Evidence map›Paper›PMID 19917295›Full record

ArticleJournal of molecular biology2010

E6 proteins from diverse papillomaviruses self-associate both in vitro and in vivo.

Katia Zanier, Christine Ruhlmann, Frederic Melin, Murielle Masson, Abdellahi Ould M'hamed Ould Sidi, Xavier Bernard, Benoit Fischer, Laurent Brino, Tutik Ristriani, Vladimir Rybin and 5 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 3 countries.

Katia ZanierEcole Supérieure de Biotechnologie de Strasbourg (IREBS, FRE 3211), Boulevard Sébastien Brant, BP 10413, 67412 Illkirch Cedex, France. zanier@esbs.u-strasbg.fr
Christine Ruhlmann
Frederic Melin
Murielle Masson
Abdellahi Ould M'hamed Ould Sidi
Xavier Bernard
Benoit Fischer
Laurent Brino
Tutik Ristriani
Vladimir Rybin
Mireille Baltzinger
Scott Vande Pol
Petra Hellwig
Patrick Schultz
Gilles Travé
École Supérieure de Biotechnologie de Strasbourg · FRInstitut de génétique et de biologie moléculaire et cellulaire · FRInstitut de Chimie de Strasbourg · FRCentre National de la Recherche Scientifique · FRCharlottesville Medical Research · USEuropean Molecular Biology Organization · DE

Funding

Papillomavirus E6 Structural ConsortiumR01CA134737 · NCI · UNIVERSITY OF VIRGINIA · PI VANDE POL, SCOTT BRIAN · 2010 to 2019
$4.2M
NCI NIH HHS R01 CA134737
6 · The paper itself

Abstract

Papillomavirus E6 oncoproteins bind and often provoke the degradation of many cellular proteins important for the control of cell proliferation and/or cell death. Structural studies on E6 proteins have long been hindered by the difficulties of obtaining highly concentrated samples of recombinant E6. Here, we show that recombinant E6 proteins from eight human papillomavirus strains and one bovine papillomavirus strain exist as oligomeric and multimeric species. These species were characterized using a variety of biochemical and biophysical techniques, including analytical gel filtration, activity assays, surface plasmon resonance, electron microscopy and Fourier transform infrared spectroscopy. The characterization of E6 oligomers is facilitated by the fusion to the maltose binding protein, which slows the formation of higher-order multimeric species. The proportion of each oligomeric form varies depending on the viral strain considered. Oligomers appear to consist of folded units, which, in the case of high-risk mucosal human papillomavirus E6, retain binding to the ubiquitin ligase E6-associated protein and the capacity to degrade the proapoptotic protein p53. In addition to the small-size oligomers, E6 proteins spontaneously assemble into large organized multimeric structures, a process that is accompanied by a significant increase in the beta-sheet secondary structure content. Finally, co-localisation experiments using E6 equipped with different tags further demonstrate the occurrence of E6 self-association in eukaryotic cells. The ensemble of these data suggests that self-association is a general property of E6 proteins that occurs both in vitro and in vivo and might therefore be functionally relevant.

Indexed as

Carrier ProteinsCell NucleusChromatography, GelHumansMaltose-Binding ProteinsMutant ProteinsProtein BindingProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryRecombinant Fusion ProteinsSolubilitySpectroscopy, Fourier Transform InfraredViral ProteinsZincCarrier ProteinsMaltose-Binding ProteinsMutant ProteinsRecombinant Fusion ProteinsViral ProteinsZinc

Identifiers

PMID19917295
PMCPMC3900769
OpenAlexW2055771866

What OpenQuestion holds

Textmetadata
LicenceTDM
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.