The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited
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Structure and dynamics of copper-free SOD: The protein before binding copperStructural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALSFunctional features cause misfolding of the ALS-provoking enzyme SOD1The structure of cardiac troponin C regulatory domain with bound Cd2+ reveals a closed conformation and unique ion coordinationInsights into the role of the unusual disulfide bond in copper-zinc superoxide dismutaseCutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.High-affinity binding of the staphylococcal HarA protein to haptoglobin and hemoglobin involves a domain with an antiparallel eight-stranded beta-barrel fold.Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutantsCommon dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.Modifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosisFolding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomersComparative metal binding and genomic analysis of the avian (chicken) and mammalian metallothionein.Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability.Diffuse binding of Zn(2+) to the denatured ensemble of Cu/Zn superoxide dismutase 1.Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability.Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.Soft Vibrational Modes Predict Breaking Events during Force-Induced Protein Unfolding.FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: a large-scale thermodynamic analysis.Novel inhibitors to Taenia solium Cu/Zn superoxide dismutase identified by virtual screening
P2860
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P2860
The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited
description
1999 nî lūn-bûn
@nan
1999 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The crystal structure of the m ...... The enzyme mechanism revisited
@ast
The crystal structure of the m ...... The enzyme mechanism revisited
@en
The crystal structure of the m ...... The enzyme mechanism revisited
@nl
type
label
The crystal structure of the m ...... The enzyme mechanism revisited
@ast
The crystal structure of the m ...... The enzyme mechanism revisited
@en
The crystal structure of the m ...... The enzyme mechanism revisited
@nl
prefLabel
The crystal structure of the m ...... The enzyme mechanism revisited
@ast
The crystal structure of the m ...... The enzyme mechanism revisited
@en
The crystal structure of the m ...... The enzyme mechanism revisited
@nl
P2093
P50
P356
P1476
The crystal structure of the m ...... The enzyme mechanism revisited
@en
P2093
P304
P356
10.1006/JMBI.1999.2681
P407
P577
1999-05-07T00:00:00Z