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

The metal cofactor zinc and interacting membranes modulate SOD1 conformation-aggregation landscape in an in vitro ALS model.

eLife - 7 Apr 2021

Sannigrahi Achinta, Chowdhury Sourav, Das Bidisha, Banerjee Amrita, Halder Animesh, Kumar Amaresh, Saleem Mohammed, Naganathan Athi N, Karmakar Sanat, Chattopadhyay Krishnananda

Abstract excerpt

Aggregation of Cu-Zn superoxide dismutase (SOD1) is implicated in the motor neuron disease, amyotrophic lateral sclerosis (ALS). Although more than 140 disease mutations of SOD1 are available, their stability or aggregation behaviors in membrane environment are not correlated with disease pathophysiology. Here, we use multiple mutational variants of SOD1 to show that the absence of Zn, and not Cu, significantly...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyotrophic Lateral Sclerosis
Share to Copper

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Aggregates

Share to Protein Aggregation, Pathological

Share to Protein Folding

Share to Structure-Activity Relationship

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 33825682
DOI: 10.7554/eLife.61453
PMCID: PMC8087447

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The metal cofactor zinc and interacting membranes modulate SOD1 conformation-aggregation landscape in an in vitro ALS model.PMID 33825682Read ↗

The metal cofactor zinc and interacting membranes modulate SOD1 conformation-aggregation landscape in an <i>in vitro</i> ALS ModelSemantic 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 ↗

The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-implications for the toxic gain of function observed in ALS.Semantic proximity Read ↗

Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.Semantic proximity Read ↗

Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

An Allosteric Pathway in Copper, Zinc Superoxide Dismutase Unravels the Molecular Mechanism of the G93A Amyotrophic Lateral Sclerosis-Linked Mutation.Semantic proximity Read ↗

Insight Into Factors Influencing the Aggregation Process in Wild-Type and P66R Mutant SOD1: Computational and Spectroscopic Approaches.Semantic proximity Read ↗

Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Semantic proximity Read ↗

The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-Implications for the toxic gain of function observed in ALSSemantic proximity Read ↗

Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Semantic proximity Read ↗

Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.Semantic proximity Read ↗

How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?Semantic proximity Read ↗

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