Evidence map›Paper›PMID 9469832›Full record

ArticleNucleic acids research1998

Adenovirus DNA polymerase: domain organisation and interaction with preterminal protein.

E J Parker, C H Botting, A Webster, R T Hay

Abstract read
In one paragraph

Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Genetic diversity of adenovirus in neotropical bats from Brazil.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

4 authors.

E J ParkerSchool of Biomedical Science, Irvine Building, University of St Andrews, North Street, St Andrews, Fife KY16 9AL, UK.
C H Botting
A Webster
R T Hay

Funding

Wellcome Trust
6 · The paper itself

Abstract

Adenovirus DNA polymerase is one of three viral proteins and two cellular proteins required for replication of the adenovirus genome. During initiation of viral DNA synthesis the viral DNA polymerase transfers dCMP onto the adenovirus preterminal protein, to which it is tightly bound. The domain structure of the 140 kDa DNA polymerase has been probed by partial proteolysis and the sites of proteolytic cleavage determined by N-terminal sequencing. At least four domains can be recognised within the DNA polymerase. Adenovirus preterminal protein interacts with three of the four proteolytically derived domains. This was confirmed by cloning and expression of each of the individual domains. These data indicate that, like other members of the pol alpha family of DNA polymerases, the adenovirus DNA polymerase has a multidomain structure and that interaction with preterminal protein takes place with non-contiguous regions of the polypeptide chain over a large surface area of the viral DNA polymerase.

Indexed as

Viral ProteinsAdenoviridaeAnimalsBase SequenceBinding SitesDNA-Directed DNA PolymeraseDNA PrimersDNA ReplicationPeptide FragmentsPhosphoproteinsProtein PrecursorsRecombinant ProteinsDNA-Directed DNA PolymeraseDNA PrimersPeptide FragmentsPhosphoproteinsProtein PrecursorspTP protein, adenovirusRecombinant ProteinsViral Proteins

Identifiers

PMID9469832
PMCPMC147410

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.