Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. - Wikidata - wikimedia - TriplyDB

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

http://www.wikidata.org/entity/Q36978868

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Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis In Vivo imaging reveals distinct inflammatory activity of CNS microglia versus PNS macrophages in a mouse model for ALS Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase The complex molecular biology of amyotrophic lateral sclerosis (ALS)Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis Solid-state NMR studies of metal-free SOD1 fibrillar structures.Cutting 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 superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols.Amyloidogenic 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 methods Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Cytotoxicity of superoxide dismutase 1 in cultured cells is linked to Zn2+ chelation.The contrasting effect of macromolecular crowding on amyloid fibril formation.An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1 IL-17A is increased in the serum and in spinal cord CD8 and mast cells of ALS patients.Aggregation modulating elements in mutant human superoxide dismutase 1.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes Zinc: indications in brain disorders.Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Cupric ions induce the oxidation and trigger the aggregation of human superoxide dismutase 1 Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis.The structural biochemistry of the superoxide dismutases.Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation Superoxide dismutases and superoxide reductases.Arresting amyloid with coulomb's law: acetylation of ALS-linked SOD1 by aspirin impedes aggregation Fibril formation of the rabbit/human/bovine prion proteins How does domain replacement affect fibril formation of the rabbit/human prion proteins

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P2860

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

http://www.wikidata.org/entity/Q36978868

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

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type

label

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

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Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

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PNAS.0807058105

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

@en

P2093

Armando Durazo

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Cynthia D Strong

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Edith B Gralla

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Joan Selverstone Valentine

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Madhuri Chattopadhyay

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Se Hui Sohn

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P2860

Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein

Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice

ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization

Unraveling the mechanisms involved in motor neuron degeneration in ALS

Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.

Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria

Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.

Pathological characterization of astrocytic hyaline inclusions in familial amyotrophic lateral sclerosis.

Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS

Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models.

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10.1073/PNAS.0807058105

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48

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105

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Julian P Whitelegge

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2008-11-20T00:00:00Z

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23486920

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19022905

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identical protein binding

Superoxide dismutase 1

amyotrophic lateral sclerosis

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2585484

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