Evidence map›Paper›PMID 18562538›Full record

ArticleJournal of virology2008

Structural analysis reveals an amyloid form of the human papillomavirus type 16 E1--E4 protein and provides a molecular basis for its accumulation.

Pauline B McIntosh, Stephen R Martin, Deborah J Jackson, Jameela Khan, Erin R Isaacson, Lesley Calder, Kenneth Raj, Heather M Griffin, Qian Wang, Peter Laskey and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 12% 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, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Potential Role of E4 Protein in Human Papillomavirus Screening: a ReviewAsian Pacific journal of cancer prevention : APJCP · 2017
    Review
  7. Article
  8. Review
  9. Stratification of HPV-induced cervical pathology using the virally encoded molecular marker E4 in combination with p16 or MCM.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2015
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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

12 authors at 1 institution in 1 country.

Pauline B McIntoshDivision of Virology, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.
Stephen R Martin
Deborah J Jackson
Jameela Khan
Erin R Isaacson
Lesley Calder
Kenneth Raj
Heather M Griffin
Qian Wang
Peter Laskey
John F Eccleston
John Doorbar
MRC London Institute of Medical Sciences · GB

Funding

Medical Research Council MC_U117573807Medical Research Council MC_U117584278
6 · The paper itself

Abstract

The abundant human papillomavirus (HPV) type 16 E4 protein exists as two distinct structural forms in differentiating epithelial cells. Monomeric full-length 16E1--E4 contains a limited tertiary fold constrained by the N and C termini. N-terminal deletions facilitate the assembly of E1--E4 into amyloid-like fibrils, which bind to thioflavin T. The C-terminal region is highly amyloidogenic, and its deletion abolishes amyloid staining and prevents E1--E4 accumulation. Amyloid-imaging probes can detect 16E1--E4 in biopsy material, as well as 18E1--E4 and 33E1--E4 in monolayer cells, indicating structural conservation. Our results suggest a role for fibril formation in facilitating the accumulation of E1--E4 during HPV infection.

Indexed as

Amino Acid SequenceAnimalsBiopsyChlorocebus aethiopsCOS CellsGene DeletionHuman papillomavirus 16HumansMolecular Sequence DataProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino Acid

Identifiers

PMID18562538
PMCPMC2519553
OpenAlexW2129998022

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.