Evidence map›Paper›PMID 39843392›Full record

ArticleChemMedChem2025

Aminocholestane and Aminoandrostane Inhibitors of the SH2 Domain-Containing Inositol 5'-Phosphatase (SHIP).

Angela M Pacherille, Dennis R Viernes, Chiara Pedicone, Sandra Fernandes, Otto M Dungan, Shawn Dormann, Daniel R Wallach, Raki Sudan, Robbie Brooks, Christopher M Russo and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ChemMedChem, 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. SHIPi improves hematologic recovery after chemotherapy.Molecular medicine (Cambridge, Mass.) · 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

14 authors.

Angela M PacherilleDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Dennis R ViernesDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Chiara PediconeDepartment of Microbiology & Immunology, SUNY Upstate Medical University, 766 Irving Avenue, Syracuse, NY, 13210, USA.
Sandra FernandesDepartment of Microbiology & Immunology, SUNY Upstate Medical University, 766 Irving Avenue, Syracuse, NY, 13210, USA.
Otto M DunganDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Shawn DormannDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Daniel R WallachDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Raki SudanDepartment of Microbiology & Immunology, SUNY Upstate Medical University, 766 Irving Avenue, Syracuse, NY, 13210, USA.
Robbie BrooksDepartment of Microbiology & Immunology, SUNY Upstate Medical University, 766 Irving Avenue, Syracuse, NY, 13210, USA.
Christopher M RussoDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Kyle T HowardDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Michael S CosgroveDepartment of Microbiology & Immunology, SUNY Upstate Medical University, 766 Irving Avenue, Syracuse, NY, 13210, USA.
William G KerrDepartment of Microbiology & Immunology, SUNY Upstate Medical University, 766 Irving Avenue, Syracuse, NY, 13210, USA.
John D ChisholmDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.ORCID https://orcid.org/0000-0001-9518-2393

Funding

Translating SHIP1 Genetics to Generate a Novel Alzheimers Pharmacologic AgentRF1AG059717 · NIA · UNIVERSITY OF KENTUCKY · PI ESTUS, STEVEN, HUMPHREY, MARY BETH · 2018 to 2019
$3.9M
Alzheimer's Association E2A-24-1145198NIA NIH HHS RF1 AG059717NIH HHS RF1AG059717
6 · The paper itself

Abstract

The SH2-containing inositol phosphatase (SHIP) has become an actively researched therapeutic target for a number of disorders, including Alzheimer's Disease, Graft-vs-Host disease, obesity and cancer. Analogs of the aminosteroid SHIP inhibitor 3α-aminocholestane (3AC) have been synthesized and tested. Analogs with improved water solubility have been identified. Deletion of the C17 alkyl group from the cholestane skeleton improves water solubility, however these compounds inhibit both SHIP1 and SHIP2. Enzyme kinetics imply that these molecules are competitive inhibitors of SHIP, binding at a site near where the substrate binds to the phosphatase. A model of the binding of the inhibitors within the active site of SHIP1 is proposed to explain the structure activity studies. Overall this work provides more water soluble aminosteroid pan-SHIP1/2 inhibitors that can be used for future studies of SHIP activity.

Indexed as

AndrostanesCholestanesEnzyme InhibitorsPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesHumansMolecular Structuresrc Homology DomainsStructure-Activity RelationshipAndrostanesCholestanesEnzyme InhibitorsINPPL1 protein, humanPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesAlzheimer's diseaseInhibitorInositol phosphataseSHIPSteroid

Identifiers

PMID39843392
PMCPMC12046972

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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.