Evidence map›Paper›PMID 3680528›Full record

ArticleThe Journal of clinical investigation1987

Structural relationship of human apolipoprotein B48 to apolipoprotein B100.

T L Innerarity, S G Young, K S Poksay, R W Mahley, R S Smith, R W Milne, Y L Marcel, K H Weisgraber

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of clinical investigation, 1987. 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
2.7field-weighted citation impact, top 9% 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, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Reading-frame restoration with an apolipoprotein B gene frameshift mutation.Proceedings of the National Academy of Sciences of the United States of America · 1992
    Article
  8. Article
  9. Article
  10. Correlation Between theClinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis
    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

8 authors at 1 institution in 2 countries.

T L InnerarityGladstone Foundation Laboratories for Cardiovascular Disease, Department of Pathology, University of California, San Francisco 94140.
S G Young
K S Poksay
R W Mahley
R S Smith
R W Milne
Y L Marcel
K H Weisgraber
Gladstone Institutes · US

Funding

TRANSCRIPTIONAL CONTROL OF GENES INVOLVED IN LDL MODIFICATION AND CATABOLISMP50HL014197 · NHLBI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI WITZTUM, JOSEPH L · 1985 to 1997
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FUNCTIONAL DOMAINS OF HUMAN APOLIPOPROTEIN BR01HL036701 · NHLBI · J. DAVID GLADSTONE INSTITUTES · PI RALL, STANLEY C · 1986 to 1988
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NHLBI NIH HHS HL-14197NHLBI NIH HHS HL-36701
6 · The paper itself

Abstract

Although the complete amino acid sequence of human apolipoprotein (apo) B100 is known (4536 amino acids), the structure of apo B48 has not been defined. The objective of our study was to define the structure of apo B48 and its relationship to apo B100. Antibodies were produced against 22 synthetic peptides corresponding to sequences in human apo B100. The levels of immunoreactivity of the antipeptides to apo B100 and apo B48 were used to define the structural relationship between these two species of apo B. Six antibodies from sequences in the amino-terminal half of apo B100, including antipeptide 2110-2129, bound to both apo B100 and apo B48. 15 other apo B-specific antipeptides from sequences carboxyl-terminal to residue 2152 bound to apo B100, but not to apo B48. Immunoblots of cyanogen bromide digests of apo B100 and apo B48 with antipeptides 2068-2091 and 2110-2129 detected a 16-KD fragment (residues 2016-2151) in the apo B100 digest and a fragment of identical size in the apo B48 digest. Because apo B48 appears to contain the apo B100 cyanogen bromide fragment 2016-2151 and because an antiserum specific for the peptide 2152-2168 does not bind to apo B48, we conclude that apo B48 represents the amino-terminal 47% of apo B100 and that the carboxyl terminus of apo B48 is in the vicinity of residue 2151 of apo B100.

Indexed as

Apolipoproteins BAmino AcidsApolipoprotein B-100Apolipoprotein B-48HumansAmino AcidsApolipoprotein B-100Apolipoprotein B-48Apolipoproteins B

Identifiers

PMID3680528
PMCPMC442455
OpenAlexW2053109324

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.