ArticleeLife2015
Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Bromodomain dimers: A case study of BRD4 and family-wide AlphaFold predictions.Structural dynamics (Melville, N.Y.) · 2026Article
- Nose-to-brain delivery of a SOD1-stabilizing small molecule ameliorates pathology in an ALS mouse model.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026Article
- An optimizedJournal of biomolecular NMR · 2025Article
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- N-terminal acetylation of superoxide dismutase 1 accelerates amyloid formation without general destabilization of the apo state.Protein science : a publication of the Protein Society · 2025Article
- Amyloid Forming Human Lysozyme Intermediates are Stabilized by Non-Native Amide-π Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Biophysical and spectroscopical insights into structural modulation of species in the aggregation pathway of superoxide dismutase 1.Communications chemistry · 2025Article
- Discovery of Novel Inhibitors against ALS-Related SOD1(A4V) Aggregation through the Screening of a Chemical Library Using Differential Scanning Fluorimetry (DSF).Pharmaceuticals (Basel, Switzerland) · 2024Article
- Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants.Nature chemical biology · 2024Article
- Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.Nature communications · 2024Article
- Protein aggregation and therapeutic strategies in SOD1- and TDP-43- linked ALS.Frontiers in molecular biosciences · 2024Review
- Extreme diversity of 12 cations in folding ALS-linked hSOD1 unveils novel hSOD1-dependent mechanisms for FeScientific reports · 2023Article
- Probing excited stateMethods (San Diego, Calif.) · 2023Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Probing Oxidant Effects on Superoxide Dismutase 1 Oligomeric States in Live Cells Using Single-Molecule Fluorescence Anisotropy.Chemical & biomedical imaging · 2023Article
- A Zn-dependent structural transition of SOD1 modulates its ability to undergo phase separation.The EMBO journal · 2023Article
- SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage.Scientific reports · 2022Article
- A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy.Journal of magnetic resonance open · 2022Article
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7 authors.
Funding
Abstract
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease involving cytotoxic conformations of Cu, Zn superoxide dismutase (SOD1). A major challenge in understanding ALS disease pathology has been the identification and atomic-level characterization of these conformers. Here, we use a combination of NMR methods to detect four distinct sparsely populated and transiently formed thermally accessible conformers in equilibrium with the native state of immature SOD1 (apoSOD1(2SH)). Structural models of two of these establish that they possess features present in the mature dimeric protein. In contrast, the other two are non-native oligomers in which the native dimer interface and the electrostatic loop mediate the formation of aberrant intermolecular interactions. Our results show that apoSOD1(2SH) has a rugged free energy landscape that codes for distinct kinetic pathways leading to either maturation or non-native association and provide a starting point for a detailed atomic-level understanding of the mechanisms of SOD1 oligomerization.
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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.