ArticleInternational journal of molecular sciences2024
Phytaspase Does Not Require Proteolytic Activity for Its Stress-Induced Internalization.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
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Who cites it
2 citing papers in PubMed.
- 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
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Phytaspases differ from other members of the plant subtilisin-like protease family by having rare aspartate cleavage specificity and unusual localization dynamics. Phytaspases are secreted from healthy plant cells but are re-internalized upon perception of death-inducing stresses. Although proteolytic activity is required for the secretion of plant subtilases, its requirement for the retrograde transportation of phytaspases is currently unknown. To address this issue, we employed an approach to complement in trans the externalization of a prodomain-less form of
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Registered trials
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