Evidence map›Paper›PMID 39117623›Full record

ArticleNature communications2024

Mass spectrometry imaging of SOD1 protein-metal complexes in SOD1G93A transgenic mice implicates demetalation with pathology.

Oliver J Hale, Tyler R Wells, Richard J Mead, Helen J Cooper

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
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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

4 authors.

Oliver J HaleSchool of Biosciences, University of Birmingham, Birmingham, UK.ORCID 0000-0002-2286-5780
Tyler R WellsSheffield Institute for Translational Neuroscience, University of Sheffield, Sheffield, UK.ORCID 0000-0002-5776-7240
Richard J MeadSheffield Institute for Translational Neuroscience, University of Sheffield, Sheffield, UK. r.j.mead@sheffield.ac.uk.ORCID 0000-0002-3207-0068
Helen J CooperSchool of Biosciences, University of Birmingham, Birmingham, UK. h.j.cooper@bham.ac.uk.ORCID 0000-0003-4590-9384

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S019456/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/S002979/1
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is characterized by degeneration of motor neurons in the central nervous system (CNS). Mutations in the metalloenzyme SOD1 are associated with inherited forms of ALS and cause a toxic gain of function thought to be mediated by dimer destabilization and misfolding. SOD1 binds two Cu and two Zn ions in its homodimeric form. We have applied native ambient mass spectrometry imaging to visualize the spatial distributions of intact metal-bound SOD1

Indexed as

Amyotrophic Lateral SclerosisBrainMass SpectrometryMice, TransgenicSpinal CordSuperoxide Dismutase-1AnimalsCopperDisease Models, AnimalHumansMaleMiceMutationProtein MultimerizationProtein Processing, Post-TranslationalSuperoxide DismutaseCopperSOD1 protein, humanSod1 protein, mouseSuperoxide DismutaseSuperoxide Dismutase-1Zinc

Identifiers

PMID39117623
PMCPMC11310518

What OpenQuestion holds

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Registered trials

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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.