(Q46654946)

24 December 2017

title

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

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24 December 2017

author

Paola Turano

7

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24 December 2017

Lucia Banci

1

Lucia Banci

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24 December 2017

2

Ivano Bertini

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24 December 2017

3

Nicola D'Amelio

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24 December 2017

Elisa Libralesso

5

Elisa Libralesso

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24 December 2017

Joan S. Valentine

8

Joan Selverstone Valentine

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24 December 2017

Elena Gaggelli

4

Elena Gaggelli

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24 December 2017

author name string

Irena Matecko

6

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24 December 2017

language of work or name

English

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publication date

16 August 2005

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24 December 2017

Journal of Biological Chemistry

published in

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24 December 2017

volume

280

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24 December 2017

issue

43

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24 December 2017

page(s)

35815-35821

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24 December 2017

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

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Rings, chains and ladders: ubiquitin goes to work in the neuron.

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

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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.

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High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation

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Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants.

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

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Misfolded CuZnSOD and amyotrophic lateral sclerosis

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

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Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation

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

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

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Synthesis and characterization of a monomeric mutant Cu/Zn superoxide dismutase with partially reconstituted enzymic activity

21 January 2018

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Faster superoxide dismutase mutants designed by enhancing electrostatic guidance

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

21 January 2018

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

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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Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis

21 January 2018

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

21 January 2018

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Intrinsically unstructured proteins and their functions

21 January 2018

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Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase

21 January 2018

1 reference

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Backbone Dynamics of Human Cu,Zn Superoxide Dismutase and of Its Monomeric F50E/G51E/E133Q Mutant: The Influence of Dimerization on Mobility and Function†

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M506637200

1 reference

24 December 2017

1 reference

24 December 2017