Evidence map›Paper›PMID 11992265›Full record

ArticleAmerican journal of human genetics2002

Reinvestigation of peroxisomal 3-ketoacyl-CoA thiolase deficiency: identification of the true defect at the level of d-bifunctional protein.

S Ferdinandusse, E G van Grunsven, W Oostheim, S Denis, E M Hogenhout, L IJlst, C W T van Roermund, H R Waterham, S Goldfischer, R J A Wanders

Open access · bronzeAbstract read
In one paragraph

Article in American journal of human genetics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Mechanisms of disease: Inborn errors of bile acid synthesis.Nature clinical practice. Gastroenterology & hepatology · 2008
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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

10 authors at 3 institutions in 2 countries.

S FerdinandusseDepartment of Clinical Chemistry, Emma Children's Hospital, Academic Medical Center, University of Amsterdam, 1100 DE Amsterdam, The Netherlands.
E G van Grunsven
W Oostheim
S Denis
E M Hogenhout
L IJlst
C W T van Roermund
H R Waterham
S Goldfischer
R J A Wanders
University of Amsterdam · NLAmsterdam UMC Location University of Amsterdam · NLAlbert Einstein College of Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this report, we reinvestigate the only patient ever reported with a deficiency of peroxisomal 3-ketoacyl-CoA thiolase (THIO). At the time when they were described, the abnormalities in this patient, which included accumulation of very-long-chain fatty acids and the bile-acid intermediate trihydroxycholestanoic acid, were believed to be the logical consequence of a deficiency of the peroxisomal beta-oxidation enzyme THIO. In light of the current knowledge of the peroxisomal beta-oxidation system, however, the reported biochemical aberrations can no longer be explained by a deficiency of this thiolase. In this study, we show that the true defect in this patient is at the level of d-bifunctional protein (DBP). Immunoblot analysis revealed the absence of DBP in postmortem brain of the patient, whereas THIO was normally present. In addition, we found that the patient had a homozygous deletion of part of exon 3 and intron 3 of the DBP gene, resulting in skipping of exon 3 at the cDNA level. Our findings imply that the group of single-peroxisomal beta-oxidation-enzyme deficiencies is limited to straight-chain acyl-CoA oxidase, DBP, and alpha-methylacyl-CoA racemase deficiency and that there is no longer evidence for the existence of THIO deficiency as a distinct clinical entity.

Indexed as

17-Hydroxysteroid DehydrogenasesEnoyl-CoA Hydratase3-Hydroxyacyl CoA DehydrogenasesAcetyl-CoA C-AcyltransferaseAmino Acid SequenceBlotting, WesternBrainExonsFibroblastsHumansHydro-LyasesIntronsKidneyMultienzyme ComplexesPeroxisomal Multifunctional Protein-2Peroxisomes17-Hydroxysteroid Dehydrogenases3-Hydroxyacyl CoA DehydrogenasesAcetyl-CoA C-AcyltransferaseEnoyl-CoA HydrataseHSD17B4 protein, humanHydro-LyasesMultienzyme ComplexesPeroxisomal Multifunctional Protein-2

Identifiers

PMID11992265
PMCPMC379147
OpenAlexW2044392113

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.