Evidence map›Paper›PMID 40841375›Full record

ArticleNature communications2025

Promiscuous and multivalent interactions between Eps15 and partner protein Dab2 generate a complex interaction network.

Andromachi Papagiannoula, Ida Marie Vedel, Kathrin Motzny, Maud Tengo, Arbesa Saiti, Sigrid Milles

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
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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

6 authors.

Andromachi Papagiannoula *Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin, Germany.ORCID http://orcid.org/0000-0002-0767-5129
Ida Marie Vedel *Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin, Germany.ORCID http://orcid.org/0000-0002-3465-4796
Kathrin MotznyLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin, Germany.
Maud TengoUniversité Grenoble Alpes, CNRS, CEA, IBS, Grenoble, France.
Arbesa SaitiLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin, Germany.
Sigrid MillesLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin, Germany. milles@fmp-berlin.de.ORCID http://orcid.org/0000-0001-9362-9606

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Euratom (H2020 Euratom Research and Training Programme 2014-2018) ERC StG 802209
6 · The paper itself

Abstract

Clathrin-mediated endocytosis depends on complex protein interactions. Eps15 plays a key role through interactions of its three EH domains with Asn-Pro-Phe (NPF) motifs in intrinsically disordered regions (IDRs) of other endocytic proteins. Using nuclear magnetic resonance spectroscopy, we investigate the interaction between Eps15's EH domains and a highly disordered Dab2 fragment (Dab2

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsEndocytosisAmino Acid MotifsBiomolecular CondensatesClathrin-Coated VesiclesHumansHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsNuclear Magnetic Resonance, BiomolecularPhenylalanineProtein DomainsProtein Interaction MapsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsDAB2 protein, humanEPS15 protein, humanIntrinsically Disordered ProteinsPhenylalanine

Identifiers

PMID40841375
PMCPMC12370899

What OpenQuestion holds

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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.