PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28381353-8 2017 Oppositely, caseins, a whey protein/casein mixture (1:4 w/w), and glutamine aggravated the TNF-alpha-induced TNF and SOD2 gene expression. Glutamine 66-75 superoxide dismutase 2 Homo sapiens 117-121 11929218-8 2002 The calculations support a very important role for the conserved second sphere Gln in MnSOD in specifically destabilizing coordinated H2O relative to coordinated OH-, and thus disfavouring the oxidized state of the metal ion. Glutamine 79-82 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. Glutamine 146-149 superoxide dismutase 2 Homo sapiens 19-24 11696579-5 2001 Both the inhibition of eNOS and the changes in its post-translational modifications were reversed by antisense inhibition of glutamine:fructose-6-phosphate amidotransferase, the rate-limiting enzyme of the hexosamine pathway, or by blocking mitochondrial superoxide overproduction with uncoupling protein-1 (UCP-1) or manganese superoxide dismutase (MnSOD). Glutamine 125-134 superoxide dismutase 2 Homo sapiens 318-348 11696579-5 2001 Both the inhibition of eNOS and the changes in its post-translational modifications were reversed by antisense inhibition of glutamine:fructose-6-phosphate amidotransferase, the rate-limiting enzyme of the hexosamine pathway, or by blocking mitochondrial superoxide overproduction with uncoupling protein-1 (UCP-1) or manganese superoxide dismutase (MnSOD). Glutamine 125-134 superoxide dismutase 2 Homo sapiens 350-355 11001096-8 2000 We have generated a mutant of MnSOD with the active site Gln in the location characteristic of Fe-specific SODs. Glutamine 57-60 superoxide dismutase 2 Homo sapiens 30-35 11001096-11 2000 Thus, moving the active site Gln converts Mn-specific SOD into a cambialistic SOD and the Gln proves to be important but not the sole determinant of metal-ion specificity. Glutamine 29-32 superoxide dismutase 2 Homo sapiens 54-57 11001096-11 2000 Thus, moving the active site Gln converts Mn-specific SOD into a cambialistic SOD and the Gln proves to be important but not the sole determinant of metal-ion specificity. Glutamine 29-32 superoxide dismutase 2 Homo sapiens 78-81 11001096-11 2000 Thus, moving the active site Gln converts Mn-specific SOD into a cambialistic SOD and the Gln proves to be important but not the sole determinant of metal-ion specificity. Glutamine 90-93 superoxide dismutase 2 Homo sapiens 54-57 11001096-13 2000 We have directly observed the side chain of the active site Gln in Fe2+ SOD and Fe2+ (Mn)SOD by 15N NMR. Glutamine 60-63 superoxide dismutase 2 Homo sapiens 72-75 10852710-0 2000 Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis. Glutamine 25-34 superoxide dismutase 2 Homo sapiens 48-78 10852710-1 2000 Glutamine 143 in human manganese superoxide dismutase (MnSOD) forms a hydrogen bond with the manganese-bound solvent molecule and is investigated by replacement using site-specific mutagenesis. Glutamine 0-9 superoxide dismutase 2 Homo sapiens 23-53 10852710-1 2000 Glutamine 143 in human manganese superoxide dismutase (MnSOD) forms a hydrogen bond with the manganese-bound solvent molecule and is investigated by replacement using site-specific mutagenesis. Glutamine 0-9 superoxide dismutase 2 Homo sapiens 55-60 10852710-3 2000 Two new water molecules in Q143A MnSOD were situated in positions nearly identical with the Oepsilon1 and Nepsilon2 of the replaced Gln 143 side chain and maintained a hydrogen-bonded network connecting the manganese-bound solvent molecule to other residues in the active site. Glutamine 132-135 superoxide dismutase 2 Homo sapiens 33-38 9537988-0 1998 Probing the active site of human manganese superoxide dismutase: the role of glutamine 143. Glutamine 77-86 superoxide dismutase 2 Homo sapiens 33-63 9537988-1 1998 Structural and biochemical characterization of the nonliganding residue glutamine 143 near the manganese of human Mn superoxide dismutase (hMnSOD), a homotetramer of 22 kDa, reveals a functional role for this residue. Glutamine 72-81 superoxide dismutase 2 Homo sapiens 114-137 9537988-1 1998 Structural and biochemical characterization of the nonliganding residue glutamine 143 near the manganese of human Mn superoxide dismutase (hMnSOD), a homotetramer of 22 kDa, reveals a functional role for this residue. Glutamine 72-81 superoxide dismutase 2 Homo sapiens 139-145 9537988-3 1998 We have prepared the site-specific mutant of hMnSOD with the conservative replacement of Gln 143 --> Asn (Q143N). Glutamine 89-92 superoxide dismutase 2 Homo sapiens 45-51 9537988-10 1998 Also, unlike the wild-type Mn(III)SOD, which is electron paramagnetic resonance (EPR) silent, Q143N MnSOD has a complex EPR spectrum with many resonances in the region below 2250 G. We conclude that the Gln 143 --> Asn mutation has increased the reduction potential of manganese to stabilize Mn(II), indicating that Gln 143 has a substantial role in maintaining a reduction potential favorable for the oxidation and reduction cycles in the catalytic disproportionation of superoxide. Glutamine 203-206 superoxide dismutase 2 Homo sapiens 100-105 9537988-10 1998 Also, unlike the wild-type Mn(III)SOD, which is electron paramagnetic resonance (EPR) silent, Q143N MnSOD has a complex EPR spectrum with many resonances in the region below 2250 G. We conclude that the Gln 143 --> Asn mutation has increased the reduction potential of manganese to stabilize Mn(II), indicating that Gln 143 has a substantial role in maintaining a reduction potential favorable for the oxidation and reduction cycles in the catalytic disproportionation of superoxide. Glutamine 319-322 superoxide dismutase 2 Homo sapiens 100-105 11001096-13 2000 We have directly observed the side chain of the active site Gln in Fe2+ SOD and Fe2+ (Mn)SOD by 15N NMR. Glutamine 60-63 superoxide dismutase 2 Homo sapiens 89-92 11001096-15 2000 Since a shorter distance from Gln to Fe and stronger interaction with Fe correlate with a lower Em in Fe(Mn)SOD, Gln has the effect of destabilizing additional electron density on the metal ion. Glutamine 30-33 superoxide dismutase 2 Homo sapiens 108-111 11001096-15 2000 Since a shorter distance from Gln to Fe and stronger interaction with Fe correlate with a lower Em in Fe(Mn)SOD, Gln has the effect of destabilizing additional electron density on the metal ion. Glutamine 113-116 superoxide dismutase 2 Homo sapiens 108-111 34858880-9 2021 Knowing that TcSODA is acetylated at lysine residues K44 and K97, and that K97 is located at a similar region in the protein structure as K68 in human manganese superoxide dismutase (MnSOD), responsible for regulating MnSOD activity, we generated mutated versions of TcSODA at K44 and K97 and found that replacing K97 by glutamine, which mimics an acetylated lysine, negatively affects the enzyme activity in vitro. Glutamine 321-330 superoxide dismutase 2 Homo sapiens 218-223 28398002-4 2017 Our data identify impairment of the pyruvate and l-glutamine metabolism causing toxic accumulation of alpha-ketoglutarate in the Sod2-deficient and intrinsically aged stromal precursor cells as a major cause for their reduced lineage differentiation. Glutamine 49-60 superoxide dismutase 2 Homo sapiens 129-133 28028182-7 2017 This study shows that SOD2 specifically binds to hsp70 at 445GERAMT450 Small peptides containing GERAMT inhibited the transfer of SOD2 to the mitochondria and decreased SOD2 activity in vitro and in vivo To determine the amino acid residues in hsp70 that are critical for SOD2 interactions, we substituted each amino acid residue for alanine or more conservative residues, glutamine or asparagine, in the GERAMT-binding site. Glutamine 373-382 superoxide dismutase 2 Homo sapiens 22-26 28028182-7 2017 This study shows that SOD2 specifically binds to hsp70 at 445GERAMT450 Small peptides containing GERAMT inhibited the transfer of SOD2 to the mitochondria and decreased SOD2 activity in vitro and in vivo To determine the amino acid residues in hsp70 that are critical for SOD2 interactions, we substituted each amino acid residue for alanine or more conservative residues, glutamine or asparagine, in the GERAMT-binding site. Glutamine 373-382 superoxide dismutase 2 Homo sapiens 130-134 28028182-7 2017 This study shows that SOD2 specifically binds to hsp70 at 445GERAMT450 Small peptides containing GERAMT inhibited the transfer of SOD2 to the mitochondria and decreased SOD2 activity in vitro and in vivo To determine the amino acid residues in hsp70 that are critical for SOD2 interactions, we substituted each amino acid residue for alanine or more conservative residues, glutamine or asparagine, in the GERAMT-binding site. Glutamine 373-382 superoxide dismutase 2 Homo sapiens 130-134 28028182-7 2017 This study shows that SOD2 specifically binds to hsp70 at 445GERAMT450 Small peptides containing GERAMT inhibited the transfer of SOD2 to the mitochondria and decreased SOD2 activity in vitro and in vivo To determine the amino acid residues in hsp70 that are critical for SOD2 interactions, we substituted each amino acid residue for alanine or more conservative residues, glutamine or asparagine, in the GERAMT-binding site. Glutamine 373-382 superoxide dismutase 2 Homo sapiens 130-134 23461587-7 2013 These computations properly reproduce the experimental trend and reveal that the drastically elevated E(m) of the metal substituted protein stems from a larger separation between the second-sphere Gln residue and the coordinated solvent in Mn(Fe)SOD relative to MnSOD, which causes a weakening of the corresponding H-bond interaction in the oxidized state and alleviates steric crowding in the reduced state. Glutamine 197-200 superoxide dismutase 2 Homo sapiens 246-249