Evidence map›Paper›PMID 9671452›Full record

ArticleMolecular and cellular biology1998

A sequence-specific RNA-binding protein complements apobec-1 To edit apolipoprotein B mRNA.

A Mehta, D M Driscoll

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. 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
2.6field-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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
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  3. Review
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  6. Identification of DNA cleavage- and recombination-specific hnRNP cofactors for activation-induced cytidine deaminase.Proceedings of the National Academy of Sciences of the United States of America · 2015
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  7. Article
  8. Detection of RNA-Protein Interactions Using Tethered RNA Affinity Capture.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  9. Article
  10. Article
  11. Article
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  16. A site-specific factor interacts directly with its cognate RNA editing site in chloroplast transcripts.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
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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

2 authors at 1 institution in 1 country.

A MehtaDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
D M Driscoll
Cleveland Clinic · US

Funding

YILMA SIV VACCINIA VACCINE TRIALP51RR000166 · NCRR · UNIVERSITY OF WASHINGTON · PI DACEY, DENNIS MICHAEL · 1985 to 2011
$161.1M
EDITING OF APOLIPOPROTEIN-B MRNAR01HL045478 · NHLBI · CLEVELAND CLINIC LERNER COL/MED-CWRU · PI DRISCOLL, DONNA M · 1996 to 2004
$1.2M
EDITING OF APOLIPOPROTEIN B MRNAR29HL045478 · NHLBI · SOUTHWEST FOUNDATION FOR BIOMEDICAL RES · PI DRISCOLL, DONNA M · 1991 to 1995
–
NCRR NIH HHS P51 RR000166NCRR NIH HHS RR00166NHLBI NIH HHS HL-45478NHLBI NIH HHS R01 HL045478
6 · The paper itself

Abstract

The editing of apolipoprotein B (apo-B) mRNA involves the site-specific deamination of cytidine to uracil. The specificity of editing is conferred by an 11-nucleotide mooring sequence located downstream from the editing site. Apobec-1, the catalytic subunit of the editing enzyme, requires additional proteins to edit apo-B mRNA in vitro, but the function of these additional factors, known as complementing activity, is not known. Using RNA affinity chromatography, we show that the complementing activity binds to a 280-nucleotide apo-B RNA in the absence of apobec-1. The activity did not bind to the antisense strand or to an RNA with three mutations in the mooring sequence. The eluate from the wild-type RNA column contained a 65-kDa protein that UV cross-linked to apo-B mRNA but not to the triple-mutant RNA. This protein was not detected in the eluates from the mutant or the antisense RNA columns. Introduction of the mooring sequence into luciferase RNA induced cross-linking of the 65-kDa protein. A 65-kDa protein that interacted with apobec-1 was also detected by far-Western analysis in the eluate from the wild-type RNA column but not from the mutant RNA column. For purification, proteins were precleared on the mutant RNA column prior to chromatography on the wild-type RNA column. Silver staining of the affinity-purified fraction detected a single prominent protein of 65 kDa. Our results suggest that the complementing activity may function as the RNA-binding subunit of the holoenzyme.

Indexed as

RNA EditingAICDA (Activation-Induced Cytidine Deaminase)AnimalsAPOBEC-1 DeaminaseApolipoprotein B-100Apolipoproteins BChromatography, AffinityCross-Linking ReagentsCytidine DeaminaseRatsRNA-Binding ProteinsRNA, MessengerStructure-Activity RelationshipAICDA (Activation-Induced Cytidine Deaminase)APOBEC-1 DeaminaseApobec1 protein, ratApolipoprotein B-100Apolipoproteins BCross-Linking ReagentsCytidine DeaminaseRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID9671452
PMCPMC109028
OpenAlexW2116975717

What Socratic 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 Socratic graph.