Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.
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Ligand binding and aggregation of pathogenic SOD1Inactivation of CDK/pRb pathway normalizes survival pattern of lymphoblasts expressing the FTLD-progranulin mutation c.709-1G>AStructural and functional analysis of human SOD1 in amyotrophic lateral sclerosis.The contrasting effect of macromolecular crowding on amyloid fibril formation.Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-lifeAggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesSuperoxide dismutases and superoxide reductases.Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.Amyotrophic lateral sclerosis: update and new developments.The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.ALS-linked misfolded SOD1 species have divergent impacts on mitochondria.Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomerThe role of crowded physiological environments in prion and prion-like protein aggregationProbing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopyNon-native soluble oligomers of Cu/Zn superoxide dismutase (SOD1) contain a conformational epitope linked to cytotoxicity in amyotrophic lateral sclerosis (ALS).Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis.Misfolded SOD1 and ALS: zeroing in on mitochondria.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Computing disease-linked SOD1 mutations: deciphering protein stability and patient-phenotype relations.Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.Evolution of magnetization due to asymmetric dimerization: theoretical considerations and application to aberrant oligomers formed by apoSOD1(2SH).Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis.The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?Protein charge ladders reveal that the net charge of ALS-linked superoxide dismutase can be different in sign and magnitude from predicted values.Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.Prognostic role of "prion-like propagation" in SOD1-linked familial ALS: an alternative view.Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.Recurrent G41S mutation in Cu/Zn superoxide dismutase gene (SOD1) causing familial amyotrophic lateral sclerosis in a large Polish family.Superoxide dismutase 1 is positively selected to minimize protein aggregation in great apes.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells.Identification of a novel Cys146X mutation of SOD1 in familial amyotrophic lateral sclerosis by whole-exome sequencing.How Do Gyrating Beads Accelerate Amyloid Fibrillization?Study of mutation and misfolding of Cu-Zn SOD1 protein.Hsp90 shapes protein and RNA evolution to balance trade-offs between protein stability and aggregation.
P2860
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P2860
Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Decreased stability and increa ...... t for disease severity in ALS.
@ast
Decreased stability and increa ...... t for disease severity in ALS.
@en
Decreased stability and increa ...... t for disease severity in ALS.
@nl
type
label
Decreased stability and increa ...... t for disease severity in ALS.
@ast
Decreased stability and increa ...... t for disease severity in ALS.
@en
Decreased stability and increa ...... t for disease severity in ALS.
@nl
prefLabel
Decreased stability and increa ...... t for disease severity in ALS.
@ast
Decreased stability and increa ...... t for disease severity in ALS.
@en
Decreased stability and increa ...... t for disease severity in ALS.
@nl
P2093
P2860
P921
P356
P1476
Decreased stability and increa ...... t for disease severity in ALS.
@en
P2093
Elizabeth M Meiering
Heather A Primmer
Helen R Stubbs
Kenrick A Vassall
Lee-Ann K Briere
Ming Sze Tong
Ryan Sobering
Saipraveen Srinivasan
Sarah M Sullivan
Stanley D Dunn
P2860
P304
P356
10.1073/PNAS.0913021108
P407
P577
2011-01-21T00:00:00Z