Evidence map›Paper›PMID 21303393›Full record

ReviewFEMS microbiology reviews2011

Phosphoethanolamine methyltransferases in phosphocholine biosynthesis: functions and potential for antiparasite therapy.

April M Bobenchik, Yoann Augagneur, Bing Hao, Jeffrey C Hoch, Choukri Ben Mamoun

Open access · bronzeAbstract readReview
In one paragraph

Review in FEMS microbiology reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.4field-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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. A Dual, Systematic Approach to Malaria Diagnostic Biomarker Discovery.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2022
    Pooled it
  2. Article
  3. Article
  4. An Introduction to Spiral Steroids.International journal of molecular sciences · 2022
    Review
  5. Adapt or Die: Targeting Unique Transmission-Stage Biology for Malaria Elimination.Frontiers in cellular and infection microbiology · 2022
    Review
  6. Article
  7. Mosquito metabolomics reveal that dengue virus replication requires phospholipid reconfiguration via the remodeling cycle.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Reduction of Sphingosine Kinase 1 Phosphorylation and Activity inFrontiers in cell and developmental biology · 2020
    Article
  10. Article
  11. Article
  12. Review
  13. Biochemical and genetic analyses of N metabolism in maize testcross seedlings: 2. Roots.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

April M BobenchikDepartment of Internal Medicine, Yale University School of Medicine, New Haven, CT 06510-3221, USA.
Yoann Augagneur
Bing Hao
Jeffrey C Hoch
Choukri Ben Mamoun
University of Connecticut · USYale University · US

Funding

Nucleoside Transporters of Plasmodium falciparumR01AI051507 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI ULLMAN, BUDDY · 2003 to 2007
$1.7M
NIAID NIH HHS AI51507NIAID NIH HHS R01 AI051507
6 · The paper itself

Abstract

S-adenosyl-L-methionine (SAM)-dependent methyltransferases represent a diverse group of enzymes that catalyze the transfer of a methyl group from a methyl donor SAM to nitrogen, oxygen, sulfur or carbon atoms of a large number of biologically active large and small molecules. These modifications play a major role in the regulation of various biological functions such as gene expression, signaling, nuclear division and metabolism. The three-step SAM-dependent methylation of phosphoethanolamine to form phosphocholine catalyzed by phosphoethanolamine N-methyltransferases (PMTs) has emerged as an important biochemical step in the synthesis of the major phospholipid, phosphatidylcholine, in some eukaryotes. PMTs have been identified in nematodes, plants, African clawed frogs, zebrafish, the Florida lancelet, Proteobacteria and human malaria parasites. Data accumulated thus far suggest an important role for these enzymes in growth and development. This review summarizes published studies on the biochemical and genetic characterization of these enzymes, and discusses their evolution and their suitability as targets for the development of therapies against parasitic infections, as well as in bioengineering for the development of nutritional and stress-resistant plants.

Indexed as

Amino Acid SequenceAnimalsAntiparasitic AgentsBioengineeringCaenorhabditisDrug DiscoveryEvolution, MolecularGenome, ArchaealHumansMethyltransferasesPhosphatidylcholinesPhosphatidylethanolaminesPhosphorylcholinePhylogenyPlasmodiumSequence AlignmentAntiparasitic AgentsMethyltransferasesPhosphatidylcholinesPhosphatidylethanolaminesphosphoethanolamine methyltransferasePhosphorylcholine

Identifiers

PMID21303393
PMCPMC4107886
OpenAlexW2115357182

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.