ArticleInternational journal of molecular sciences2017
Predicting Amyloidogenic Proteins in the Proteomes of Plants.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Protein nonadditive expression and solubility contribute to heterosis inFrontiers in plant science · 2023Article
- Exploring cryptic amyloidogenic regions in prion-like proteins from plants.Frontiers in plant science · 2022Article
- Article
- Review
- β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis.International journal of molecular sciences · 2021Review
- Temporal Control of Seed Development in Dicots: Molecular Bases, Ecological Impact and Possible Evolutionary Ramifications.International journal of molecular sciences · 2021Review
- Article
- Accumulation of storage proteins in plant seeds is mediated by amyloid formation.PLoS biology · 2020Article
- WALTZ-DB 2.0: an updated database containing structural information of experimentally determined amyloid-forming peptides.Nucleic acids research · 2020Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule BacteriumBiomolecules · 2019Article
- Amyloidosis and Longevity: A Lesson from Plants.Biology · 2019Article
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Special Protein Molecules Computational Identification.International journal of molecular sciences · 2018Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids are protein fibrils with characteristic spatial structure. Though amyloids were long perceived to be pathogens that cause dozens of incurable pathologies in humans and mammals, it is currently clear that amyloids also represent a functionally important form of protein structure implicated in a variety of biological processes in organisms ranging from archaea and bacteria to fungi and animals. Despite their social significance, plants remain the most poorly studied group of organisms in the field of amyloid biology. To date, amyloid properties have only been demonstrated in vitro or in heterologous systems for a small number of plant proteins. Here, for the first time, we performed a comprehensive analysis of the distribution of potentially amyloidogenic proteins in the proteomes of approximately 70 species of land plants using the Waltz and SARP (Sequence Analysis based on the Ranking of Probabilities) bioinformatic algorithms. We analyzed more than 2.9 million protein sequences and found that potentially amyloidogenic proteins are abundant in plant proteomes. We found that such proteins are overrepresented among membrane as well as DNA- and RNA-binding proteins of plants. Moreover, seed storage and defense proteins of most plant species are rich in amyloidogenic regions. Taken together, our data demonstrate the diversity of potentially amyloidogenic proteins in plant proteomes and suggest biological processes where formation of amyloids might be functionally important.
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