ArticleAnalytical chemistry2020
ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease.
Article in Analytical chemistry, 2020. 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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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.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- A single-amino-acid cleavage controls global mitochondrial complex integrity.Nature structural & molecular biology · 2026Article
- Processing and release of the maize phytocytokine Zip1.Plant physiology · 2026Article
- Linking Superoxide Production and Scavenging in Plant Development.Plant, cell & environment · 2026Review
- Cysteine proteases and how YabG fits into clan CD of the MEROPS database.Journal of bacteriology · 2025Review
- Postproline Cleaving Enzymes also Show Specificity to Reduced Cysteine.Analytical chemistry · 2024Article
- Phytocystatin 6 is a context-dependent, tight-binding inhibitor of Arabidopsis thaliana legumain isoform β.The Plant journal : for cell and molecular biology · 2023Article
- ProtView: A Versatile Tool forJournal of proteome research · 2023Article
- Profiling Sequence Specificity of Proteolytic Activities Using Proteome-Derived Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Sensitive Plant N-Terminome Profiling with HUNTER.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities.ACS catalysis · 2021Article
- MANTI: Automated Annotation of Protein N-Termini for Rapid Interpretation of N-Terminome Data Sets.Analytical chemistry · 2021Article
- To New Beginnings: Riboproteogenomics Discovery of N-Terminal Proteoforms inFrontiers in plant science · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bottom-up mass spectrometry-based proteomics utilizes proteolytic enzymes with well characterized specificities to generate peptides amenable for identification by high-throughput tandem mass spectrometry. Trypsin, which cuts specifically after the basic residues lysine and arginine, is the predominant enzyme used for proteome digestion, although proteases with alternative specificities are required to detect sequences that are not accessible after tryptic digest. Here, we show that the human cysteine protease legumain exhibits a strict substrate specificity for cleavage after asparagine and aspartic acid residues during in-solution digestions of proteomes extracted 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.