sameAs
SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationAn electron-transfer path through an extended disulfide relay system: the case of the redox protein ALRMolecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein importStructural interplay between calcium(II) and copper(II) binding to S100A13 proteinMIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondriaAn NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes proteinA hint for the function of human Sco1 from different structuresAn idea whose time has comeNMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteriaThe solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerizationStructure and dynamics of copper-free SOD: The protein before binding copperSolution structure of CopC: a cupredoxin-like protein involved in copper homeostasisA new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)Solution structure and characterization of the heme chaperone CcmEA redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sitesHuman Sco1 functional studies and pathological implications of the P174L mutantA strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas SyringaeA core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilisSolution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein foldingThe evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transductionStructural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilisSolution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assemblySolution structure of apo CopZ from Bacillus subtilis: further analysis of the changes associated with the presence of copperThe characterization and role of zinc binding in yeast Cox4NMR structural analysis of cadmium sensing by winged helix repressor CmtRMatrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitorsA structural characterization of human SCO2Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinaseA structural-dynamical characterization of human Cox17Metal Binding Domains 3 and 4 of the Wilson Disease Protein: Solution Structure and Interaction with the Copper(I) Chaperone HAH1 † ‡Mechanism of CuA assemblyThe copper-responsive repressor CopR of Lactococcus lactis is a 'winged helix' proteinSolution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidisStructural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsCopper(I)-mediated protein-protein interactions result from suboptimal interaction surfacesNMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteinsThe Binding Mode of ATP Revealed by the Solution Structure of the N-domain of Human ATP7ASco proteins are involved in electron transfer processesMolecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR
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