Evidence map›Paper›PMID 19244625›Full record

ArticleJournal of molecular biology2009

Determinants of stability for the E6 protein of papillomavirus type 16.

Yuqi Liu, Jonathan J Cherry, Joseph V Dineen, Elliot J Androphy, James D Baleja

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. 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
2.4field-weighted citation impact, top 11% 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, 32 citations in OpenAlex.

  1. DARPin-induced reactivation of p53 in HPV-positive cells.Nature structural & molecular biology · 2025
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  16. Construction and identification of a yeast two-hybrid bait vector and its effect on the growth of yeast cells and the self-activating function of reporter genes for screening of HPV18 E6-interacting protein.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2010
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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

5 authors at 2 institutions in 1 country.

Yuqi LiuDepartment of Biochemistry, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Jonathan J Cherry
Joseph V Dineen
Elliot J Androphy
James D Baleja
Tufts University · USUniversity of Massachusetts Chan Medical School · US

Funding

Small Molecule Inhibitors of Oncogenic Human PapillomavirusR01CA119904 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ANDROPHY, ELLIOT J. · 2008 to 2011
$1.3M
NCI NIH HHS CA119904NCI NIH HHS R01 CA119904
6 · The paper itself

Abstract

E6 is an oncoprotein produced by human papillomavirus (HPV). The E6 protein from high-risk HPV type 16 contains two zinc-binding domains with two C-x-x-C motifs each. E6 exerts its transforming functions through formation of a complex with E6AP, which binds p53 and stimulates its degradation. There have been few biophysical and structural studies due to difficulty in preparation of soluble protein; here we describe the preparation of soluble E6 constructs including the two separated zinc-binding domains of E6. These proteins are used to examine the extent to which the two domains cooperate to mediate E6 function, how zinc influences the behavior of E6 protein, and which domains mediate aggregation. We demonstrate, using p53 degradation, E6AP binding, and hDlg (human homolog of the Drosophila discs large tumor suppressor protein) PDZ (postsynaptic density/disc large/zonula occludens) protein binding assays, that these soluble proteins are active, and, using NMR, circular dichroism, and fluorescence spectroscopies, we show that they are folded and stable. We show that the separated N-terminal and C-terminal domains interact, but nonproductively, for E6 function. The two domains bind zinc differently with higher affinity associated with the C-terminal domain. Analyses using surface plasmon resonance and circular dichroism and fluorescence spectroscopies show that aggregation is mediated more through the N-terminal domain than through the C-terminal domain. These studies allow a model in which the C-terminal zinc-binding domain of E6 recruits a target protein such as hDlg and the N-terminal domain is mostly responsible for recruiting a ubiquitin ligase to mediate target protein degradation.

Indexed as

Magnetic Resonance SpectroscopyMutant ProteinsOncogene Proteins, ViralProtein BindingProtein DenaturationProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsRepressor ProteinsSolubilityTemperatureUreaZincE6 protein, Human papillomavirus type 16Mutant ProteinsOncogene Proteins, ViralRecombinant Fusion ProteinsRepressor ProteinsUreaZinc

Identifiers

PMID19244625
PMCPMC2768073
OpenAlexW2013241714

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.