SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization (Q21090100)

mutation

1 reference

superoxide dismutase

1 reference

6

Joan Selverstone Valentine

author given names

Joan Selverstone

author last names

Valentine

1 reference

8 August 2022

1

Lucia Banci

Lucia

Banci

1 reference

8 August 2022

2

Ivano Bertini

Ivano

Bertini

1 reference

8 August 2022

5

Manuele Martinelli

Manuele

Martinelli

1 reference

8 August 2022

4

Stefania

Girotto

Stefania Girotto

1 reference

8 August 2022

7

Miguela

Vieru

Miguela Vieru

1 reference

8 August 2022

3

Mirela

Boca

Mirela Boca

1 reference

Creative Commons Attribution 4.0 International

8 August 2022

language of work or name

English

0 references

publication date

2008

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published in

PLOS One

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volume

3

0 references

issue

2

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page(s)

e1677

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copyright license

start time

27 February 2008

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

0 references

cites work

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Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?

19 March 2017

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

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Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria

6 April 2017

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

7 April 2017

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Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.

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12 September 2017

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Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants

12 September 2017

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12 September 2017

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

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Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state

12 September 2017

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Toxic proteins in neurodegenerative disease

12 September 2017

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Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1

12 September 2017

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Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions

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Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.

30 May 2018

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Crossref

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001677

Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions

21 January 2018

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Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria.

21 January 2018

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A characterization of copper/zinc superoxide dismutase mutants at position 124. Zinc-deficient proteins

21 January 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/18301754

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status

1 reference

https://pubmed.ncbi.nlm.nih.gov/18301754

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PONE.0001677

1 reference

ADS bibcode

2008PLoSO...3.1677B

0 references

1 reference

1 reference

1 reference