Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form (Q46807674)

25 December 2017

title

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

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1

Lucia Banci

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2

Ivano Bertini

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3

Francesca Cantini

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Elena Gaggelli

series ordinal

5

object named as

Elena Gaggelli

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author name string

Nicola D'Amelio

series ordinal

4

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language of work or name

English

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publication date

14 November 2005

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Journal of Biological Chemistry

published in

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volume

281

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page(s)

2333-2337

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issue

4

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Formation and transfer of disulphide bonds in living cells

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

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Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

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

21 January 2018

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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.

21 January 2018

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

21 January 2018

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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

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Amyotrophic lateral sclerosis

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

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

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

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

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A structure-based mechanism for copper-zinc superoxide dismutase

21 January 2018

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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

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M506497200

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25 December 2017

PubMed ID

16291742

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25 December 2017