoprecipitation/immunoblotting experiments confirmed that MnSOD tyrosine nitration occurs in AIDS-KS cells. Tyrosine 88-96 superoxide dismutase 2 Homo sapiens 176-181 14656937-10 2004 Functional SOD assays showed that AIDS-KS cells possess significantly lower MnSOD activity relative to matched control cells; findings which correspond with ongoing MnSOD tyrosine nitration and subsequent inactivation within AIDS-KS cells. Tyrosine 171-179 superoxide dismutase 2 Homo sapiens 165-170 14678790-7 2004 Extensive tyrosine nitration of Mn-superoxide dismutase occurred when exposed to either cytochrome c or MPx-11 in the presence of H2O2 and NO2-, with no apparent decrease in catalytic activity. Tyrosine 10-18 superoxide dismutase 2 Homo sapiens 32-55 12646264-1 2003 Endogenous tyrosine nitration and inactivation of manganese superoxide dismutase (MnSOD) has previously been shown to occur in both human and rat chronic renal allograft rejection. Tyrosine 11-19 superoxide dismutase 2 Homo sapiens 82-87 12646264-4 2003 Tyrosine nitration of specific mitochondrial proteins, MnSOD and cytochrome c, occurred at the earliest time point examined, an event that preceded significant renal injury. Tyrosine 0-8 superoxide dismutase 2 Homo sapiens 55-60 11912930-5 2002 The active site of MnSOD is dominated by a hydrogen bond network comprising the manganese-bound aqueous ligand, the side chains of four residues (Gln-143, Tyr-34, His-30, and Tyr-166 from an adjacent subunit), as well as other water molecules. Tyrosine 155-158 superoxide dismutase 2 Homo sapiens 19-24 12207539-4 2002 Our experimental and computational data indicate that both reduced FeSOD and oxidized MnSOD do not bind hydroxide at high pH; rather, the active-site pK for these two species is attributed to deprotonation of a second-sphere tyrosine. Tyrosine 225-233 superoxide dismutase 2 Homo sapiens 86-91 11912930-5 2002 The active site of MnSOD is dominated by a hydrogen bond network comprising the manganese-bound aqueous ligand, the side chains of four residues (Gln-143, Tyr-34, His-30, and Tyr-166 from an adjacent subunit), as well as other water molecules. Tyrosine 175-178 superoxide dismutase 2 Homo sapiens 19-24 10488113-1 1999 Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. Tyrosine 213-216 superoxide dismutase 2 Homo sapiens 22-52 11744334-1 2001 Endogenous tyrosine nitration and inactivation of manganese superoxide dismutase (MnSOD) has previously been reported to occur during end-stage human renal allograft rejection. Tyrosine 11-19 superoxide dismutase 2 Homo sapiens 50-80 11744334-1 2001 Endogenous tyrosine nitration and inactivation of manganese superoxide dismutase (MnSOD) has previously been reported to occur during end-stage human renal allograft rejection. Tyrosine 11-19 superoxide dismutase 2 Homo sapiens 82-87 11328670-10 2001 Our laboratory has recently demonstrated that MnSOD is tyrosine nitrated and inactivated during human kidney allograft rejection and human pancreatic ductal adenocarcinoma. Tyrosine 55-63 superoxide dismutase 2 Homo sapiens 46-51 11328670-12 2001 Tyrosine nitration and inactivation of MnSOD would lead to increased levels of superoxide and concomitant increases in ONOO- within the mitochondria which, could lead to tyrosine nitration/oxidation of key mitochondrial proteins and ultimately mitochondrial dysfunction and cell death. Tyrosine 170-178 superoxide dismutase 2 Homo sapiens 39-44 10762167-3 2000 Nitrated tyrosine residue-containing protein was observed in the cerebrospinal fluid and was concluded to be manganese superoxide dismutase (Mn-SOD). Tyrosine 9-17 superoxide dismutase 2 Homo sapiens 109-139 10762167-3 2000 Nitrated tyrosine residue-containing protein was observed in the cerebrospinal fluid and was concluded to be manganese superoxide dismutase (Mn-SOD). Tyrosine 9-17 superoxide dismutase 2 Homo sapiens 141-147 10488113-1 1999 Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. Tyrosine 213-216 superoxide dismutase 2 Homo sapiens 54-59 10488113-1 1999 Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. Tyrosine 226-229 superoxide dismutase 2 Homo sapiens 22-52 10488113-1 1999 Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. Tyrosine 226-229 superoxide dismutase 2 Homo sapiens 54-59 10334867-6 1999 Collectively, these results suggest that complete inactivation of MnSOD by ONOO- can occur independent of the active site tyrosine residue and includes not only nitration of critical tyrosine residues but also tyrosine oxidation and subsequent formation of dityrosine. Tyrosine 122-130 superoxide dismutase 2 Homo sapiens 66-71 10334867-1 1999 Recent studies from this laboratory have demonstrated that human manganese superoxide dismutase (MnSOD) is a target for tyrosine nitration in several chronic inflammatory diseases including chronic organ rejection, arthritis, and tumorigenesis. Tyrosine 120-128 superoxide dismutase 2 Homo sapiens 65-95 10334867-1 1999 Recent studies from this laboratory have demonstrated that human manganese superoxide dismutase (MnSOD) is a target for tyrosine nitration in several chronic inflammatory diseases including chronic organ rejection, arthritis, and tumorigenesis. Tyrosine 120-128 superoxide dismutase 2 Homo sapiens 97-102 10334867-6 1999 Collectively, these results suggest that complete inactivation of MnSOD by ONOO- can occur independent of the active site tyrosine residue and includes not only nitration of critical tyrosine residues but also tyrosine oxidation and subsequent formation of dityrosine. Tyrosine 183-191 superoxide dismutase 2 Homo sapiens 66-71 10334867-6 1999 Collectively, these results suggest that complete inactivation of MnSOD by ONOO- can occur independent of the active site tyrosine residue and includes not only nitration of critical tyrosine residues but also tyrosine oxidation and subsequent formation of dityrosine. Tyrosine 183-191 superoxide dismutase 2 Homo sapiens 66-71