ArticleScientific reports2017
A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026Review
- Recent Development on Copper-Sensor and its Biological Applications: A Review.Journal of fluorescence · 2025Review
- Downregulation of Parahippocampal Copper Chaperone for Superoxide Dismutase in Alzheimer's Disease.Brain sciences · 2025Article
- Pathogenic RBiochemistry · 2024Article
- A comprehensive assessment of selective amino acidJournal of biomolecular NMR · 2024Article
- Controlling the incorporation of fluorinated amino acids in human cells and its structural impact.Protein science : a publication of the Protein Society · 2024Article
- Copper toxicity and deficiency: the vicious cycle at the core of protein aggregation in ALS.Frontiers in molecular neuroscience · 2024Review
- Review
- Direct Expression of Fluorinated Proteins in Human Cells forJournal of the American Chemical Society · 2023Article
- Recent Advances in Copper-Based Organic Complexes and Nanoparticles for Tumor Theranostics.Molecules (Basel, Switzerland) · 2022Review
- Altered SOD1 maturation and post-translational modification in amyotrophic lateral sclerosis spinal cord.Brain : a journal of neurology · 2022Article
- A pathological link between dysregulated copper binding in Cu/Zn-superoxide dismutase and amyotrophic lateral sclerosis.Journal of clinical biochemistry and nutrition · 2022Article
- Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR.Chemical reviews · 2022Review
- Determination of intracellular protein-ligand binding affinity by competition binding in-cell NMR.Acta crystallographica. Section D, Structural biology · 2021Article
- Free energy calculations of ALS-causing SOD1 mutants reveal common perturbations to stability and dynamics along the maturation pathway.Protein science : a publication of the Protein Society · 2021Article
- Superoxide Dismutase 1 in Health and Disease: How a Frontline Antioxidant Becomes Neurotoxic.Angewandte Chemie (International ed. in English) · 2021Review
- Molecular and pharmacological chaperones for SOD1.Biochemical Society transactions · 2020Review
- Real-Time Quantitative In-Cell NMR: Ligand Binding and Protein Oxidation Monitored in Human Cells Using Multivariate Curve Resolution.Analytical chemistry · 2020Article
- Copper Sources for Sod1 Activation.Antioxidants (Basel, Switzerland) · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Superoxide dismutase 1 (SOD1) is an important metalloprotein for cellular oxidative stress defence, that is mutated in familiar variants of Amyotrophic Lateral Sclerosis (fALS). Some mutations destabilize the apo protein, leading to the formation of misfolded, toxic species. The Copper Chaperone for SOD1 (CCS) transiently interacts with SOD1 and promotes its correct maturation by transferring copper and catalyzing disulfide bond formation. By in vitro and in-cell NMR, we investigated the role of the SOD-like domain of CCS (CCS-D2). We showed that CCS-D2 forms a stable complex with zinc-bound SOD1 in human cells, that has a twofold stabilizing effect: it both prevents the accumulation of unstructured mutant SOD1 and promotes zinc binding. We further showed that CCS-D2 interacts with apo-SOD1 in vitro, suggesting that in cells CCS stabilizes mutant apo-SOD1 prior to zinc binding. Such molecular chaperone function of CCS-D2 is novel and its implications in SOD-linked fALS deserve further investigation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.