Evidence map›Paper›PMID 10669759›Full record

ArticleMolecular and cellular biology2000

Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA.

A Mehta, M T Kinter, N E Sherman, D M Driscoll

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
9.6field-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

105 citing papers in PubMed, 257 citations in OpenAlex.

  1. Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026
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  19. Curcumin modulates the apolipoprotein B mRNA editing by coordinating the expression of cytidine deamination to uridine editosome components in primary mouse hepatocytes.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2019
    Article
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45 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

A MehtaDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
M T Kinter
N E Sherman
D M Driscoll
Cleveland Clinic · USIONICS Mass Spectrometry (Canada) · CA

Funding

YILMA SIV VACCINIA VACCINE TRIALP51RR000166 · NCRR · UNIVERSITY OF WASHINGTON · PI HU, SHIU-LOK · 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 HL45478NHLBI NIH HHS R01 HL045478
6 · The paper itself

Abstract

The C-to-U editing of apolipoprotein B (apo-B) mRNA is catalyzed by a multiprotein complex that recognizes an 11-nucleotide mooring sequence downstream of the editing site. The catalytic subunit of the editing enzyme, apobec-1, has cytidine deaminase activity but requires additional unidentified proteins to edit apo-B mRNA. We purified a 65-kDa protein that functionally complements apobec-1 and obtained peptide sequence information which was used in molecular cloning experiments. The apobec-1 complementation factor (ACF) cDNA encodes a novel 64.3-kDa protein that contains three nonidentical RNA recognition motifs. ACF and apobec-1 comprise the minimal protein requirements for apo-B mRNA editing in vitro. By UV cross-linking and immunoprecipitation, we show that ACF binds to apo-B mRNA in vitro and in vivo. Cross-linking of ACF is not competed by RNAs with mutations in the mooring sequence. Coimmunoprecipitation experiments identified an ACF-apobec-1 complex in transfected cells. Immunodepletion of ACF from rat liver extracts abolished editing activity. The immunoprecipitated complexes contained a functional holoenzyme. Our results support a model of the editing enzyme in which ACF binds to the mooring sequence in apo-B mRNA and docks apobec-1 to deaminate its target cytidine. The fact that ACF is widely expressed in human tissues that lack apobec-1 and apo-B mRNA suggests that ACF may be involved in other RNA editing or RNA processing events.

Indexed as

AICDA (Activation-Induced Cytidine Deaminase)Amino Acid SequenceAnimalsAPOBEC-1 DeaminaseApolipoproteins BCloning, MolecularCytidine DeaminaseDNA, ComplementaryHumansMolecular Sequence DataRatsRNA-Binding ProteinsRNA EditingRNA, MessengerAICDA (Activation-Induced Cytidine Deaminase)APOBEC-1 DeaminaseAPOBEC1 protein, humanApobec1 protein, ratApolipoproteins BCytidine DeaminaseDNA, ComplementaryRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID10669759
PMCPMC85365
OpenAlexW2140097965

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.