ArticleNature plants2026
Cross-ribbon conformation defines peptide recognition in SCREW/CTNIP-NUT/HSL3 signalling.
Article in Nature plants, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
Abstract
Plants balance gas exchange with pathogen defense through dynamic stomatal regulation. Stomata close temporarily during pathogen attack to limit invasion, then reopen to restore photosynthesis and transpiration while lowering apoplast water saturation to inhibit pathogen proliferation. The secreted peptides, SCREW/CTNIP promote stomatal reopening through the receptor NUT/HSL3 and co-receptor BAK1/SERK3, thereby counteracting ABA and MAMP-triggered stomatal closure. Here we present the cryo-EM structures of AtNUTECD and the AtNUTECD-SCREW2/CTNIP4-AtBAK1ECD complex, uncovering a distinctive peptide-receptor interaction mechanism. SCREW2 adopts a unique cross-ribbon conformation that distinguishes it from other known conformations of LRR-RK-binding peptides, enabling its specific recognition by AtNUT and subsequent recruitment of AtBAK1. An N-linked glycan at N449 within the SCREW2-AtNUT binding interface is required for efficient SCREW2 recognition. Mutations in SCREW2 recognition sites significantly attenuated downstream MAPK activation and PTI marker gene expression.
Indexed as
Identifiers
42754654What OpenQuestion holds
Registered trials
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.