Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu,Zn superoxide dismutases.
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Superoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosisStructural 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.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric speciesNonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisDecreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Heterogeneous side chain conformation highlights a network of interactions implicated in hysteresis of the knotted protein, minimal tied trefoil.Superoxide dismutase as a novel macromolecular nitric oxide carrier: preparation and characterization.The rough energy landscape of superfolder GFP is linked to the chromophoreGlutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis.Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1Effect of Oxidative Damage on the Stability and Dimerization of Superoxide Dismutase 1.Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants.Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.Application of high-throughput isothermal denaturation to assess protein stability and screen for ligands.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Calorimetric analysis of thermodynamic stability and aggregation for apo and holo amyotrophic lateral sclerosis-associated Gly-93 mutants of superoxide dismutase.
P2860
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P2860
Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu,Zn superoxide dismutases.
description
2005 nî lūn-bûn
@nan
2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@en
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@nl
type
label
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@en
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@nl
prefLabel
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@en
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@nl
P2093
P1476
Mechanism and thermodynamics o ...... t Cu,Zn superoxide dismutases.
@en
P2093
Avijit Chakrabarrty
Elizabeth M Meiering
James R Lepock
Jessica A O Rumfeldt
Peter B Stathopulos
P304
P356
10.1016/J.JMB.2005.10.042
P407
P577
2005-11-08T00:00:00Z