(Q46566731)

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Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase

scientific article published on 19 February 2002

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase (English)

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

amyotrophic lateral sclerosis

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Ashutosh Tiwari

5

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

6

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Robert H Brown

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

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Jorge A Rodriguez

1

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Europe PubMed Central

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23 December 2017

http://europepmc.org/abstract/MED/11854285

Joan S Valentine

2

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

Daryl K Eggers

3

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Europe PubMed Central

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23 December 2017

http://europepmc.org/abstract/MED/11854285

James A Roe

4

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

Lawrence J Hayward

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23 December 2017

http://europepmc.org/abstract/MED/11854285

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publication date

19 February 2002

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Europe PubMed Central

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23 December 2017

http://europepmc.org/abstract/MED/11854285

Journal of Biological Chemistry

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23 December 2017

http://europepmc.org/abstract/MED/11854285

277

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PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

18

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

15932-15937

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

Differential scanning calorimetry of Cu,Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Structure and mechanism of copper, zinc superoxide dismutase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

How to measure and predict the molar absorption coefficient of a protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

High-resolution differential scanning calorimetric analysis of the subunits of Escherichia coli aspartate transcarbamoylase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Study of strong to ultratight protein interactions using differential scanning calorimetry

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M112088200

21 January 2018

Identifiers

10.1074/JBC.M112088200

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/11854285

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