Evidence map›Paper›PMID 32221295›Full record

ArticleNature communications2020

A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors.

Junqiao Du, Kuok Yap, Lai Yue Chan, Fabian B H Rehm, Fong Yang Looi, Aaron G Poth, Edward K Gilding, Quentin Kaas, Thomas Durek, David J Craik

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Metabolite Mediated Protein Macrocyclization.Synlett : accounts and rapid communications in synthetic organic chemistry · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Junqiao DuInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0003-3790-2975
Kuok YapInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0002-9409-5287
Lai Yue ChanInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0002-9346-2487
Fabian B H RehmInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0003-2508-8582
Fong Yang LooiInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.
Aaron G PothInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0002-1497-8347
Edward K GildingInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0003-1720-1282
Quentin KaasInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia.ORCID http://orcid.org/0000-0001-9988-6152
Thomas DurekInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia. t.durek@imb.uq.edu.au.
David J CraikInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, 4072, Australia. d.craik@imb.uq.edu.au.ORCID http://orcid.org/0000-0003-0007-6796
The University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Asparaginyl endopeptidases (AEPs) catalyze the key backbone cyclization step during the biosynthesis of plant-derived cyclic peptides. Here, we report the identification of two AEPs from Momordica cochinchinensis and biochemically characterize MCoAEP2 that catalyzes the maturation of trypsin inhibitor cyclotides. Recombinantly produced MCoAEP2 catalyzes the backbone cyclization of a linear cyclotide precursor (MCoTI-II-NAL) with a k

Indexed as

BiocatalysisAmino Acid SequenceAsparaginyl EndopeptidaseCyclizationCysteine EndopeptidasesHydrogen-Ion ConcentrationKineticsModels, MolecularPeptides, CyclicPlant ProteinsProtein EngineeringRecombinant ProteinsSubstrate SpecificityTrypsin InhibitorsAsparaginyl EndopeptidaseCysteine EndopeptidasesPeptides, CyclicPlant ProteinsRecombinant ProteinsTrypsin Inhibitors

Identifiers

PMID32221295
PMCPMC7101308
OpenAlexW3013178722

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.