Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R.

Biochemistry - 13 Jul 2010

Seetharaman Sai V, Winkler Duane D, Taylor Alexander B, Cao Xiaohang, Whitson Lisa J, Doucette Peter A, Valentine Joan S, Schirf Virgil, Demeler Borries, Carroll Mark C, Culotta Valeria C, Hart P John

Abstract excerpt

Mutations in human copper-zinc superoxide dismutase (SOD1) cause an inherited form of the fatal neurodegenerative disease amyotrophic lateral sclerosis (ALS). Here, we present structures of the pathogenic SOD1 variants D124V and H80R, both of which demonstrate compromised zinc-binding sites. The disruption of the zinc-binding sites in H80R SOD1 leads to conformational changes in loop elements, permitting...

Topics

Amyotrophic Lateral Sclerosis
Animals
Binding Sites
Copper
Crystallography, X-Ray
Humans
Mice
Mice, Transgenic
Molecular Chaperones
Mutation
Superoxide Dismutase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

X-Ray Diffraction

X-Rays

Zinc

Source

Open in PubMed Open full text

Identifiers

PMID: 20515040
DOI: 10.1021/bi100314n
PMCID: PMC3037816

Genes

SOD1
CCS

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R.PMID 20515040Read ↗

Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes.Semantic proximity Read ↗

Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs).Semantic proximity Read ↗

Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis.Semantic proximity Read ↗

ALS-causing SOD1 mutations promote production of copper-deficient misfolded species.Semantic proximity Read ↗

Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.Semantic proximity Read ↗

Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Semantic proximity Read ↗

Pathogenic superoxide dismutase structure, folding, aggregation and turnover.Semantic proximity Read ↗

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

Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.Semantic proximity Read ↗

Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.Semantic proximity Read ↗

Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.