SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. (Q48918632)

16 February 2018

title

SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. (English)

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16 February 2018

amyotrophic lateral sclerosis

main subject

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author

Niels Christian Danbolt

3

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16 February 2018

author name string

D Trotti

1

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16 February 2018

A Rolfs

2

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16 February 2018

R H Brown

4

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16 February 2018

M A Hediger

5

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16 February 2018

language of work or name

English

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publication date

1 May 1999

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16 February 2018

published in

Nature Neuroscience

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16 February 2018

volume

2

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16 February 2018

page(s)

427-433

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16 February 2018

issue

5

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16 February 2018

https://scigraph.springernature.com/pub.10.1038/8091

exact match

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cites work

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Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superox

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Elevated "hydroxyl radical" generation in vivo in an animal model of amyotrophic lateral sclerosis.

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Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity

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Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function.

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A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value.

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Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis

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A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide

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Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate

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Brain glutamate transporter proteins form homomultimers.

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The number of glutamate transporter subtype molecules at glutamatergic synapses: chemical and stereological quantification in young adult rat brain

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Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis

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Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis

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Glutamate transporter gene expression in amyotrophic lateral sclerosis motor cortex

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Mutations in the glutamate transporter EAAT2 gene do not cause abnormal EAAT2 transcripts in amyotrophic lateral sclerosis

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Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis

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Glutamate uptake is decreased tardively in the spinal cord of FALS mice.

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ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions.

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Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients

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Peroxynitrite inhibits glutamate transporter subtypes.

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Differential modulation of the uptake currents by redox interconversion of cysteine residues in the human neuronal glutamate transporter EAAC1.

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Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury

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A potent superoxide dismutase mimic: manganese beta-octabromo-meso-tetrakis-(N-methylpyridinium-4-yl) porphyrin

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Riluzole preserves motor function in a transgenic model of familial amyotrophic lateral sclerosis.

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Identifiers

DOI

10.1038/8091

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16 February 2018

release_h4ui4znrhffplealo5ue22hcw4

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/h4ui4znrhffplealo5ue22hcw4

24 November 2022

mapped directly with Wikidata item

PubMed ID

10321246

1 reference

16 February 2018