Evidence map›Paper›PMID 7707506›Full record

ArticleJournal of virology1995

Zinc-binding and protein-protein interactions mediated by the polyomavirus large T antigen zinc finger.

P E Rose, B S Schaffhausen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1995. 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
1.5field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Lessons in signaling and tumorigenesis from polyomavirus middle T antigen.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The polyoma virus T antigen interferes with interferon-inducible gene expression.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

2 authors at 1 institution in 1 country.

P E RoseDepartment of Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
B S Schaffhausen
Tufts University · US

Funding

PRODUCTS OF THE TRANSFORMING GENES OF POLYOMAVIRUSR01CA034722 · NCI · TUFTS UNIVERSITY BOSTON · PI SCHAFFHAUSEN, BRIAN S · 1985 to 2015
$6.0M
PRODUCTS OF THE TRANSFORMING GENES OF POLYOMA VIRUSR37CA034722 · NCI · TUFTS UNIVERSITY BOSTON · PI SCHAFFHAUSEN, BRIAN S · 1991 to 1998
–
NCI NIH HHS CA34722NCI NIH HHS R01 CA034722
6 · The paper itself

Abstract

Polyomavirus large tumor antigen (LT) contains a potential C2H2 zinc binding element between residues 452 and 472. LT also contains a third histidine in this region, conserved among the polyomavirus LTs. Synthetic peptides of this region bound a single atom of zinc, as determined by spectroscopic analysis. Blotting experiments also showed that fusion proteins containing the element, as well as full-length LT, bound 65Zn. Polyomavirus middle T and small T antigens also bound zinc in the blotting assay. Site-directed mutagenesis showed the importance of this element in LT. Point mutations in four of the conserved residues (C-452, C-455, H-465, and H-469) blocked the ability of LT to function in viral DNA replication, while mutation of H-472-->L decreased replication to 1/30th that of the wild type. Point mutations in intervening residues tested had little effect on replication. Mutants resulting from mutations in the conserved cysteine or histidine residues retained the ability to bind origin DNA. However, they did show a defect in self-association. Because double-hexamer formation is involved in DNA replication, this deficiency is sufficient to explain the defect in replication. Mutants created by point mutations of the coordinating residues were also deficient in replication-associated phosphorylations.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsAntigens, Polyomavirus TransformingBase SequenceBinding SitesDNA ReplicationDNA, ViralMiceMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationPoint MutationPolyomavirusProtein BindingZincAntigens, Polyomavirus TransformingDNA, ViralZinc

Identifiers

PMID7707506
PMCPMC188979
OpenAlexW1638981824

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.