Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.
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SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationMolecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutaseStructural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALSEmerging mechanisms of molecular pathology in ALSParsing Disease-relevant Protein Modifications from Epiphenomena: Perspective on the Structural Basis of SOD1-Mediated ALS.Intermolecular transmission of superoxide dismutase 1 misfolding in living cells.Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsMetal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric speciesDNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Direct observation of defects and increased ion permeability of a membrane induced by structurally disordered Cu/Zn-superoxide dismutase aggregates.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.Heat shock factor 1 over-expression protects against exposure of hydrophobic residues on mutant SOD1 and early mortality in a mouse model of amyotrophic lateral sclerosis.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.The Copper Metabolism MURR1 domain protein 1 (COMMD1) modulates the aggregation of misfolded protein species in a client-specific mannerBiochemical properties and in vivo effects of the SOD1 zinc-binding site mutant (H80G)Metal-deficient SOD1 in amyotrophic lateral sclerosis.Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models.Mutant SOD1 forms ion channel: implications for ALS pathophysiology.BODIPY-Based Fluorescent Probes for Sensing Protein Surface-Hydrophobicity.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria.A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivoMutant 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.ALS mutant SOD1 interacts with G3BP1 and affects stress granule dynamicsA common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosisComputational approaches to understanding protein aggregation in neurodegeneration.An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis.Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis.Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.A cysteine residue affects the conformational state and neuronal toxicity of mutant SOD1 in mice: relevance to the pathogenesis of ALS.Motoneuron Disease: Basic Science.Aberrant molecular properties shared by familial Parkinson's disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1.Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity.Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1.
P2860
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P2860
Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Aberrantly increased hydrophob ...... amyotrophic lateral sclerosis.
@en
type
label
Aberrantly increased hydrophob ...... amyotrophic lateral sclerosis.
@en
prefLabel
Aberrantly increased hydrophob ...... amyotrophic lateral sclerosis.
@en
P2860
P356
P1476
Aberrantly increased hydrophob ...... amyotrophic lateral sclerosis
@en
P2093
Lawrence J Hayward
Zuoshang Xu
P2860
P304
29771-29779
P356
10.1074/JBC.M504039200
P407
P577
2005-06-15T00:00:00Z