ArticleScientific reports2021
Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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
15 citing papers in PubMed, 24 citations in OpenAlex.
- Cysteine-Rich Peptides in Food Systems: Structure, Sources, Functional Properties, Potential Applications, and Future Perspectives.Probiotics and antimicrobial proteins · 2026Review
- A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B.Current research in microbial sciences · 2026Article
- The Small Key to the Treasure Chest: Endogenous Plant Peptides Involved in Symbiotic Interactions.Plants (Basel, Switzerland) · 2025Review
- Antagonism within mutualism: host control of symbionts through nodule-specific antimicrobial peptides.Frontiers in microbiology · 2025Review
- Multifaceted antimicrobial mechanisms of NCR147-derived peptides fromFrontiers in microbiology · 2025Article
- Chickpea NCR13 disulfide cross-linking variants exhibit profound differences in antifungal activity and modes of action.PLoS pathogens · 2024Article
- Plant peptides - redefining an area of ribosomally synthesized and post-translationally modified peptides.Natural product reports · 2024Review
- NCRs make the difference.Nature plants · 2023Article
- Enhanced Antibacterial Activity of Substituted Derivatives of NCR169C Peptide.International journal of molecular sciences · 2023Article
- The γ-Core Motif Peptides of AMPs from Grasses Display Inhibitory Activity against Human and Plant Pathogens.International journal of molecular sciences · 2022Article
- Rationally Designed Antimicrobial Peptides Are Potential Tools to Combat Devastating Bacteria and Fungi.International journal of molecular sciences · 2022Article
- Nanoparticles in association with antimicrobial peptides (NanoAMPs) as a promising combination for agriculture development.Frontiers in molecular biosciences · 2022Review
- A variable gene family encoding nodule-specific cysteine-rich peptides in pea (Frontiers in plant science · 2022Article
- Legume Plant Peptides as Sources of Novel Antimicrobial Molecules Against Human Pathogens.Frontiers in molecular biosciences · 2022Article
- Fungal effector SIB1 of Colletotrichum orbiculare has unique structural features and can suppress plant immunity in Nicotiana benthamiana.The Journal of biological chemistry · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A model legume, Medicago truncatula, has over 600 nodule-specific cysteine-rich (NCR) peptides required for symbiosis with rhizobia. Among them, NCR169, an essential factor for establishing symbiosis, has four cysteine residues that are indispensable for its function. However, knowledge of NCR169 structure and mechanism of action is still lacking. In this study, we solved two NMR structures of NCR169 caused by different disulfide linkage patterns. We show that both structures have a consensus C-terminal β-sheet attached to an extended N-terminal region with dissimilar features; one moves widely, whereas the other is relatively stapled. We further revealed that the disulfide bonds of NCR169 contribute to its structural stability and solubility. Regarding the function, one of the NCR169 oxidized forms could bind to negatively charged bacterial phospholipids. Furthermore, the positively charged lysine-rich region of NCR169 may be responsible for its antimicrobial activity against Escherichia coli and Sinorhizobium meliloti. This active region was disordered even in the phospholipid bound state, suggesting that the disordered conformation of this region is key to its function. Morphological observations suggested the mechanism of action of NCR169 on bacteria. The present study on NCR169 provides new insights into the structure and function of NCR peptides.
Indexed as
Identifiers
What 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.