Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.
about
Protein folding: then and nowMolecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutaseSuperoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosisGlobal structural motions from the strain of a single hydrogen bondThe complex molecular biology of amyotrophic lateral sclerosis (ALS)The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthaseStructural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsA prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformersDimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cellsConformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases.Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisCu,Zn-superoxide dismutase without Zn is folded but catalytically inactive.The structural biochemistry of the superoxide dismutases.Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria.SOD1 exhibits allosteric frustration to facilitate metal binding affinity.Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation.Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation.Mutant copper-zinc superoxide dismutase associated with amyotrophic lateral sclerosis binds to adenine/uridine-rich stability elements in the vascular endothelial growth factor 3'-untranslated region.Modifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosisStructural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V.SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease.Computational approaches to understanding protein aggregation in neurodegeneration.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Misfolded SOD1 and ALS: zeroing in on mitochondria.A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability.A mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human-A Discrete Molecular Dynamics Study.Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.A theoretical study on Zn binding loop mutants instigating destabilization and metal binding loss in human SOD1 protein.Study of mutation and misfolding of Cu-Zn SOD1 protein.A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.
P2860
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P2860
Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Common dynamical signatures of ...... superoxide dismutase mutants.
@ast
Common dynamical signatures of ...... superoxide dismutase mutants.
@en
Common dynamical signatures of ...... superoxide dismutase mutants.
@nl
type
label
Common dynamical signatures of ...... superoxide dismutase mutants.
@ast
Common dynamical signatures of ...... superoxide dismutase mutants.
@en
Common dynamical signatures of ...... superoxide dismutase mutants.
@nl
prefLabel
Common dynamical signatures of ...... superoxide dismutase mutants.
@ast
Common dynamical signatures of ...... superoxide dismutase mutants.
@en
Common dynamical signatures of ...... superoxide dismutase mutants.
@nl
P2860
P356
P1476
Common dynamical signatures of ...... superoxide dismutase mutants.
@en
P2093
Sagar D Khare
P2860
P304
P356
10.1073/PNAS.0511266103
P407
P577
2006-02-17T00:00:00Z