Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
about
Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosisDisulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model miceChemical approaches to detect and analyze protein sulfenic acidsTop-down proteomics in health and disease: challenges and opportunitiesMolecular 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 ALSStructural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsFunctional features cause misfolding of the ALS-provoking enzyme SOD1Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93ACharacterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80RStructures of mouse SOD1 and human/mouse SOD1 chimerasStructural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzymeStructural Consequences of Cysteinylation of Cu/Zn-Superoxide DismutaseThree-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNaseEdge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphataseThe rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosisBinding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current statusParsing 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.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensityAmyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.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 speciesA prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformersDNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrilsThe effect of red pigment on the amyloidization of yeast proteins.Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Copper-based pulsed dipolar ESR spectroscopy as a probe of protein conformation linked to disease states.Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.Aggregation modulating elements in mutant human superoxide dismutase 1.
P2860
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P2860
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@ast
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@en
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@nl
type
label
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@ast
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@en
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@nl
prefLabel
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@ast
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@en
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@nl
P2093
P50
P356
P1476
Amyloid-like filaments and wat ...... roteins linked to familial ALS
@en
P2093
Alexander B Taylor
Joan Selverstone Valentine
Jorge A Rodriguez
Lawrence J Hayward
P John Hart
Peter A Doucette
Richard Strange
S Samar Hasnain
P356
10.1038/NSB935
P577
2003-06-01T00:00:00Z