Evidence map›Paper›PMID 18369234›Full record

ReviewJournal of lipid research2008

Thematic review series: Glycerolipids. Acyltransferases in bacterial glycerophospholipid synthesis.

Yong-Mei Zhang, Charles O Rock

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
  2. Adaptive laboratory evolution ofFrontiers in microbiology · 2026
    Article
  3. Review
  4. Two putativeMicrobiology (Reading, England) · 2025
    Article
  5. Microbiology (Reading, England) · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Acylation of glycerolipids in mycobacteria.Nature communications · 2023
    Article
  10. Article
  11. RSC advances · 2023
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Decoding allosteric regulation by the acyl carrier protein.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  20. Article

8 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Yong-Mei ZhangDepartment of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. yongmei.zhang@stjude.org
Charles O Rock
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
REGULATION OF LIPID METABOLISM IN E COLIR01GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 1985 to 2022
$9.2M
REGULATION OF LIPID METABOLISM IN BACTERIAR37GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 2001 to 2010
$5.7M
NCI NIH HHS CA 21765NCI NIH HHS P30 CA021765NIGMS NIH HHS GM 34496NIGMS NIH HHS R01 GM034496NIGMS NIH HHS R37 GM034496
6 · The paper itself

Abstract

Phospholipid biosynthesis is a vital facet of bacterial physiology that begins with the synthesis of the fatty acids by a soluble type II fatty acid synthase. The bacterial glycerol-phosphate acyltransferases utilize the completed fatty acid chains to form the first membrane phospholipid and thus play a critical role in the regulation of membrane biogenesis. The first bacterial acyltransferase described was PlsB, a glycerol-phosphate acyltransferase. PlsB is a key regulatory point that coordinates membrane phospholipid formation with cell growth and macromolecular synthesis. Phosphatidic acid is then produced by PlsC, a 1-acylglycerol-phosphate acyltransferase. These two acyltransferases use thioesters of either CoA or acyl carrier protein (ACP) as the acyl donors and have homologs that perform the same reactions in higher organisms. However, the most prevalent glycerol-phosphate acyltransferase in the bacterial world is PlsY, which uses a recently discovered acyl-phosphate fatty acid intermediate as an acyl donor. This unique activated fatty acid is formed from the acyl-ACP end products of the fatty acid biosynthetic pathway by PlsX, an acyl-ACP:phosphate transacylase.

Indexed as

1-Acylglycerol-3-Phosphate O-AcyltransferaseAcetyltransferasesAcyl Carrier ProteinAcyltransferasesBacteriaBacterial ProteinsEscherichia coli ProteinsFatty Acid Synthase, Type IIGlycerol-3-Phosphate O-AcyltransferaseGlycerophospholipidsPhylogeny1-Acylglycerol-3-Phosphate O-AcyltransferaseAcetyltransferasesAcyl Carrier ProteinAcyltransferasesBacterial ProteinsEscherichia coli ProteinsFatty Acid Synthase, Type IIGlycerol-3-Phosphate O-AcyltransferaseGlycerophospholipidsPlsB protein, E coliplsC protein, E coliplsX protein, bacteria

Identifiers

PMID18369234
PMCPMC2515527
OpenAlexW2044483591

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.