Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS (Q27680903)

2

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Elizabeth L Guenther

3

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Lisa M Johnson

4

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Duane D Winkler

5

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Ahmad Galaleldeen

6

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Michael R Sawaya

7

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P John Hart

8

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David S Eisenberg

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

9

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language of work or name

English

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publication date

7 January 2014

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published in

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volume

111

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page(s)

197-201

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issue

1

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cites work

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Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis

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Molecular basis for insulin fibril assembly

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury

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SOD1 aggregation and ALS: role of metallation states and disulfide status

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Extracellular aggregated Cu/Zn superoxide dismutase activates microglia to give a cytotoxic phenotype.

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IL-17A is increased in the serum and in spinal cord CD8 and mast cells of ALS patients

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An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1

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Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients

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Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species

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Initiation and elongation in fibrillation of ALS-linked superoxide dismutase

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Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria

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Molecular biology of amyotrophic lateral sclerosis: insights from genetics

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Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature

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Expression of wild-type human superoxide dismutase-1 in mice causes amyotrophic lateral sclerosis.

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Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site

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Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability

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Clinical and functional investigation of 10 missense mutations and a novel frameshift insertion mutation of the gene for copper-zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/24344300

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.1320786110

1 reference

2666061

ADS bibcode

2014PNAS..111..197I

0 references

2666061

1 reference

1 reference

1 reference