ArticlePhysiologia plantarum
A Structural Bridge Between Kingdoms: How Collagen-Derived Peptides Influence Plant Stress and Growth Pathways.
Article in Physiologia plantarum. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- A Structural Bridge Between Kingdoms: How Collagen-Derived Peptides Influence Plant Stress and Growth Pathways.Physiologia plantarumArticle
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen-derived protein hydrolysates (CDPH) are widely used as plant biostimulants primarily due to their content of bioactive oligopeptides. When applied to hydroponically grown Solanum lycopersicum plants, CDPH significantly promoted root development, particularly by increasing the number and length of lateral roots. To gain insight into the underlying molecular mechanisms, we hypothesized that plants may possess proteins capable of interacting with collagen-like peptides. To test this, we conducted a comprehensive homology search of the Arabidopsis thaliana proteome using a Hidden Markov model-based approach built from three human collagen-binding proteins (CBPs) and 14 known collagen-binding domains (CBDs). After filtering, 10 Arabidopsis proteins emerged as putative candidates with the potential to bind collagen. Notably, the highest homology was observed for a matrix metalloproteinase, At5-MMP, showing 44% identity with its human counterpart HsMMP1, and for AtSERPIN1, which displayed the strongest e-value match to HsSERPINH1 (22% identity). Both plant proteins are functionally associated with responses to abiotic and biotic stresses, a feature that mirrors the known physiological effects of CDPH-based biostimulants. These findings support the hypothesis that plants possess proteins capable of recognizing collagen-like structures, offering a plausible molecular basis for the activity of CDPH-based biostimulants and paving the way for future biochemical validation.
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.