Evidence map›Paper›PMID 40436739›Full record

ArticleJournal of medicinal chemistry2025

Design of Paromomycin and Neomycin as Sulfated and Hydrophobic Glycans to Target Heparanase-Driven Tumor Progression and Metastasis.

Hawau Abdulsalam, Livia Philip, Kartikey Singh, Malik Farhoud, Neta Ilan, Israel Vlodavsky, Hien M Nguyen

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Heparan Sulfate Proteoglycans in Immunity.Proteoglycan research · 2026
    Article
  3. Integrated 3D-QSAR and cellular profiling of sulfated and hydrophobic aminoglycoside glycans to modulate heparanase activity.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Article
  4. 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

7 authors.

Hawau AbdulsalamDepartment of Chemistry, Wayne State University, Detroit, Michigan 48202, United States.ORCID 0009-0004-1837-2352
Livia PhilipDepartment of Chemistry, Wayne State University, Detroit, Michigan 48202, United States.
Kartikey SinghDepartment of Chemistry, Wayne State University, Detroit, Michigan 48202, United States.ORCID 0000-0002-0257-7415
Malik FarhoudTechnion Integrated Cancer Center, Rappaport Faculty of Medicine, Technion─Israel Institute of Technology, Haifa 3525422, Israel.
Neta IlanTechnion Integrated Cancer Center, Rappaport Faculty of Medicine, Technion─Israel Institute of Technology, Haifa 3525422, Israel.
Israel VlodavskyTechnion Integrated Cancer Center, Rappaport Faculty of Medicine, Technion─Israel Institute of Technology, Haifa 3525422, Israel.
Hien M NguyenDepartment of Chemistry, Wayne State University, Detroit, Michigan 48202, United States.ORCID 0000-0002-7626-8439

Funding

Tailoring Structures of Sulfated Oligosaccharides for Modulating Heparanase ActivityR01GM098285 · NIGMS · WAYNE STATE UNIVERSITY · PI NGUYEN, HIEN M · 2012 to 2022
$3.5M
500 MHz NMR SpectrometerS10OD028488 · OD · WAYNE STATE UNIVERSITY · PI ALLEN, MATTHEW J · 2021 to 2021
$600k
NIGMS NIH HHS R01 GM098285NIH HHS S10 OD028488
6 · The paper itself

Abstract

Heparanase (HPSE) is the sole mammalian endoglycosidase that degrades heparan sulfate (HS) proteoglycans, disrupting the extracellular matrix (ECM) and promoting cancer invasion and metastasis. Although HPSE overexpression is linked to tumor progression, no clinically approved HPSE inhibitors exist. We developed aminoglycoside-based HS mimetics with defined sulfation and hydrophobic modifications to target HPSE's lipophilic pockets, a novel approach distinct from traditional HS glycans. Computational modeling showed that these mimetics engage HPSE through hydrophobic and π-π stacking interactions, enhancing affinity. The most potent compounds inhibited HPSE-driven ECM degradation, tumor cell proliferation, and invasion.

Indexed as

Antineoplastic AgentsDrug DesignGlucuronidasePolysaccharidesAnimalsCell Line, TumorCell ProliferationDisease ProgressionHeparanaseHumansHydrophobic and Hydrophilic InteractionsMelanoma, ExperimentalMiceMice, Inbred C57BLNeoplasm MetastasisStructure-Activity RelationshipAntineoplastic AgentsGlucuronidaseHeparanasePolysaccharides

Identifiers

PMID40436739
PMCPMC12184805

What Socratic 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 Socratic graph.