Evidence map›Paper›PMID 10527927›Full record

ReviewThe Biochemical journal1999

The malonyl-CoA-long-chain acyl-CoA axis in the maintenance of mammalian cell function.

V A Zammit

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 107 citations in OpenAlex.

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  14. The Randle cycle revisited: a new head for an old hat.American journal of physiology. Endocrinology and metabolism · 2009
    Review
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  20. Specificity of activation by phosphoinositides determines lipid regulation of Kir channels.Proceedings of the National Academy of Sciences of the United States of America · 2003
    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

1 author at 1 institution in 1 country.

V A ZammitCell Biochemistry, Hannah Research Institute, Ayr, KA6 5HL, Scotland, U.K. zammitv@hri.sari.ac.uk
Hannah Research Foundation · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Long-chain acyl-CoA esters have potent specific actions (e.g. on gene transcription, membrane trafficking) as well as non-specific ones (e.g. on phospholipid bilayers). They are synthesized on the cytosolic aspects of several intracellular membranes, to give rise to (a) cytosolic pool(s) to which a variety of enzymes and processes have access, including some localized in the nucleus. Their concentration in cells is highly regulated, interconversion with corresponding acylcarnitines being the most important mechanism involved. This reaction is catalysed by cytosol-accessible carnitine long-chain acyl (palmitoyl) transferase activities that are themselves located on multiple membrane systems. Regulation of these activities is through the inhibitory action of malonyl-CoA. Hence the existence of a potent malonyl-CoA-acyl-CoA axis through which many processes involved in the maintenance of mammalian cell function are regulated. The molecular, topographical and physiological interactions that make this possible are described and discussed.

Indexed as

Cell Physiological PhenomenaAcyl Coenzyme AAnimalsCarnitine O-PalmitoyltransferaseCytosolMalonyl Coenzyme AMammalsAcyl Coenzyme ACarnitine O-PalmitoyltransferaseMalonyl Coenzyme A

Identifiers

PMID10527927
PMCPMC1220580
OpenAlexW2062644914

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.