Evidence map›Paper›PMID 41223590›Full record

ArticleBioorganic chemistry2025

Modifications of NU-9, a potent protein aggregation inhibitor. Properties and activity in a cellular model of amyotrophic lateral sclerosis.

Mohamed F Elmansy, Pedro Soares, Jose Ricardo D Dos Remedios, Raghad Nowar, Susan G Fox, Anan Yu, William L Klein, Richard I Morimoto, Richard B Silverman

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioorganic chemistry, 2025. 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
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.

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

9 authors.

Mohamed F ElmansyDepartment of Chemistry, Chemistry of Life Processes Institute, and Center for Developmental Therapeutics, Northwestern University, Evanston, IL 60208, USA; Organometallic and Organometalloid Chemistry Department, National Research Centre, 12622 Cairo, Egypt.
Pedro SoaresDepartment of Chemistry, Chemistry of Life Processes Institute, and Center for Developmental Therapeutics, Northwestern University, Evanston, IL 60208, USA; Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Jose Ricardo D Dos RemediosDepartment of Chemistry, Chemistry of Life Processes Institute, and Center for Developmental Therapeutics, Northwestern University, Evanston, IL 60208, USA.
Raghad NowarDepartment of Neurobiology, Northwestern University, Evanston, IL 60208, USA.
Susan G FoxDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA; Daniel F. and Ada L. Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208, USA.
Anan YuDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA; Daniel F. and Ada L. Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208, USA.
William L KleinDepartment of Chemistry, Chemistry of Life Processes Institute, and Center for Developmental Therapeutics, Northwestern University, Evanston, IL 60208, USA; Department of Neurobiology, Northwestern University, Evanston, IL 60208, USA; Department of Neurology, Northwestern University, Chicago, IL 60611, USA.
Richard I MorimotoDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA; Daniel F. and Ada L. Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208, USA.
Richard B SilvermanDepartment of Chemistry, Chemistry of Life Processes Institute, and Center for Developmental Therapeutics, Northwestern University, Evanston, IL 60208, USA; Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA; Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. Electronic address: r-silverman@northwestern.edu.

Funding

Novel Protein Aggregation Inhibitors and Upper Motor Neuron Stabilizers for ALS and other Neurodegenerative DiseasesR01AG061708 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WILLIAM L KLEIN, Pembe Hande Ozdinler · 2019 to 2026
$10.5M
A robotic plate handling system for high content screening and 3D organoid cultureS10OD032367 · OD · NORTHWESTERN UNIVERSITY · PI HORVATH, CURT M · 2022 to 2022
$137k
NIA NIH HHS R01 AG061708NIH HHS S10 OD032367
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is a fast-progressing disease characterized by the loss of voluntary movements and death due to respiratory failure. The presence of protein aggregates is a major hallmark of the disease. Hence, targeting the pathological protein aggregation may provide more efficient therapeutics for ALS. Recently, we reported a cyclohexane-1,3-dione (NU-9) with in vitro anti-aggregation capacity and promising in vivo efficacy in ALS animal models, which validated our approach toward the development of novel and potentially more effective ALS therapeutics. Herein, we report the design and synthesis of a new series of small-molecule derivatives of NU-9 and the evaluation of their in vitro anti-aggregation activity in a PC12 cellular model containing an SOD1

Indexed as

Amyotrophic Lateral SclerosisProtein AggregatesProtein Aggregation, PathologicalAnimalsDose-Response Relationship, DrugHumansMolecular StructurePC12 CellsRatsStructure-Activity RelationshipSuperoxide Dismutase-1Protein AggregatesSuperoxide Dismutase-1Amyotrophic lateral sclerosisCyclohexane-1,3-dionesProtein aggregationSmall-moleculesSOD-1

Identifiers

PMID41223590
PMCPMC12648443

What OpenQuestion holds

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LicenceCC BY
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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.