ArticleInternational journal of molecular sciences2021
Identification of Phytaspase Interactors via the Proximity-Dependent Biotin-Based Identification Approach.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 11 citations in OpenAlex.
- Application of Proximity-Labeling Techniques in Plants: A Review of Successful Cases.International journal of molecular sciences · 2026Review
- Genome-Wide Association Study Reveals Genetic Loci, Candidate Genes and Favorable Haplotypes for Important Agronomic Traits inJournal of fungi (Basel, Switzerland) · 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
- TurboID-Based Proximity Labeling: A Method to Decipher Protein-Protein Interactions in Plants.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
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Proteolytic enzymes are instrumental in various aspects of plant development, including senescence. This may be due not only to their digestive activity, which enables protein utilization, but also to fulfilling regulatory functions. Indeed, for the largest family of plant serine proteases, subtilisin-like proteases (subtilases), several members of which have been implicated in leaf and plant senescence, both non-specific proteolysis and regulatory protein processing have been documented. Here, we strived to identify the protein partners of phytaspase, a plant subtilase involved in stress-induced programmed cell death that possesses a characteristic aspartate-specific hydrolytic activity and unusual localization dynamics. A proximity-dependent biotin identification approach in
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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.