Evidence map›Paper›PMID 24074597›Full record

ArticleVirology2013

Nuclear import of high risk HPV16 E7 oncoprotein is mediated by its zinc-binding domain via hydrophobic interactions with Nup62.

Jeremy Eberhard, Zeynep Onder, Junona Moroianu

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Jeremy EberhardBiology Department, Boston College, Chestnut Hill, MA 02467, USA.
Zeynep Onder
Junona Moroianu
Boston College · US

Funding

Nuclear Import Pathways for HPV MacromoleculesR01CA094898 · NCI · BOSTON COLLEGE · PI MOROIANU, JUNONA F · 2002 to 2010
$2.0M
NCI NIH HHS R01 CA094898NCI NIH HHS R01CA94898
6 · The paper itself

Abstract

We previously discovered that nuclear import of high risk HPV16 E7 is mediated by a cNLS located within the zinc-binding domain via a pathway that is independent of karyopherins/importins (Angeline et al., 2003; Knapp et al., 2009). In this study we continued our characterization of the cNLS and nuclear import pathway of HPV16 E7. We find that an intact zinc-binding domain is essential for the cNLS function in mediating nuclear import of HPV16 E7. Mutagenesis of cysteine residues to alanine in each of the two CysXXCys motifs involved in zinc-binding changes the nuclear localization of the EGFP-16E7 and 2xEGFP-16E7 mutants. We further discover that a patch of hydrophobic residues, 65LRLCV69, within the zinc-binding domain of HPV16 E7 mediates its nuclear import via hydrophobic interactions with the FG domain of the central channel nucleoporin Nup62.

Indexed as

Active Transport, Cell NucleusProtein Interaction Domains and MotifsProtein Interaction MappingVirus ReplicationDNA Mutational AnalysisHeLa CellsHuman papillomavirus 16HumansHydrophobic and Hydrophilic InteractionsMembrane GlycoproteinsMutagenesis, Site-DirectedMutant ProteinsNuclear Pore Complex ProteinsPapillomavirus E7 ProteinsProtein BindingZincMembrane GlycoproteinsMutant ProteinsNuclear Pore Complex Proteinsnuclear pore protein p62oncogene protein E7, Human papillomavirus type 16Papillomavirus E7 ProteinsZincEGFPenhanced green fluorescent proteinFG nucleoporinglutathione-S-transferaseGSTHPVHPV16 E7 oncoproteinhuman papillomavirusHuman papillomavirusNESNLSNPCnuclear export signalnuclear localization signalNuclear localization signalnuclear pore complexNup62

Identifiers

PMID24074597
PMCPMC3789256
OpenAlexW1984362338

What OpenQuestion holds

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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.