Evidence map›Paper›PMID 41071873›Full record

ArticleScience advances2025

Plasticity of the cytotoxic Nep1-like protein enables promiscuity in binding to its lipid receptor glycosylinositol phosphorylceramides.

Nika Žibrat Kalanj, Andreja Prešern, Katerina Naumoska, Tina Snoj, Jana Aupič, Vesna Glavnik, Alen Albreht, Mojca Mally, Jure Derganc, Peter Greimel and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Deletion ofJournal of fungi (Basel, Switzerland) · 2026
    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

12 authors.

Nika Žibrat KalanjDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0002-4889-0108
Andreja PrešernDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0009-0003-5210-3757
Katerina NaumoskaLaboratory for Food Chemistry, Department of Analytical Chemistry, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0003-1087-0694
Tina SnojDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0002-1049-4222
Jana AupičCNR-Istituto Officina dei Materiali (IOM), 34136 Trieste, Italy.ORCID 0000-0001-6246-962X
Vesna GlavnikLaboratory for Food Chemistry, Department of Analytical Chemistry, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0003-0766-0266
Alen AlbrehtLaboratory for Food Chemistry, Department of Analytical Chemistry, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0003-0594-8899
Mojca MallyInstitute of Biophysics, Faculty of Medicine, University of Ljubljana, 1000 Ljubljana, Slovenia.ORCID 0000-0002-5176-8701
Jure DergancInstitute of Biophysics, Faculty of Medicine, University of Ljubljana, 1000 Ljubljana, Slovenia.
Peter GreimelLaboratory for Cell Function Dynamics, RIKEN Center for Brain Science, Wako, Saitama 351-0198, Japan.ORCID 0000-0002-4931-6183
Alessandra MagistratoCNR-Istituto Officina dei Materiali (IOM), 34136 Trieste, Italy.ORCID 0000-0002-2003-1985
Gregor AnderluhDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0002-9916-8465

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interactions between plants and pathogens pose a major challenge for plant health and agriculture. One type of threat comes from widespread cytolysins necrosis- and ethylene-inducing peptide 1-like proteins (NLPs) secreted by microbial pathogens. NLPs disrupt plant membranes through interactions with glycosylinositol phosphorylceramides (GIPCs), but the specificity of these interactions remains unclear. We studied binding and pore formation of NLPs in model membranes with GIPCs derived from dicotyledonous or monocotyledonous plants. Using the cytotoxic NLP 2 from fungus

Indexed as

Fungal ProteinsMolecular Dynamics SimulationProtein BindingPythiumFungal Proteins

Identifiers

PMID41071873
PMCPMC12513423

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.