Evidence map›Paper›PMID 31123145›Full record

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

Structural determinants for peptide-bond formation by asparaginyl ligases.

Xinya Hemu, Abbas El Sahili, Side Hu, Kaho Wong, Yu Chen, Yee Hwa Wong, Xiaohong Zhang, Aida Serra, Boon Chong Goh, Dina A Darwis and 5 more

Open access · bronzeAbstract 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 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  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. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Vacuolar Processing Enzymes in Plant Programmed Cell Death and Autophagy.International journal of molecular sciences · 2023
    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

15 authors at 1 institution in 1 country.

Xinya HemuSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.ORCID 0000-0003-1979-5854
Abbas El SahiliSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.ORCID 0000-0003-3973-686X
Side HuSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Kaho WongSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Yu ChenSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Yee Hwa WongSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Xiaohong ZhangSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Aida SerraSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.ORCID 0000-0002-4017-1096
Boon Chong GohNTU Institute of Structural Biology, Nanyang Technological University, 636921 Singapore.
Dina A DarwisSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Ming Wei ChenSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Siu Kwan SzeSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Chuan-Fa LiuSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore.
Julien LescarSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore; julien@ntu.edu.sg jptam@ntu.edu.sg.ORCID 0000-0002-9623-8130
James P TamSchool of Biological Sciences, Nanyang Technological University, 637551 Singapore; julien@ntu.edu.sg jptam@ntu.edu.sg.ORCID 0000-0003-4433-198X
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Asparaginyl endopeptidases (AEPs) are cysteine proteases which break Asx (Asn/Asp)-Xaa bonds in acidic conditions. Despite sharing a conserved overall structure with AEPs, certain plant enzymes such as butelase 1 act as a peptide asparaginyl ligase (PAL) and catalyze Asx-Xaa bond formation in near-neutral conditions. PALs also serve as macrocyclases in the biosynthesis of cyclic peptides. Here, we address the question of how a PAL can function as a ligase rather than a protease. Based on sequence homology of butelase 1, we identified AEPs and PALs from the cyclic peptide-producing plants

Indexed as

Asparaginyl EndopeptidaseCysteine EndopeptidasesLigasesMutagenesisPeptides, CyclicPlant ProteinsViolaceaeAsparaginyl EndopeptidaseCysteine EndopeptidasesLigasesPeptides, CyclicPlant Proteinsdata miningligase-activity determinantpeptide ligase

Identifiers

PMID31123145
PMCPMC6576118
OpenAlexW2946803285

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.