Evidence map›Paper›PMID 30944220›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Papain-like cysteine proteases prepare plant cyclic peptide precursors for cyclization.

Fabian B H Rehm, Mark A Jackson, Ewout De Geyter, Kuok Yap, Edward K Gilding, Thomas Durek, David J Craik

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.5field-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

30 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Use of a head-to-tail peptide cyclase to prepare hybrid RiPPs.Chemical communications (Cambridge, England) · 2024
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Enzymatic C-to-C Protein Ligation.Angewandte Chemie (International ed. in English) · 2022
    Article
  16. Structure determinants defining the specificity of papain-like cysteine proteases.Computational and structural biotechnology journal · 2022
    Review
  17. Article
  18. Article
  19. Review
  20. Plant derived cyclic peptides.Biochemical Society transactions · 2021
    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

7 authors at 1 institution in 1 country.

Fabian B H RehmInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0003-2508-8582
Mark A JacksonInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Ewout De GeyterInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Kuok YapInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Edward K GildingInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Thomas DurekInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia t.durek@imb.uq.edu.au d.craik@imb.uq.edu.au.ORCID 0000-0003-0686-227X
David J CraikInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia t.durek@imb.uq.edu.au d.craik@imb.uq.edu.au.ORCID 0000-0003-0007-6796
The University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclotides are plant defense peptides that have been extensively investigated for pharmaceutical and agricultural applications, but key details of their posttranslational biosynthesis have remained elusive. Asparaginyl endopeptidases are crucial in the final stage of the head-to-tail cyclization reaction, but the enzyme(s) involved in the prerequisite steps of N-terminal proteolytic release were unknown until now. Here we use activity-guided fractionation to identify specific members of papain-like cysteine proteases involved in the N-terminal cleavage of cyclotide precursors. Through both characterization of recombinantly produced enzymes and

Indexed as

CyclotidesCysteine ProteasesPapainPlant ProteinsDefensinsModels, MolecularCyclotidesCysteine ProteasesDefensinsPapainPlant Proteinscyclotidekalata B1papain-like cysteine proteaseplant defensinsRiPP biosynthesis

Identifiers

PMID30944220
PMCPMC6475389
OpenAlexW2931364513

What OpenQuestion holds

Textmetadata
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.