ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mapping.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 78 citations in OpenAlex.
- Randomized, double-blind, placebo-controlled trial of arimoclomol in rapidly progressiveNeurology · 2018Trial
- Efficient induction of motor neuron disease in transgenic G93A SOD1 mice by prion-like seeding.Prion · 2026Article
- Seeds from ALS patients homozygous for the SOD1 D90A mutation transmit two types of SOD1 aggregation and motor neuron disease.Acta neuropathologica · 2026Article
- Fast and slow strains of misfolded mutant superoxide dismutase 1 in familial amyotrophic lateral sclerosis.Acta neuropathologica communications · 2026Article
- N-Truncated Superoxide Dismutase-1 in Cerebrospinal Fluid Is Folded and Active.Journal of neurochemistry · 2026Article
- Modifications of NU-9, a potent protein aggregation inhibitor. Properties and activity in a cellular model of amyotrophic lateral sclerosis.Bioorganic chemistry · 2025Article
- Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N.EMBO reports · 2025Article
- Diverse effects of coexpression of human SOD1 variants on motor neuron disease.Human molecular genetics · 2025Article
- SOD1 Protein Content in Human Central Nervous System and Peripheral Tissues.Journal of neurochemistry · 2025Article
- Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.Science advances · 2024Article
- Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants.Nature chemical biology · 2024Article
- Amyloidogenic regions in beta-strands II and III modulate the aggregation and toxicity of SOD1 in living cells.Open biology · 2024Article
- MS785-MS27 Reactive Misfolded/Non-Native Zn-Deficient SOD1 Species Exhibit Cytotoxicity and Adopt Heterozygous Conformations in Motor Neurons.International journal of molecular sciences · 2024Article
- Mutant SOD1 aggregates formed in vitro and in cultured cells are polymorphic and differ from those arising in the CNS.Journal of neurochemistry · 2023Article
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
- Alteration of Mitochondrial Integrity as Upstream Event in the Pathophysiology of SOD1-ALS.Cells · 2022Article
- Prionoids in amyotrophic lateral sclerosis.Brain communications · 2022Review
- Phenotypic diversity in ALS and the role of poly-conformational protein misfolding.Acta neuropathologica · 2021Review
- Peripheral administration of SOD1 aggregates does not transmit pathogenic aggregation to the CNS of SOD1 transgenic mice.Acta neuropathologica communications · 2021Article
- Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis.The EMBO journal · 2021Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite considerable progress in uncovering the molecular details of protein aggregation in vitro, the cause and mechanism of protein-aggregation disease remain poorly understood. One reason is that the amount of pathological aggregates in neural tissue is exceedingly low, precluding examination by conventional approaches. We present here a method for determination of the structure and quantity of aggregates in small tissue samples, circumventing the above problem. The method is based on binary epitope mapping using anti-peptide antibodies. We assessed the usefulness and versatility of the method in mice modeling the neurodegenerative disease amyotrophic lateral sclerosis, which accumulate intracellular aggregates of superoxide dismutase-1. Two strains of aggregates were identified with different structural architectures, molecular properties, and growth kinetics. Both were different from superoxide dismutase-1 aggregates generated in vitro under a variety of conditions. The strains, which seem kinetically under fragmentation control, are associated with different disease progressions, complying with and adding detail to the growing evidence that seeding, infectivity, and strain dependence are unifying principles of neurodegenerative disease.
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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.