| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M402728200 |
| P698 | PubMed publication ID | 15328354 |
| P50 | author | Catherine Berthomieu | Q45851660 |
| P2093 | author name string | Claude Vidaud | |
| François Dupeyrat | |||
| Alain Lorphelin | |||
| P2860 | cites work | A novel nickel-containing superoxide dismutase from Streptomyces spp | Q24529926 |
| Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal | Q27617758 | ||
| A structure-based mechanism for copper-zinc superoxide dismutase | Q27639804 | ||
| Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A | Q27641795 | ||
| Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0 A resolution | Q27652228 | ||
| Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase | Q27729237 | ||
| Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution | Q27729825 | ||
| Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase | Q27732792 | ||
| Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography | Q27748554 | ||
| Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme? | Q27765168 | ||
| Modelling the three-dimensional structure and the electrostatic potential field of two Cu,Zn superoxide dismutase variants from tomato leaves. | Q30193371 | ||
| Conserved patterns in the Cu,Zn superoxide dismutase family. | Q30194350 | ||
| Crystal structure of yeast Cu,Zn superoxide dismutase. Crystallographic refinement at 2.5 A resolution | Q30195352 | ||
| Evolutionary aspects of superoxide dismutase: the copper/zinc enzyme | Q30195732 | ||
| What vibrations tell us about proteins. | Q30332582 | ||
| The infrared absorption of amino acid side chains | Q34166914 | ||
| Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms | Q34236223 | ||
| Structure and mechanism of copper, zinc superoxide dismutase | Q34255150 | ||
| Isolation of two cDNA clones from tomato containing two different superoxide dismutase sequences | Q35052186 | ||
| Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins | Q39753611 | ||
| The conformational analysis of peptides using Fourier transform IR spectroscopy | Q40401595 | ||
| Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms | Q40832095 | ||
| Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases | Q41076485 | ||
| Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis | Q41896194 | ||
| Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence | Q43553322 | ||
| Iron coordination in photosystem II: interaction between bicarbonate and the QB pocket studied by Fourier transform infrared spectroscopy | Q43573974 | ||
| Crystallographic characterization of a Cu,Zn superoxide dismutase from Photobacterium leiognathi | Q43794435 | ||
| Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study | Q44090094 | ||
| The two histidine axial ligands of the primary electron donor chlorophylls (P700) in photosystem I are similarly perturbed upon P700+ formation | Q44130571 | ||
| Electrochemistry of immobilized CuZnSOD and FeSOD and their interaction with superoxide radicals | Q44251576 | ||
| Assignment of active-site protons in the 1H-NMR spectrum of reduced human Cu/Zn superoxide dismutase | Q44533295 | ||
| A facilitated electron transfer of copper--zinc superoxide dismutase (SOD) based on a cysteine-bridged SOD electrode | Q45712739 | ||
| Faster superoxide dismutase mutants designed by enhancing electrostatic guidance | Q45965859 | ||
| The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: computational and experimental evaluation by mutational analysis | Q46281486 | ||
| Electrostatic recognition between superoxide and copper, zinc superoxide dismutase | Q47649395 | ||
| Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c. | Q53694755 | ||
| Evidence of his61 imidazolate bridge rupture in reduced crystalline Cu,Zn superoxide dismutase. | Q54094998 | ||
| Crystal structure of the cyanide-inhibitedXenopus laevisCu,Zn superoxide dismutase at 98 K | Q56877700 | ||
| Crystallographic Study of Azide-inhibited Bovine Cu,Zn Superoxide Dismutase | Q56877701 | ||
| Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in ?-, ?-, and random coil conformations | Q57223177 | ||
| Binding of fluoride to copper zinc superoxide dismutase | Q57975865 | ||
| P433 | issue | 46 | |
| P407 | language of work or name | English | Q1860 |
| P1104 | number of pages | 11 | |
| P304 | page(s) | 48091-48101 | |
| P577 | publication date | 2004-08-24 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Long distance charge redistribution upon Cu,Zn-superoxide dismutase reduction: significance for dismutase function | |
| P478 | volume | 279 |
| Q42427204 | CO binding and ligand discrimination in human myeloperoxidase |
| Q37513796 | Fourier transform infrared (FTIR) spectroscopy |
| Q42717469 | Identification of hepatic copper-binding proteins from tilapia by column chromatography with proteomic approaches |
| Q38123702 | Insights into metalloenzyme microenvironments: biomimetic metal complexes with a functional second coordination sphere |
| Q63442058 | Mid- and Far-Infrared Marker Bands of the Metal Coordination Sites of the Histidine Side Chains in the Protein Cu,Zn-Superoxide Dismutase |
| Q47382895 | Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior |
| Q89706496 | Nucleation and kinetics of SOD1 aggregation in human cells for ALS1 |
| Q50731388 | Redox infrared markers of the heme and axial ligands in microperoxidase: Bases for the analysis of c-type cytochromes. |
| Q37731552 | The production of nitrous oxide by the heme/nonheme diiron center of engineered myoglobins (Fe(B)Mbs) proceeds through a trans-iron-nitrosyl dimer |
Search more.