Evidence mapPaperPMID 39656022Full record

ArticleJournal of medicinal chemistry2024

Constrained β-Hairpins Targeting the EphA4 Ligand Binding Domain.

Anne Marie Prentiss, Carlo Baggio, James Pagett, Anna O Kulinich, Iryna M Ethell, Kendall Muzzarelli, Zahra Assar, Maurizio Pellecchia

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2024. 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

8 authors.

Anne Marie PrentissDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, California 92521, United States.
Carlo BaggioDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, California 92521, United States.
James PagettDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, California 92521, United States.
Anna O KulinichDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, California 92521, United States.
Iryna M EthellDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, California 92521, United States.
Kendall MuzzarelliCayman Chemical Co., 1180 E. Ellsworth Road, Ann Arbor, Michigan 48108, United States.
Zahra AssarCayman Chemical Co., 1180 E. Ellsworth Road, Ann Arbor, Michigan 48108, United States.
Maurizio PellecchiaDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, California 92521, United States.ORCID 0000-0001-5179-470X

Funding

Mcl-1/Bfl-1 in apoptosis and signal transduction: a structure/function approachR01CA168517 · NCI · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI Maurizio Pellecchia · 2022 to 2024
$1.3M
Molecular and cellular mechanisms of inhibitory synapse developmentR01NS129555 · UNIVERSITY OF CALIFORNIA RIVERSIDE · 2025 to 2025
$482k
Targeting the EphA4 in motor neuron disease: a structure-based approachR01NS107479 · UNIVERSITY OF CALIFORNIA RIVERSIDE · 2025 to 2025
$398k
NCI NIH HHS P20 CA242620NCI NIH HHS R01 CA168517NIGMS NIH HHS P41 GM103311NINDS NIH HHS R01 NS107479NINDS NIH HHS R01 NS129555
6 · The paper itself

Abstract

The activity of the receptor tyrosine kinase EphA4 has been implicated in several pathologies including oncology (gastric and pancreatic cancers) and neurodegenerative diseases (amyotrophic lateral sclerosis and Alzheimer's disease). However, advances in validating EphA4 as a possible drug target have been limited by the lack of suitable pharmacological inhibitors. Recently, we reported on the design of potent EphA4 agonistic agents targeting its ligand binding domain (LBD). Based on previous studies with a phage display cyclic peptide inhibitor, we designed a β-hairpin mimetic with high affinity for EphA4-LBD. These agents hold great promise for further validation and development of EphA4-based therapeutics. Moreover, our studies introduce a possible strategy for the design of constrained β-hairpin peptides.

Indexed as

Receptor, EphA4Binding SitesDrug DesignHumansLigandsModels, MolecularPeptides, CyclicProtein BindingProtein DomainsLigandsPeptides, CyclicReceptor, EphA4

Identifiers

PMID39656022
PMCPMC11684737

What Socratic holds

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LicenceCC BY-NC-ND
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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.