Evidence mapPaperPMID 2312735Full record

ArticleThe Journal of clinical investigation1990

Familial hypobetalipoproteinemia caused by a mutation in the apolipoprotein B gene that results in a truncated species of apolipoprotein B (B-31). A unique mutation that helps to define the portion of the apolipoprotein B molecule required for the formation of buoyant, triglyceride-rich lipoproteins.

S G Young, S T Hubl, R S Smith, S M Snyder, J F Terdiman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
15.8field-weighted citation impact, top 1% 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

13 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
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  7. Article
  8. Targeted modification of the apolipoprotein B gene results in hypobetalipoproteinemia and developmental abnormalities in mice.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
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  12. Expression, secretion, and lipid-binding characterization of the N-terminal 17% of apolipoprotein B.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
  13. 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

5 authors at 1 institution in 1 country.

S G YoungGladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140.
S T Hubl
R S Smith
S M Snyder
J F Terdiman
Gladstone Institutes · US

Funding

STRUCTURAL AND PHYSICAL BIOCHEMICAL ANALYSIS OF APOLIPOPROTEIN EP01HL041633 · J. DAVID GLADSTONE INSTITUTES · 1989 to 2003
$8.5M
NHLBI NIH HHS HL-01672NHLBI NIH HHS HL-41633
6 · The paper itself

Abstract

Apolipoprotein B-100 has a crucial structural role in the formation of VLDL and LDL. Familial hypobetalipoproteinemia, a syndrome in which the concentration of LDL cholesterol in plasma is abnormally low, can be caused by mutations in the apo B gene that prevent the translation of a full-length apo B-100 molecule. Prior studies have revealed that truncated species of apo B [e.g., apo B-37 (1728 amino acids), apo B-46 (2057 amino acids)] can occasionally be identified in the plasma of subjects with familial hypobetalipoproteinemia; in each of these cases, the truncated apo B species has been a prominent protein component of VLDL. In this report, we describe a kindred with hypobetalipoproteinemia in which the plasma of four affected heterozygotes contained a unique truncated apo B species, apo B-31. Apolipoprotein B-31 is caused by the deletion of a single nucleotide in the apo B gene, and it is predicted to contain 1425 amino acids. Apolipoprotein B-31 is the shortest of the mutant apo B species to be identified in the plasma of a subject with hypobetalipoproteinemia. In contrast to longer truncated apo B species, apo B-31 was undetectable in the VLDL and the LDL; however, it was present in the HDL fraction and the lipoprotein-deficient fraction of plasma. The density distribution of apo B-31 in the plasma suggests the possibility that the amino-terminal 1425 amino acids of apo B-100 are sufficient to permit the formation and secretion of small, dense lipoproteins but are inadequate to support the formation of the more lipid-rich VLDL and LDL particles.

Indexed as

AdultAgedApolipoproteins BFemaleHeterozygoteHumansHypobetalipoproteinemiasHypolipoproteinemiasLipoproteinsMaleMiddle AgedMutationTriglyceridesApolipoproteins BLipoproteinsTriglycerides

Identifiers

PMID2312735
PMCPMC296513
OpenAlexW2169420530

What Socratic holds

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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 Socratic graph.