ArticleFrontiers in plant science2019
Clathrin-Mediated Endocytosis Delivers Proteolytically Active Phytaspases Into Plant Cells.
Article in Frontiers in plant science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- A Peculiar Phospholipid-Binding Specificity and Cell Death-Related Properties of Tubic (International journal of molecular sciences · 2026Article
- Plant caspase-like proteins: from function identification to application in winter rapeseed genetic breeding.Frontiers in plant science · 2026Review
- Long-Term Phytaspase Responses inInternational journal of molecular sciences · 2025Article
- Retrograde Transport of Tobacco Phytaspase Is Mediated by Its Partner, Tubby-like F-Box Protein 8.International journal of molecular sciences · 2025Article
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Phytaspase Does Not Require Proteolytic Activity for Its Stress-Induced Internalization.International journal of molecular sciences · 2024Article
- Characterization of Phytaspase Proteolytic Activity Using Fluorogenic Peptide Substrates.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Purification of Phytaspases Using a Biotinylated Peptide Inhibitor.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal from Tobacco Calreticulin-3.International journal of molecular sciences · 2023Article
- Mechanisms controlling plant proteases and their substrates.Cell death and differentiation · 2023Review
- Protease inhibitor ASP enhances freezing tolerance by inhibiting protein degradation in kumquat.Horticulture research · 2023Article
- Identification of Phytaspase Interactors via the Proximity-Dependent Biotin-Based Identification Approach.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phytaspases belong to the family of plant subtilisin-like proteases and are distinct from other family members, as they have strict and rarely occurring aspartate cleavage specificity and unusual localization dynamics. After being secreted into the apoplast of healthy plant tissues, phytaspases are able to return back into cells that have been committed to cell death due to a variety of biotic and abiotic stresses. It was recently discovered that retrograde transport of phytaspases involves clathrin-mediated endocytosis. Here, consequences of phytaspase internalization were studied. Proteolytic activity of phytaspases in the apoplast and intracellular protein fractions obtained from
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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.