Evidence map›Paper›PMID 8995605›Full record

ArticleJournal of virology1997

Mapping and characterization of the interaction domains of human papillomavirus type 16 E1 and E2 proteins.

T Yasugi, J D Benson, H Sakai, M Vidal, P M Howley

Abstract read
In one paragraph

Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Review
  6. Article
  7. Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. The E1 proteins.Virology · 2013
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors.

T YasugiDepartment of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
J D Benson
H Sakai
M Vidal
P M Howley

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The papillomavirus E1 and E2 proteins are both necessary and sufficient in vivo for efficient origin-dependent viral DNA replication. The ability of E1 and E2 to complex with each other appears to be essential for efficient viral DNA replication. In this study, we used the yeast two-hybrid system and in vitro binding assays to map the domains of the human papillomavirus type 16 (HPV16) E1 and E2 proteins required for complex formation. The amino-terminal 190-amino-acid domain of HPV16 E2 was both required and sufficient for E1 binding. The carboxyl-terminal 229 amino acids of E 1 were essential for binding E2, and the amino-terminal 143 amino acids of HPV16 E1 were dispensable. Although the ability of the E1 minimal domain (amino acids [aa] 421 to 649) to interact with E2 was strong at 4 degrees C, it was significantly reduced at temperatures above 25 degrees C. A larger domain of E1 from aa 144 to 649 bound E2 efficiently at any temperature, suggesting that aa 144 to 420 of E1 may play a role in the HPV16 E1-E2 interaction at physiological temperatures.

Indexed as

DNA-Binding ProteinsBinding SitesHumansOncogene ProteinsOncogene Proteins, ViralPapillomaviridaePeptide MappingProtein BindingVirus ReplicationDNA-Binding ProteinsE1 protein, Human papillomavirus 16E2 protein, Human papillomavirus type 16Oncogene ProteinsOncogene Proteins, Viral

Identifiers

PMID8995605
PMCPMC191136

What OpenQuestion holds

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Registered trials

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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.