Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.
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Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilisPolymer uncrossing and knotting in protein folding, and their role in minimal folding pathwaysFunctional features cause misfolding of the ALS-provoking enzyme SOD1Ligand binding and aggregation of pathogenic SOD1Copper delivery to the CNS by CuATSM effectively treats motor neuron disease in SOD(G93A) mice co-expressing the Copper-Chaperone-for-SODCutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric speciesInsights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability.Identification of human monoclonal antibodies specific for human SOD1 recognizing distinct epitopes and forms of SOD1.Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.Measuring copper and zinc superoxide dismutase from spinal cord tissue using electrospray mass spectrometry.The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation.Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomerRegulation of superoxide dismutase genes: implications in disease.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis.Diffuse binding of Zn(2+) to the denatured ensemble of Cu/Zn superoxide dismutase 1.The role of solvent exclusion in the interaction between D124 and the metal site in SOD1: implications for ALS.Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants.The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study.
P2860
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P2860
Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@ast
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@en
type
label
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@ast
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@en
prefLabel
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@ast
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@en
P2860
P1476
Zinc binding modulates the ent ...... an Cu,Zn superoxide dismutase.
@en
P2093
C Robert Matthews
Jill A Zitzewitz
P2860
P304
P356
10.1016/J.JMB.2008.09.045
P407
P577
2008-09-26T00:00:00Z