Evidence map›Paper›PMID 40623182›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

An aminosterol breaks the autocatalytic cycle of Aβ

Lucas B Fallot, Johnathan R Pinc, Joseph E Buselmeier, Julia C Palchak, Supria S Shroff, Kaitlyn Zang, Dillon J Rinauro, Kate M Bacon, Michael Nguyen, Mary Claire Schleck and 20 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Special Issue "Molecules at Play in Neurological Diseases".Current issues in molecular biology · 2025
    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

30 authors.

Lucas B FallotDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0000-0003-3056-2947
Johnathan R PincDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0008-7447-2680
Joseph E BuselmeierDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0001-6099-4778
Julia C PalchakDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0001-9887-427X
Supria S ShroffDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Kaitlyn ZangDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Dillon J RinauroCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Kate M BaconDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Michael NguyenDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0001-6645-6014
Mary Claire SchleckDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0009-5424-5568
Alyssa R CornellDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0009-1737-0685
Alexandra OshidarDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Donald J DarrellDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Justus M GabrielDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0009-0009-5353-2717
Aidan K WrightDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Liam R SasserDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Ryan P KreiserDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
F John BurpoDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0000-0002-0303-1043
Alessia SantambrogioCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Peifeng XuCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Robert W KubiakDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Joseph LoverdeDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Victor A JaffettDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Justin R TooleDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.
Denise BarbutBAZ Therapeutics, Inc., Philadelphia, PA 19103.
Michael ZasloffBAZ Therapeutics, Inc., Philadelphia, PA 19103.
Fabrizio ChitiSection of Biochemistry, Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence 50134, Italy.ORCID 0000-0002-1330-1289
Alexander J DearDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich 8093, Switzerland.
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-3616-1610
Ryan LimbockerDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996.ORCID 0000-0002-6030-6656

Funding

DOD | ARPA | Defense Sciences Office, DARPA (DSO) N/ADOD | Defense Threat Reduction Agency (DTRA) SARIDOD | Office of the Under Secretary of Defense for Research and Engineering (USDR&E) N/ADOD | USA | AFC | CCDC | DEVCOM Army Research Laboratory (DEVCOM ARL) N/APhotonics Research Center N/A
6 · The paper itself

Abstract

Aberrant aggregates of the 42-residue form of the amyloid-β peptide (Aβ

Indexed as

Amyloid beta-PeptidesCell MembranePeptide FragmentsProtein AggregatesProtein Aggregation, PathologicalAlzheimer DiseaseAmyloidCell Line, TumorHumansAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsProtein AggregatesAlzheimer’samyloidchemical kineticsdrug discoveryprotein misfolded oligomers

Identifiers

PMID40623182
PMCPMC12280974

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.