Evidence map›Paper›PMID 8093000›Full record

ArticleThe Biochemical journal1994

Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size.

J Knudsen, N J Faergeman, H Skøtt, R Hummel, C Børsting, T M Rose, J S Andersen, P Højrup, P Roepstorff, K Kristiansen

Abstract readComparative Study
In one paragraph

Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

35 citing papers in PubMed, 105 citations in OpenAlex.

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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 1 institution in 1 country.

J KnudsenInstitute of Biochemistry, Odense University, Denmark.
N J Faergeman
H Skøtt
R Hummel
C Børsting
T M Rose
J S Andersen
P Højrup
P Roepstorff
K Kristiansen
Program for Appropriate Technology in Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acyl-CoA-binding protein (ACBP) is a 10 kDa protein characterized in vertebrates. We have isolated two ACBP homologues from the yeast Saccharomyces carlsbergensis, named yeast ACBP types 1 and 2. Both proteins contain 86 amino acid residues and are identical except for four conservative substitutions. In comparison with human ACBP, yeast ACBPs exhibit 48% (type 1) and 49% (type 2) conservation of amino acid residues. The amino acid sequence of S. carlsbergensis ACBP type 1 was found to be identical with the one ACBP present in Saccharomyces cerevisiae. A recombinant form of this protein was expressed in Escherichia coli and S. cerevisiae, purified, and its acyl-CoA-binding properties were characterized by isoelectric focusing and microcalorimetric analyses. The yeast ACBP was found to bind acyl-CoA esters with high affinity (Kd 0.55 x 10(-10) M). Overexpression of yeast ACBP in S. cerevisiae resulted in a significant expansion of the intracellular acyl-CoA pool. Finally, Southern-blotting analysis of the two genes encoding ACBP types 1 and 2 in S. carlsbergensis strongly indicated that this species is a hybrid between S. cerevisiae and Saccharomyces monacensis.

Indexed as

Acyl Coenzyme AAmino Acid SequenceBase SequenceBlotting, SouthernCalorimetryCarrier ProteinsDiazepam Binding InhibitorElectron Spin Resonance SpectroscopyElectrophoresis, Polyacrylamide GelEscherichia coliGenes, FungalGenome, FungalHumansIsoelectric PointMass SpectrometryMolecular Sequence DataAcyl Coenzyme ACarrier ProteinsDiazepam Binding InhibitorRecombinant Proteins

Identifiers

PMID8093000
PMCPMC1137253
OpenAlexW2242477415

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.