Evidence map›Paper›PMID 40295933›Full record

ArticleClinical proteomics2025

An ALS assembly modulator signature in peripheral blood mononuclear cells: implications for ALS pathophysiology, therapeutics, and diagnostics.

Shao Feng Yu, Maya Michon, Anuradha F Lingappa, Kumar Paulvannan, Dennis Solas, Kim Staats, Justin Ichida, Debendranath Dey, Jeffrey Rosenfeld, Vishwanath R Lingappa

Abstract read
In one paragraph

Article in Clinical proteomics, 2025. 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

10 authors.

Shao Feng YuProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA.
Maya MichonProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA.
Anuradha F LingappaProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA.
Kumar PaulvannanProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA.
Dennis SolasProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA.
Kim StaatsUniversity of Southern California, Los Angeles, CA, 90033, USA.
Justin IchidaUniversity of Southern California, Los Angeles, CA, 90033, USA.
Debendranath DeyProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA.
Jeffrey RosenfeldDepartment of Neurology, Loma Linda University Health, Loma Linda, CA, 92354, USA.
Vishwanath R LingappaProsetta Biosciences, Inc., 670 5th St, San Francisco, CA, 94107, USA. vlingappa@prosetta.com.

Funding

DOD CDMRP W81XWH2210721Target ALS IL-2023-C4-L1
6 · The paper itself

Abstract

Assembly modulators are a new class of allosteric site-targeted therapeutic small molecules, some of which are effective at restoring nuclear localization of TDP-43 in ALS cellular models, and which display efficacy in a variety of ALS animal models. These compounds have been shown to bind selectively to a small subset of protein disulfide isomerase (PDI), a protein implicated in ALS pathophysiology. The targeted subset of PDI is found within a novel, transient and energy-dependent multi-protein complex that includes other important members of the ALS interactome, such as TDP-43, RanGTPase, and selective autophagy receptor p62/SQSTM1. We demonstrate here that a similar multi-protein complex drug target is present in PBMCs as isolated by energy-dependent drug resin affinity chromatography (eDRAC) and characterized by mass spectrometry and by Western blot (WB). Signature alterations in the composition of the multi-protein complex in PBMCs from ALS patients compared to PBMCs from healthy individuals were identified by WB of eDRAC bound proteins, thereby extending earlier literature suggesting PBMC dysfunction in ALS. Changes in the PBMC drug target in ALS patients compared to healthy individuals include diminished p62/SQSTM1 and appearance of a 17 kDa post-translationally modified form of RanGTPase. These changes are not readily apparent from analysis of whole cell extracts, as the individual protein components within the drug target multi-protein complex comprise only small percentages of the total of those component proteins in the extract. Furthermore, whole blood from ALS patients shows a distinctive degradation of total RanGTPase not observed in blood from healthy individuals. This degradation appears to be rescued by treatment of whole blood from ALS patients for 72 h with ALS-active assembly modulator small molecules. Our findings are consistent with the hypothesis that ALS is fundamentally a disorder of homeostasis that can be detected early, prior to disability, in blood by the methods described, and restored to the healthy state by assembly modulator drug treatment.

Identifiers

PMID40295933
PMCPMC12036218

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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.