Evidence map›Paper›PMID 18077827›Full record

ReviewJournal of lipid research2008

Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes.

Michael Schlame

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 192 papers.

0numbers the graph read from it
0cells of the map it votes in
192citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

192 citing papers in PubMed, 382 citations in OpenAlex.

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  16. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  17. Article
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  19. Review
  20. Review

132 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

1 author at 1 institution in 1 country.

Michael SchlameDepartment of Anesthesiology and Cell Biology, New York University School of Medicine, New York, NY 10016, USA. michael.schlame@med.nyu.edu
New York University · US

Funding

Molecular Mechanism of Barth SyndromeR01HL078788 · NHLBI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SCHLAME, MICHAEL · 2006 to 2009
$1.5M
NHLBI NIH HHS R01 HL 078788NHLBI NIH HHS R01 HL078788
6 · The paper itself

Abstract

In this article, the formation of prokaryotic and eukaryotic cardiolipin is reviewed in light of its biological function. I begin with a detailed account of the structure of cardiolipin, its stereochemistry, and the resulting physical properties, and I present structural analogs of cardiolipin that occur in some organisms. Then I continue to discuss i) the de novo formation of cardiolipin, ii) its acyl remodeling, iii) the assembly of cardiolipin into biological membranes, and iv) the degradation of cardiolipin, which may be involved in apoptosis and mitochondrial fusion. Thus, this article covers the entire metabolic cycle of this unique phospholipid. It is shown that mitochondria produce cardiolipin species with a high degree of structural uniformity and molecular symmetry, among which there is often a dominant form with four identical acyl chains. The subsequent assembly of cardiolipin into functional membranes is largely unknown, but the analysis of crystal structures of membrane proteins has revealed a first glimpse into the underlying principles of cardiolipin-protein interactions. Disturbances of cardiolipin metabolism are crucial in the pathophysiology of human Barth syndrome and perhaps also play a role in diabetes and ischemic heart disease.

Indexed as

AcyltransferasesAmino Acid SequenceAnimalsBacteriaCardiolipinsCell MembraneHumansMembrane ProteinsMitochondrial MembranesMolecular Sequence DataPhospholipase DPhospholipases ASequence AlignmentTranscription FactorsTransferases (Other Substituted Phosphate Groups)AcyltransferasesCardiolipinscardiolipin synthetaseMembrane ProteinsPhospholipase DPhospholipases ATAFAZZIN protein, humanTranscription FactorsTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID18077827
PMCPMC2444000
OpenAlexW2077637487

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.