Evidence map›Paper›PMID 16690141›Full record

ArticleAntiviral research2006

Identification of inhibitors to papillomavirus type 16 E6 protein based on three-dimensional structures of interacting proteins.

James D Baleja, Jonathan J Cherry, Zhiguo Liu, Hua Gao, Marc C Nicklaus, Johannes H Voigt, Jason J Chen, Elliot J Androphy

Open access · greenAbstract read
In one paragraph

Article in Antiviral research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

40 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Human Papillomavirus (HPV) Entry Inhibitors.Advances in experimental medicine and biology · 2022
    Article
  10. Article
  11. Review
  12. Article
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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

8 authors at 4 institutions in 1 country.

James D BalejaDepartment of Biochemistry, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, USA. jim.baleja@tufts.edu
Jonathan J Cherry
Zhiguo Liu
Hua Gao
Marc C Nicklaus
Johannes H Voigt
Jason J Chen
Elliot J Androphy
University of Massachusetts Chan Medical School · USFrederick National Laboratory for Cancer Research · USNational Cancer Institute · USTufts University · US

Funding

DESIGN OF UMAN PAPILLOMAVIRUS INHIBITORSR01AI038001 · NIAID · TUFTS UNIVERSITY BOSTON · PI BALEJA, JAMES D · 2000 to 2004
$1.8M
Small Molecule Inhibitors of Oncogenic Human PapillomavirusR01CA119904 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ANDROPHY, ELLIOT J. · 2008 to 2011
$1.3M
In Silico Screening for Cancer TargetsZ01BC010639 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NICKLAUS, MARC · 2004 to 2008
$925k
Novel Approach to Cervical Cancer PreventionR03CA092746 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CHEN, JASON J · 2001 to 2002
$158k
NCI NIH HHS R01 CA119904NCI NIH HHS R03 CA92746NIAID NIH HHS R01 AI038001NIAID NIH HHS R01 AI38001
6 · The paper itself

Abstract

Human papillomaviruses (HPV) cause cutaneous and genital warts. A subset of HPV types is associated with a high-risk for progression to malignancy. The E6 protein from the high-risk HPV types represents an attractive target for intervention because of its roles in viral propagation and cellular transformation. E6 functions in part by interaction with human cellular proteins, several of which possess a helical E6-binding motif. The role for each amino acid in this motif for binding E6 has been tested through structure determination and site-directed mutagenesis. These structural and molecular biological approaches defined the spatial geometry of functional groups necessary for binding to E6. This E6-binding information (the E6-binding pharmacophore) was transferred into a three-dimensional query format suitable for computational screening of large chemical databases. Compounds were identified and tested using in vitro and cell culture-based assays. Several compounds selectively inhibited E6 interaction with the E6-binding protein E6AP and interfered with the ability of E6 to promote p53 degradation. Such compounds provide leads for the development of new pharmacologic agents to treat papillomavirus infections and their associated cancers.

Indexed as

Drug DesignAntiviral AgentsBinding SitesOncogene Proteins, ViralPapillomaviridaeProtein BindingRepressor ProteinsZinc FingersAntiviral AgentsE6 protein, Human papillomavirus type 16Oncogene Proteins, ViralRepressor Proteins

Identifiers

PMID16690141
PMCPMC2776632
OpenAlexW2045048736

What OpenQuestion holds

Textmetadata
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.