ReviewThe New phytologist2018
Macrocyclization by asparaginyl endopeptidases.
Review in The New phytologist, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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
14 citing papers in PubMed, 50 citations in OpenAlex.
- Identification of a key peptide cyclase for novel cyclic peptide discovery in Pseudostellaria heterophylla.Plant communications · 2025Article
- Enzymatic Protein Immobilization for Nanobody Array.Molecules (Basel, Switzerland) · 2024Article
- On the design of a constitutively active peptide asparaginyl ligase for facile protein conjugation.FEBS open bio · 2023Article
- Vacuolar Processing Enzymes in Plant Programmed Cell Death and Autophagy.International journal of molecular sciences · 2023Review
- The flax genome reveals orbitide diversity.BMC genomics · 2022Article
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Scalable and Efficient In Planta Biosynthesis of Sunflower Trypsin Inhibitor-1 (SFTI) Peptide Therapeutics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Plant asparaginyl endopeptidases and their structural determinants of function.Biochemical Society transactions · 2021Review
- Engineering protein theranostics using bio-orthogonal asparaginyl peptide ligases.Theranostics · 2021Article
- Site-Specific Sequential Protein Labeling Catalyzed by a Single Recombinant Ligase.Journal of the American Chemical Society · 2019Article
- Natural Occurring and Engineered Enzymes for Peptide Ligation and Cyclization.Frontiers in chemistry · 2019Review
- Rapid and Scalable Plant-Based Production of a Potent Plasmin Inhibitor Peptide.Frontiers in plant science · 2019Article
- Structural analyses ofThe Journal of biological chemistry · 2018Article
- Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Contents Summary 923 I. Introduction 923 II. Plant AEPs with macrocyclizing ability 924 III. Mechanism of macrocyclization by AEPs 925 IV. Conclusions 927 Acknowledgements 927 References 927 SUMMARY: Plant asparaginyl endopeptidases (AEPs) are important for the post-translational processing of seed storage proteins via cleavage of precursor proteins. Some AEPs also function as peptide bond-makers during the biosynthesis of several unrelated classes of cyclic peptides, namely the kalata-type cyclic peptides, PawS-Derived Peptides and cyclic knottins. These three families of gene-encoded peptides have different evolutionary origins, but all have recruited AEPs for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEPs capable of peptide macrocyclization, and insights have been gained from the first AEP crystal structures, albeit mammalian ones. Although the biochemical studies have improved our understanding of the mechanism of action, the focus now is to understand what changes in AEP sequence and structure enable some plant AEPs to perform macrocyclization reactions.
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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.