Evidence map›Paper›PMID 43020795›Full record

ArticleNature communications2026

Mechanistic insights into NET1-UNC5B complex formation and Its targeted disruption by NP137 fab and NET1 peptide competitors.

Faride Rafiei, Monika Gupta, Elena N Kitova, Oliver Peters, Scott Legare, Fabian Heide, Natalie Krahn, Ben A Bailey-Elkin, Serife Akgül, Morgan Brisset and 14 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. 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

24 authors.

Faride Rafiei *Department of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.ORCID 0000-0002-5314-4521
Monika Gupta *Department of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Elena N Kitova *Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0003-0812-3286
Oliver Peters *Department of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.ORCID 0000-0001-8671-6955
Scott LegareDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.ORCID 0000-0003-4112-706X
Fabian HeideDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Natalie KrahnDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, USA.ORCID 0000-0003-0696-433X
Ben A Bailey-ElkinDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.ORCID 0000-0001-6863-2643
Serife AkgülInstitute for Dental Research and Oral Muscuskeletal Biology, Center for Biochemistry, Faculty of Medicine and University Hospital, University of Cologne, 50931, Cologne, Germany.
Morgan BrissetApoptosis, Cancer and Development Laboratory - Equipe labellisée 'La Ligue', LabEx DEVweCAN, Institut Convergence PLAsCAN, Centre de Recherche en Cancérologie de Lyon (CRCL), INSERM U1052-CNRS UMR5286, Université de Lyon, Université Claude Bernard Lyon1, Centre Léon Bérard, 69008, Lyon, France.ORCID 0000-0002-4665-0661
Haben GabirDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Candice Harder-ViddalDepartment of Chemistry and Physics, Canadian Mennonite University, Winnipeg, MB, Canada.
Roy RoshkoDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Markus MeierDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.ORCID 0000-0003-1068-746X
Gay Pauline Padilla-MeierDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Abdelrhman ZakariaDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
Miguel A Alejandre AlcázarInstitute for Lung Health (ILH), University of Giessen and Marburg Lung Center (UGMLC), Member of the German Center for Lung Research (DZL), Cologne, Germany.ORCID 0000-0002-3176-0411
Oleksiy KlymenkoInstitute for Lung Health (ILH), University of Giessen and Marburg Lung Center (UGMLC), Member of the German Center for Lung Research (DZL), Cologne, Germany.
Vesna StanojlovicDepartment of Biosciences and Medical Biology, University of Salzburg, Salzburg, Austria.
Chiara CabreleDepartment of Molecular Biology, University of Salzburg, Salzburg, Austria.
Patrick MehlenNetris Pharma, 69008, Lyon, France.ORCID 0000-0003-1743-5417
John S KlassenDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada. john.klassen@ualberta.ca.ORCID 0000-0002-3389-7112
Manuel KochInstitute for Dental Research and Oral Muscuskeletal Biology, Center for Biochemistry, Faculty of Medicine and University Hospital, University of Cologne, 50931, Cologne, Germany. Manuel.Koch@uni-koeln.de.ORCID 0000-0002-2962-7814
Jörg StetefeldDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada. Jorg.stetefeld@umanitoba.ca.ORCID 0000-0003-1478-3248

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Netrin‑1, a secreted protein initially characterized for its role in axon guidance, has emerged as a critical mediator of cancer progression. Preclinical studies with the anti‑netrin‑1 antibody NP137, which blocks the netrin‑1-UNC5B interaction, have demonstrated reactivation of tumor suppressor functions and sensitization of cancer cells to chemotherapy. Here, we identified the molecular binding interface of the netrin‑1-UNC5B complex using integrative structural and quantitative biophysical analyses. We then determined how NP137 binding inhibits this interaction by sterically blocking key contact points within the interface. Guided by these mechanistic insights, we rationally designed peptides that disrupt the netrin‑1-UNC5B complex through interfering with heparin-mediated stabilization of the complex by binding to shared heparin-binding sites. This comprehensive structural and mechanistic analysis advances understanding of netrin‑1 signaling and establishes strategies for therapeutic intervention in netrin‑1-driven malignancies.

Indexed as

Immunoglobulin Fab FragmentsNetrin-1Netrin ReceptorsPeptidesAnimalsAntibodies, Monoclonal, HumanizedBinding SitesHumansModels, MolecularProtein BindingSignal TransductionAntibodies, Monoclonal, HumanizedImmunoglobulin Fab FragmentsNetrin-1netrin-1 inhibitor NP137Netrin ReceptorsNTN1 protein, humanPeptides

Identifiers

PMID43020795
PMCPMC13759497

What OpenQuestion holds

Textmetadata
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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 OpenQuestion graph.