Evidence map›Paper›PMID 41025909›Full record

ArticleACS chemical neuroscience2025

Asparagine Deamidation Attenuates Toxicity, Aggregation, and Microglial Responses of Alzheimer's Amyloid-β.

Maria Sajimon, Christopher J Wheeler, Alejandro R Foley, Ka Chan, Martin N Griffin, Daniel M Dinakarapandian, Abigail Holberton, Jery Joy, Anant K Paravastu, Levi B Wood and 1 more

Abstract read
In one paragraph

Article in ACS chemical neuroscience, 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

11 authors.

Maria SajimonDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.ORCID 0000-0002-6753-6841
Christopher J WheelerDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.
Alejandro R FoleyDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.ORCID 0000-0002-8644-0546
Ka ChanDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.
Martin N GriffinGeorge W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Daniel M DinakarapandianSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332-0100, United States.
Abigail HolbertonGeorge W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Jery JoyDepartment of Anatomy, University of California, San Francisco, California 94141, United States.
Anant K ParavastuSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332-0100, United States.ORCID 0000-0001-7183-1942
Levi B WoodGeorge W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Jevgenij A RaskatovDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.ORCID 0000-0002-0082-9113

Funding

Using Chirality to Understand and Control Amyloid Beta Neuronal Uptake and ToxicityR01AG074954 · NIA · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI Jevgenij Raskatov · 2022 to 2026
$1.9M
NIA NIH HHS R01 AG074954
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a growing global challenge that imposes a tremendous burden on society and economies. Though recently approved anti-amyloid β (Aβ) immunotherapies show effectiveness in clearing amyloid and slowing cognitive decline, the removal of cerebral Aβ can also cause serious adverse events (SAEs). Therefore, decreasing the detrimental effects of Aβ in the brain without promoting SAEs is an unmet need in AD treatment. Here, we show that deamidation of Asparagine 27(N27) in Aβ1-42 can significantly reduce Aβ's neurotoxicity and decrease selective microglial pro-inflammatory cytokine production. We also show that deamidation of N27 produces a pronounced decrease in Aβ's aggregation propensity and decreases soluble oligomer formation, suggesting a potential mechanism for its mitigation of Aβ's detrimental cellular effects. Modulation of these Aβ properties by N27 deamidation represents a proof of concept for a potential strategy to alter the detrimental effects of Aβ that may not require its removal from the brain. Our findings on reducing Aβ's toxic properties by N27 deamidation may provide a basis for future therapeutic interventions.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAsparagineMicrogliaPeptide FragmentsAnimalsHumansMiceAmyloid beta-Peptidesamyloid beta-protein (1-42)AsparaginePeptide FragmentsAlzheimer’s diseaseamyloid-β (Aβ)Asparagine deamidationAβ-modificationneurotoxicityoligomer

Identifiers

PMID41025909
PMCPMC12989966

What OpenQuestion holds

Textmetadata
LicenceTDM
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.