Evidence map›Paper›PMID 25606060›Full record

ArticleMobile DNA2014

Development of a monoclonal antibody specific to the endonuclease domain of the human LINE-1 ORF2 protein.

Mark Sokolowski, Cecily B DeFreece, Geraldine Servant, Kristine J Kines, Dawn L deHaro, Victoria P Belancio

Open access · goldAbstract read
In one paragraph

Article in Mobile DNA, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-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

17 citing papers in PubMed, 21 citations in OpenAlex.

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  13. Transposable elements in cancer.Nature reviews. Cancer · 2017
    Review
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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

6 authors at 2 institutions in 1 country.

Mark Sokolowski *Department of Structural and Cellular Biology, Tulane School of Medicine, Tulane Cancer Center, and Tulane Center for Aging, New Orleans, LA 70112 USA.
Cecily B DeFreece *Department of Biology, Xavier University, 1 Drexel Drive, Box 85, New Orleans, LA 70125-7918 USA.
Geraldine ServantDepartment of Epidemiology, Tulane School of Public Health, Tulane Cancer Center, New Orleans, LA 70112 USA.
Kristine J KinesDepartment of Structural and Cellular Biology, Tulane School of Medicine, Tulane Cancer Center, and Tulane Center for Aging, New Orleans, LA 70112 USA.
Dawn L deHaroDepartment of Structural and Cellular Biology, Tulane School of Medicine, Tulane Cancer Center, and Tulane Center for Aging, New Orleans, LA 70112 USA.
Victoria P BelancioDepartment of Structural and Cellular Biology, Tulane School of Medicine, Tulane Cancer Center, and Tulane Center for Aging, New Orleans, LA 70112 USA.
Tulane University · USXavier University · US

Funding

Xavier's RCMI Cancer Research ProgramG12MD007595 · NIMHD · XAVIER UNIVERSITY OF LOUISIANA · PI D'AMOUR, GENE, WANG, GUANGDI · 2012 to 2018
$15.7M
Mentoring a Cancer Genetics ProgramP20GM103518 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI DEININGER, PRESCOTT L. · 2012 to 2013
$4.3M
NIGMS NIH HHS P20 GM103518NIMHD NIH HHS G12 MD007595
6 · The paper itself

Abstract

backgroundLINE-1 (L1) retrotransposons are common occupants of mammalian genomes representing about a fifth of the genetic content. Ongoing L1 retrotransposition in the germ line and somatic tissues has contributed to structural genomic variations and disease-causing mutations in the human genome. L1 mobilization relies on the function of two, self-encoded proteins, ORF1 and ORF2. The ORF2 protein contains two characterized domains: endonuclease and reverse transcriptase.

resultsUsing a bacterially purified endonuclease domain of the human L1 ORF2 protein, we have generated a monoclonal antibody specific to the human ORF2 protein. We determined that the epitope recognized by this monoclonal antibody includes amino acid 205, which is required for the function of the L1 ORF2 protein endonuclease. Using an in vitro L1 cleavage assay, we demonstrate that the monoclonal anti-ORF2 protein antibody partially inhibits L1 endonuclease activity without having any effect on the in vitro activity of the human AP endonuclease.

conclusionsOverall, our data demonstrate that this anti-ORF2 protein monoclonal antibody is a useful tool for human L1-related studies and that it provides a rationale for the development of antibody-based inhibitors of L1-induced damage.

Indexed as

EndonucleaseIn vitro assayL1L1 antibodyLINE-1ORF2Retrotransposition

Identifiers

PMID25606060
PMCPMC4279459
OpenAlexW2158195234

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.