ReviewProtein science : a publication of the Protein Society2018
Global substrate specificity profiling of post-translational modifying enzymes.
Review in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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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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
23 citing papers in PubMed, 42 citations in OpenAlex.
- DeepPTMPred: a multi-modal deep learning framework for accurate prediction of protein post-translational modification sites.Briefings in bioinformatics · 2026Article
- A helical peptide antagonist of the human growth hormone receptor.Endocrinology · 2026Article
- Substrate prediction for RiPP biosynthetic enzymesDigital discovery · 2025Article
- Comprehensive proteolytic profiling of Aedes aegypti mosquito midgut extracts: Unraveling the blood meal protein digestion system.PLoS neglected tropical diseases · 2025Article
- Advances of NAT10 in diseases: insights from dual properties as protein and RNA acetyltransferase.Cell biology and toxicology · 2024Review
- Nonallosteric activation of posttranslational modification enzymes by active site-directed inhibitors.Computational and structural biotechnology journal · 2024Article
- Description of an activity-based enzyme biosensor for lung cancer detection.Communications medicine · 2024Article
- Harmony of Protein Tags and Chimeric Molecules Empowers Targeted Protein Ubiquitination and Beyond.Cells · 2024Review
- Substrate Prediction for RiPP Biosynthetic Enzymes via Masked Language Modeling and Transfer Learning.ArXiv · 2024Article
- Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.Nature communications · 2024Article
- Geometric Remodeling of Nitrilase Active Pocket Based on ALF-Scanning Strategy To Enhance Aromatic Nitrile Substrate Preference and Catalytic Efficiency.Applied and environmental microbiology · 2023Article
- Lysine Malonylation and Its Links to Metabolism and Diseases.Aging and disease · 2023Review
- Multiplex substrate profiling by mass spectrometry for proteases.Methods in enzymology · 2023Article
- A reactive center loop-based prediction platform to enhance the design of therapeutic SERPINs.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- In Vivo Measurement of Granzyme Proteolysis from Activated Immune Cells with PET.ACS central science · 2021Article
- Origin and Expansion of the Serine Protease Repertoire in the Myelomonocyte Lineage.International journal of molecular sciences · 2021Review
- Quantitative profiling of protease specificity.PLoS computational biology · 2021Article
- Assessment of Proteolysis by Pyrylium and Other Fluorogenic Reagents.Protein and peptide letters · 2021Article
- Platform to Discover Protease-Activated Antibiotics and Application to Siderophore-Antibiotic Conjugates.Journal of the American Chemical Society · 2020Article
- Cysteine Cathepsin Protease Inhibition: An update on its Diagnostic, Prognostic and Therapeutic Potential in Cancer.Pharmaceuticals (Basel, Switzerland) · 2019Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Enzymes that modify the proteome, referred to as post-translational modifying (PTM) enzymes, are central regulators of cellular signaling. Determining the substrate specificity of PTM enzymes is a critical step in unraveling their biological functions both in normal physiological processes and in disease states. Advances in peptide chemistry over the last century have enabled the rapid generation of peptide libraries for querying substrate recognition by PTM enzymes. In this article, we highlight various peptide-based approaches for analysis of PTM enzyme substrate specificity. We focus on the application of these technologies to proteases and also discuss specific examples in which they have been used to uncover the substrate specificity of other types of PTM enzymes, such as kinases. In particular, we highlight our multiplex substrate profiling by mass spectrometry (MSP-MS) assay, which uses a rationally designed, physicochemically diverse library of tetradecapeptides. We show how this method has been applied to PTM enzymes to uncover biological function, and guide substrate and inhibitor design. We also briefly discuss how this technique can be combined with other methods to gain a systems-level understanding of PTM enzyme regulation and function.
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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.