Evidence map›Paper›PMID 31330798›Full record

ArticleToxins2019

The Dual α-Amidation System in Scorpion Venom Glands.

Gustavo Delgado-Prudencio, Lourival D Possani, Baltazar Becerril, Ernesto Ortiz

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Quantitative analysis of growth and diversification in venom data using database metrics.Database : the journal of biological databases and curation · 2026
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. An overview of some enzymes from buthid scorpion venoms from Colombia:The journal of venomous animals and toxins including tropical diseases · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Production, composition, and mode of action of the painful defensive venom produced by a limacodid caterpillar,Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Gustavo Delgado-PrudencioDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico.
Lourival D PossaniDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico.ORCID 0000-0001-6357-2661
Baltazar BecerrilDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico.
Ernesto OrtizDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos 62210, Mexico. erne@ibt.unam.mx.ORCID 0000-0002-8713-0224
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many peptides in scorpion venoms are amidated at their C-termini. This post-translational modification is paramount for the correct biological function of ion channel toxins and antimicrobial peptides, among others. The discovery of canonical amidation sequences in transcriptome-derived scorpion proproteins suggests that a conserved enzymatic α-amidation system must be responsible for this modification of scorpion peptides. A transcriptomic approach was employed to identify sequences putatively encoding enzymes of the α-amidation pathway. A dual enzymatic α-amidation system was found, consisting of the membrane-anchored, bifunctional, peptidylglycine α-amidating monooxygenase (PAM) and its paralogs, soluble monofunctional peptidylglycine α-hydroxylating monooxygenase (PHM

Indexed as

Amidine-LyasesAnimalsCarboxypeptidase HExocrine GlandsMixed Function OxygenasesMultienzyme ComplexesProprotein ConvertasesProtein Processing, Post-TranslationalScorpionsScorpion VenomsAmidine-LyasesCarboxypeptidase HMixed Function OxygenasesMultienzyme Complexespeptidylamidoglycolate lyasepeptidylglycine monooxygenaseProprotein ConvertasesScorpion Venomsamidationevolutionposttranslational modificationsscorpiontranscriptomics

Identifiers

PMID31330798
PMCPMC6669573
OpenAlexW2963653689

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.