ArticleMethods in molecular biology (Clifton, N.J.)2022
Identification of Cognate Protease/Substrate Pairs by Use of Class-Specific Inhibitors.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Assay for Phytaspase-mediated Peptide Precursor Cleavage Using Synthetic Oligopeptide Substrates.Bio-protocol · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins are regulated post-translationally by proteolytic processing. This includes plant signaling peptides that are proteolytically released from larger precursor proteins. The proteases involved in the biogenesis of signaling peptides and in regulation of other proteins by limited proteolysis are largely unknown. Here we describe how protease inhibitors that are specific for a certain class of proteases can be employed for the identification of proteases that are responsible for the processing of a given target protein. After having identified the protease family to which the processing enzyme belongs, candidate proteases and the GFP-tagged target protein are agro-infiltrated for transient expression in N. benthamiana leaves. Cleavage products are analyzed on immuno-blots and specificity of cleavage is confirmed by co-expression of class-specific inhibitors. For the identification of processing sites within the target protein, cleavage product(s) are purified by immunoprecipitation followed by polyacrylamide gel electrophoresis and analyzed by mass spectrometry.
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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.