(Q46807674)

25 December 2017

title

Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form (English)

1 reference

25 December 2017

1 reference

0 references

1

Lucia Banci

1 reference

25 December 2017

2

Ivano Bertini

1 reference

25 December 2017

3

Francesca Cantini

1 reference

25 December 2017

Elena Gaggelli

series ordinal

5

object named as

Elena Gaggelli

1 reference

25 December 2017

author name string

Nicola D'Amelio

series ordinal

4

1 reference

25 December 2017

language of work or name

English

0 references

publication date

14 November 2005

1 reference

25 December 2017

Journal of Biological Chemistry

published in

1 reference

25 December 2017

volume

281

1 reference

25 December 2017

issue

4

1 reference

25 December 2017

page(s)

2333-2337

1 reference

25 December 2017

Formation and transfer of disulphide bonds in living cells

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

The copper chaperone for superoxide dismutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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.M506497200

Amyotrophic lateral sclerosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Structure and dynamics of copper-free SOD: The protein before binding copper

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Torsion angle dynamics for NMR structure calculation with the new program DYANA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

A structure-based mechanism for copper-zinc superoxide dismutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506497200

21 January 2018

Identifiers

DOI

10.1074/JBC.M506497200

1 reference

25 December 2017

1 reference

25 December 2017