Evidence map›Paper›PMID 20564017›Full record

ReviewBiopolymers2010

Ribosomal biosynthesis of the cyclic peptide toxins of Amanita mushrooms.

Jonathan D Walton, Heather E Hallen-Adams, Hong Luo

Open access · greenAbstract readReview
In one paragraph

Review in Biopolymers, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Review
  3. Subcellular localization of fungal specialized metabolites.Fungal biology and biotechnology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. A Convergent Total Synthesis of the Death Cap Toxin α-Amanitin.Angewandte Chemie (International ed. in English) · 2020
    Article
  9. Review
  10. Article
  11. The Biosynthesis of Heterophyllin B inFrontiers in plant science · 2019
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Biosynthetic investigation of phomopsins reveals a widespread pathway for ribosomal natural products in Ascomycetes.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. 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

3 authors at 1 institution in 1 country.

Jonathan D WaltonDepartment of Energy Plant Research Laboratory, Michigan State University, E. Lansing, MI 48824, USA. walton@msu.edu
Heather E Hallen-Adams
Hong Luo
Michigan State University · US

Funding

BIOSYNTHESIS OF THE CYCLIC PEPTIDE TOXINS OF AMANITA MUSHROOMSR01GM088274 · NIGMS · MICHIGAN STATE UNIVERSITY · PI WALTON, JONATHAN · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM088274
6 · The paper itself

Abstract

Some species of mushrooms in the genus Amanita are extremely poisonous and frequently fatal to mammals including humans and dogs. Their extreme toxicity is due to amatoxins such as alpha- and beta-amanitin. Amanita mushrooms also biosynthesize a chemically related group of toxins, the phallotoxins, such as phalloidin. The amatoxins and phallotoxins (collectively known as the Amanita toxins) are bicyclic octa- and heptapeptides, respectively. Both contain an unusual Trp-Cys crossbridge known as tryptathionine. We have shown that, in Amanita bisporigera, the amatoxins and phallotoxins are synthesized as proproteins on ribosomes and not by nonribosomal peptide synthetases. The proproteins are 34-35 amino acids in length and have no predicted signal peptides. The genes for alpha-amanitin (AMA1) and phallacidin (PHA1) are members of a large family of related genes, characterized by highly conserved amino acid sequences flanking a hypervariable "toxin" region. The toxin regions are flanked by invariant proline (Pro) residues. An enzyme that could cleave the proprotein of phalloidin was purified from the phalloidin-producing lawn mushroom Conocybe apala. The enzyme is a serine protease in the prolyl oligopeptidase (POP) subfamily. The same enzyme cuts at both Pro residues to release the linear hepta- or octapeptide.

Indexed as

Protein BiosynthesisAgaricalesAmanitinsAmino Acid SequenceAnimalsHumansMolecular Sequence DataMolecular StructurePeptides, CyclicPoisonsProtein PrecursorsAmanitinsPeptides, CyclicPoisonsProtein Precursors

Identifiers

PMID20564017
PMCPMC4001729
OpenAlexW2000568253

What OpenQuestion holds

Textmetadata
LicenceTDM
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.