Evidence map›Paper›PMID 42084503›Full record

ArticleProtein science : a publication of the Protein Society2026

Structural analysis of Cu/Zn-superoxide dismutase linked to neurodegenerative disease by antibody-guided cryo-EM.

Yuki Shino, Norifumi Muraki, Yui Kobatake, Hiroaki Kamishina, Hirofumi Kosuge, Makoto Nakakido, Kouhei Tsumoto, Yoshiaki Furukawa

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Yuki ShinoDepartment of Chemistry, Keio University, Yokohama, Japan.
Norifumi MurakiDepartment of Chemistry, Keio University, Yokohama, Japan.
Yui KobatakeJoint Department of Veterinary Medicine, Faculty of Applied Biological Science, Gifu University, Gifu, Japan.
Hiroaki KamishinaKyoto AR Advanced Veterinary Medical Center, Kyoto, Japan.
Hirofumi KosugeDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, Japan.
Makoto NakakidoDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, Japan.
Kouhei TsumotoDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, Japan.
Yoshiaki FurukawaDepartment of Chemistry, Keio University, Yokohama, Japan.

Funding

Ministry of Education, Culture, Sports, Science and Technology 19H05765Ministry of Education, Culture, Sports, Science and Technology 22H02768Ministry of Education, Culture, Sports, Science and Technology 22K19389
6 · The paper itself

Abstract

Accumulation of misfolded proteins is a hallmark of many neurodegenerative diseases. To characterize such misfolded species in vivo, conformation-specific antibodies are widely used; however, limited knowledge of antibody-epitope interactions often hampers mechanistic insight. To address this, we determined the cryo-electron microscopy structure of the complex between a monoclonal antibody, 19A9, and Cu/Zn-superoxide dismutase (SOD1), a protein associated with canine degenerative myelopathy (DM), which is related to human amyotrophic lateral sclerosis. Biochemical analyses confirmed that 19A9 specifically recognizes monomeric SOD1, and the structure revealed binding near the interface normally used for homodimerization in native SOD1, with steric hindrance preventing interaction when the protein is in its homodimeric form. Immunofluorescence staining of spinal cord sections revealed that 19A9 stained a subset of motoneurons in DM-affected dogs, but not in asymptomatic controls. Structural characterization of the 19A9-monomeric SOD1 complex enabled us to propose that SOD1 monomers can arise in vivo under pathological conditions.

Indexed as

Antibodies, MonoclonalNeurodegenerative DiseasesSuperoxide Dismutase-1Amyotrophic Lateral SclerosisAnimalsCryoelectron MicroscopyDogsHumansModels, MolecularAntibodies, MonoclonalSuperoxide Dismutase-1amyotrophic lateral sclerosisantibodycanine degenerative myelopathycryo‐EMCu/Zn‐superoxide dismutaseprotein misfolding

Identifiers

PMID42084503
PMCPMC13142091

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.