Structural Analysis of SOD1 Fibrils with Mass Spectrometry, Limited Proteolysis, and Atomic Force Microscopy (AFM).

Bon-Kyung Koo, Julian Whitelegge

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact, top 52% of its field

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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Bon-Kyung KooThe Department of Chemistry and Biochemistry, School of Physical Sciences, University of California, Los Angeles, USA.

Julian WhiteleggeThe Pasarow Mass Spectrometry Laboratory, The Jane and Terry Semel Institute for Neuroscience and Human Behavior, David Geffen School of Medicine, University of California, Los Angeles, USA. jpw@chem.ucla.edu.

University of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This protocol describes a method to purify SOD1 in Saccharomyces cerevisiae to characterize using ICP-MS and AFM, to agitate and fibrillate for aggregation of SOD1. The human SOD1 (hSOD1) is a 32-kDa homodimer, with one copper- and one zinc-binding site per 153-amino acid subunit. Misfolded protein aggregates are often correlated with diseases known as amyloidosis, including ALS, Alzheimer's, Parkinson's, and prion disease (Valentine and Hart, Proc Natl Acad Sci USA 100: 3617-3622, 2003; Tanzi and Bertram, Cell 120: 545-555, 2005; Soto and Pritzkow, Nat Neurosci 21:1332-1340, 2018; Sarafian et al., J Neurosci Res 95:1871-1887, 2017). Proteinaceous aggregates containing hSOD1 have frequently been found in the spinal cords of ALS patients.

Indexed as

Amyotrophic Lateral SclerosisHumansMass SpectrometryMicroscopy, Atomic ForceMutationProtein AggregatesProteolysisSuperoxide DismutaseSuperoxide Dismutase-1Protein AggregatesSOD1 protein, humanSuperoxide DismutaseSuperoxide Dismutase-1AFMAggregationALS (Amyotrophic lateral sclerosis)Cu/Zn SOD1 (Superoxide dismutase1)FibrillationICP-MS

Identifiers

PMID36310221

DOI10.1016/j.bpj.2016.12.004

OpenAlexW4307642726

What OpenQuestion holds

Textmetadata

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.