Aggregate formation in Cu,Zn superoxide dismutase-related proteins (Q42693610)

4 November 2017

title

Aggregate formation in Cu,Zn superoxide dismutase-related proteins (English)

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4 November 2017

Marjatta Son

1

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4 November 2017

C Dyan Cloyd

2

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4 November 2017

Jeffrey D Rothstein

3

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4 November 2017

Bhagya Rajendran

4

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4 November 2017

Jeffrey L Elliott

5

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4 November 2017

language of work or name

English

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publication date

27 January 2003

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Journal of Biological Chemistry

4 November 2017

published in

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4 November 2017

volume

278

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4 November 2017

issue

16

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4 November 2017

page(s)

14331-14336

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Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

4 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation

21 January 2018

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An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria

21 January 2018

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

21 January 2018

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Current status of SOD1 mutations in familial amyotrophic lateral sclerosis

21 January 2018

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Impairment of the ubiquitin-proteasome system by protein aggregation

21 January 2018

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Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis

21 January 2018

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Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues

21 January 2018

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

21 January 2018

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Experimental models of amyotrophic lateral sclerosis

21 January 2018

1 reference

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Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain

21 January 2018

1 reference

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Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase

21 January 2018

1 reference

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Crystal structure of the copper chaperone for superoxide dismutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase

21 January 2018

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Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene

21 January 2018

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Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase

21 January 2018

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Alpha-synuclein in Lewy bodies

21 January 2018

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Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein

21 January 2018

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Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

21 January 2018

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Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures

21 January 2018

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

21 January 2018

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Zinc and copper in the pathogenesis of amyotrophic lateral sclerosis

21 January 2018

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Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice.

21 January 2018

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Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Normal prion protein has an activity like that of superoxide dismutase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Location and properties of metal-binding sites on the human prion protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Amyotrophy in prion diseases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

Prion protein binds copper within the physiological concentration range

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211698200

21 January 2018

Identifiers

DOI

10.1074/JBC.M211698200

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4 November 2017

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