Evidence map›Paper›PMID 26428925›Full record

ArticleJournal of microbiology (Seoul, Korea)2015

Characterization of the rapamycin-inducible EBV LMP1 activation system.

Sang Yong Kim, Jung-Eun Kim, Jiyeon Won, Yoon-Jae Song

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Article in Journal of microbiology (Seoul, Korea), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

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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

5 citing papers in PubMed.

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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

4 authors.

Sang Yong KimDepartment of Life Science, Gachon University, Seongnam, 13120, Republic of Korea.
Jung-Eun KimDepartment of Life Science, Gachon University, Seongnam, 13120, Republic of Korea.
Jiyeon WonDepartment of Life Science, Gachon University, Seongnam, 13120, Republic of Korea.
Yoon-Jae SongDepartment of Life Science, Gachon University, Seongnam, 13120, Republic of Korea. songyj@gachon.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is required for EBV-mediated B lymphocyte transformation into proliferating lymphoblastoid cell lines (LCL). LMP1 oligomerizes spontaneously in membrane lipid rafts via its transmembrane domain and constitutively activates signal transduction pathways, including NF-κB, p38 Mitogen-Activated Protein Kinase (MAPK), and c-Jun N-terminal Kinase (JNK). Since LMP1 mimics the tumor necrosis factor receptor (TNFR), CD40, it may be effectively utilized to study the effects of constitutive activation of signal transduction pathways on cellular physiology. On the other hand, LMP1 presents a disadvantage in terms of determining the sequential events and factors involved in signaling pathways. A CD40-LMP1 chimeric molecule has been generated to overcome this limitation but does not represent the authentic and physiological nature of LMP1. In the current study, a ligand-dependent activation system for LMP1 using rapamycin-inducible dimerization was generated to delineate the LMP1 signaling pathway.

Indexed as

Carrier ProteinsCell MembraneDNA PrimersGene ExpressionHEK293 CellsHerpesvirus 4, HumanHumansNF-kappa BProtein MultimerizationRecombinant Fusion ProteinsSignal TransductionSirolimusTacrolimus Binding ProteinsTOR Serine-Threonine KinasesViral Matrix ProteinsCarrier ProteinsDNA PrimersEBV-associated membrane antigen, Epstein-Barr virusMTOR protein, humanNF-kappa BRecombinant Fusion ProteinsSirolimusTacrolimus Binding ProteinsTOR Serine-Threonine KinasesViral Matrix ProteinsEpstein-Barr viruslatent membrane protein 1NF-κB

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Registered trials

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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.