ArticleThe Journal of biological chemistry2018
Structural analyses of
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 47 citations in OpenAlex.
- Positional scanning and computational modeling reveal determinants of legumain transpeptidase activity.Protein science : a publication of the Protein Society · 2026Article
- Transcriptome-guided discovery and active-site gatekeeper engineering of a Viola arcuata asparaginyl ligase with superior catalytic performance.The Journal of biological chemistry · 2026Article
- Phytocystatin 6 is a context-dependent, tight-binding inhibitor of Arabidopsis thaliana legumain isoform β.The Plant journal : for cell and molecular biology · 2023Article
- On the design of a constitutively active peptide asparaginyl ligase for facile protein conjugation.FEBS open bio · 2023Article
- Structural basis for proenzyme maturation, substrate recognition, and ligation by a hyperactive peptide asparaginyl ligase.The Plant cell · 2022Article
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- PAL-Mediated Ligation for Protein and Cell-Surface Modification.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The legumain McPAL1 from Momordica cochinchinensis is a highly stable Asx-specific splicing enzyme.The Journal of biological chemistry · 2021Article
- The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities.ACS catalysis · 2021Article
- Structural and biochemical analyses of concanavalin A circular permutation by jack bean asparaginyl endopeptidase.The Plant cell · 2021Article
- Plant asparaginyl endopeptidases and their structural determinants of function.Biochemical Society transactions · 2021Review
- Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of α-Helix As Oxyanion-Binding Site.Journal of the American Chemical Society · 2021Article
- Engineering protein theranostics using bio-orthogonal asparaginyl peptide ligases.Theranostics · 2021Article
- Site-Specific Protein Modifications by an Engineered Asparaginyl Endopeptidase fromFrontiers in chemistry · 2021Article
- Structural and functional studies ofThe Journal of biological chemistry · 2020Article
- A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors.Nature communications · 2020Article
- Progress toward sourcing plants for new bioconjugation tools: a screening evaluation of a model peptide ligase using a synthetic precursor.3 Biotech · 2019Article
- Site-Specific Sequential Protein Labeling Catalyzed by a Single Recombinant Ligase.Journal of the American Chemical Society · 2019Article
- A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein.Scientific reports · 2019Article
- Structural determinants for peptide-bond formation by asparaginyl ligases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Legumain is a dual-function protease-peptide ligase whose activities are of great interest to researchers studying plant physiology and to biotechnological applications. However, the molecular mechanisms determining the specificities for proteolysis and ligation are unclear because structural information on the substrate recognition by a fully activated plant legumain is unavailable. Here, we present the X-ray structure of
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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.