Evidence map›Paper›PMID 40456702›Full record

ArticleChemMedChem2025

Inhibition of the Clathrin Terminal Domain-Amphiphysin Protein-Protein Interaction. Probing the Pitstop 2 Aromatic Moiety.

Kate Prichard, Mark J Robertson, Ngoc Chau, Jing Xue, Martin Neuenschwander, Uwe Fink, Andre Horatscheck, Marc Nazare, Phillip J Robinson, Volker Haucke and 1 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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. 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

11 authors.

Kate PrichardChemistry, School of Environmental & Life Sciences, The University of Newcastle, University Drive, Callaghan, NSW, 2308, Australia.ORCID https://orcid.org/0000-0003-0458-5037
Mark J RobertsonChemistry, School of Environmental & Life Sciences, The University of Newcastle, University Drive, Callaghan, NSW, 2308, Australia.
Ngoc ChauCell Signalling Unit, Children's Medical Research Institute, The University of Sydney, Hawkesbury Road, Westmead, Sydney, NSW 2145, Australia.ORCID https://orcid.org/0000-0001-5507-0493
Jing XueCell Signalling Unit, Children's Medical Research Institute, The University of Sydney, Hawkesbury Road, Westmead, Sydney, NSW 2145, Australia.ORCID https://orcid.org/0009-0007-1062-2881
Martin NeuenschwanderMarc Nazare - Chemical Biology, Leibniz Institute fur Molecular Pharmacologie, Robert-Roessle-Strasse 10, 13125, Berlin, Germany.ORCID https://orcid.org/0000-0002-3114-7975
Uwe FinkMarc Nazare - Chemical Biology, Leibniz Institute fur Molecular Pharmacologie, Robert-Roessle-Strasse 10, 13125, Berlin, Germany.
Andre HoratscheckMarc Nazare - Chemical Biology, Leibniz Institute fur Molecular Pharmacologie, Robert-Roessle-Strasse 10, 13125, Berlin, Germany.ORCID https://orcid.org/0000-0001-6485-6391
Marc NazareMarc Nazare - Chemical Biology, Leibniz Institute fur Molecular Pharmacologie, Robert-Roessle-Strasse 10, 13125, Berlin, Germany.ORCID https://orcid.org/0000-0002-1602-2330
Phillip J RobinsonCell Signalling Unit, Children's Medical Research Institute, The University of Sydney, Hawkesbury Road, Westmead, Sydney, NSW 2145, Australia.ORCID https://orcid.org/0000-0002-7878-0313
Volker HauckeMarc Nazare - Chemical Biology, Leibniz Institute fur Molecular Pharmacologie, Robert-Roessle-Strasse 10, 13125, Berlin, Germany.ORCID https://orcid.org/0000-0003-3119-6993
Adam McCluskeyChemistry, School of Environmental & Life Sciences, The University of Newcastle, University Drive, Callaghan, NSW, 2308, Australia.ORCID https://orcid.org/0000-0001-7125-863X

Funding

Australian Research Council DP180101781National Health and Medical Research Council 1022218
6 · The paper itself

Abstract

Pitstop 2, (Z)-N-(5-(4-bromenzylidene)-4-oxo-4,5-dihydrothiazol-2-yl)naphthalene-1-sulfonamide (1) inhibits the clathrin terminal domain-amphiphysin interaction (NTD-PPI) and has been widely used to investigate endocytosis. Herein, the synthesis of 56 novel Pitstop 2 analogues via four discrete focused libraries is reported. Specific modification to the 4-bromonenzylidene moiety is explored, and their ability to inhibit the NTD-PPI interaction is examined by ELISA. In cell endocytosis, effects are measured for selective analogues as is the inhibition of dynamin, another protein involved in the endocytosis process. The most NTD-PPI active analogues retain 2- and 4-disposed substituents on the aromatic head, with 2,3,4-trihydroxy (28) the most active (IC

Indexed as

ClathrinNerve Tissue ProteinsSulfonamidesDose-Response Relationship, DrugEndocytosisHumansMolecular StructureProtein BindingProtein DomainsStructure-Activity RelationshipThiazolidinesamphiphysinClathrinNerve Tissue Proteinspitstop 2SulfonamidesThiazolidinesaromatic moietyclathrin‐mediated endocytosislibrary synthesismolecular dockingpitstop

Identifiers

PMID40456702
PMCPMC12368479

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.