ArticlePloS one2010
Amyloid-like protein inclusions in tobacco transgenic plants.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana.Journal of experimental botany · 2023Article
- Complex Networks of Prion-Like Proteins Reveal Cross Talk Between Stress and Memory Pathways in Plants.Frontiers in plant science · 2021Article
- Emerging Roles of Functional Bacterial Amyloids in Gene Regulation, Toxicity, and Immunomodulation.Microbiology and molecular biology reviews : MMBR · 2020Review
- Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.PLoS pathogens · 2019Article
- Amyloidosis and Longevity: A Lesson from Plants.Biology · 2019Article
- A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants.Frontiers in plant science · 2019Article
- The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease.Frontiers in aging neuroscience · 2018Review
- Review
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- The Over-expression of the Plastidial Transglutaminase from Maize in Arabidopsis Increases the Activation Threshold of Photoprotection.Frontiers in plant science · 2016Article
- The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.Microbial cell factories · 2015Article
- Overexpressed Arabidopsis Annexin4 accumulates in inclusion body-like structures.Acta histochemica · 2015Article
- When amyloids become prions.Prion · 2014Article
- Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.PloS one · 2014Article
- Plastid proteostasis and heterologous protein accumulation in transplastomic plants.Plant physiology · 2012Article
- Role of plastid transglutaminase in LHCII polyamination and thylakoid electron and proton flow.PloS one · 2012Article
- Structural insights into functional and pathological amyloid.The Journal of biological chemistry · 2011Review
- Active protein aggregates produced in Escherichia coli.International journal of molecular sciences · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of amyloid structures in bacteria and fungi our data argue that amyloid formation is likely a ubiquitous process occurring across the different kingdoms of life. The discovery of amyloid conformations inside inclusions of genetically modified plants might have implications regarding their use for human applications.
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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.