Evidence map›Paper›PMID 9765384›Full record

ArticleJournal of virology1998

High-mobility group 1/2 proteins are essential for initiating rolling-circle-type DNA replication at a parvovirus hairpin origin.

S F Cotmore, P Tattersall

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. 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
4.2field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

S F CotmoreDepartments of Laboratory Medicine, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
P Tattersall
Yale University · US

Funding

MOLECULAR BASIS OF PARVOVIRUS TARGET CELL SPECIFICITYR01CA029303 · NCI · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 1985 to 2016
$7.5M
Molecular Genetics of Parvoviral DNA ReplicationR37AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 2009 to 2018
$5.4M
MOLECULAR GENETICS OF PARVOVIRAL DNA REPLICATIONR01AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 1988 to 2009
$3.0M
NCI NIH HHS CA29303NCI NIH HHS R01 CA029303NIAID NIH HHS AI26109NIAID NIH HHS R01 AI026109NIAID NIH HHS R37 AI026109
6 · The paper itself

Abstract

Rolling-circle replication is initiated by a replicon-encoded endonuclease which introduces a single-strand nick into specific origin sequences, becoming covalently attached to the 5' end of the DNA at the nick and providing a 3' hydroxyl to prime unidirectional, leading-strand synthesis. Parvoviruses, such as minute virus of mice (MVM), have adapted this mechanism to amplify their linear single-stranded genomes by using hairpin telomeres which sequentially unfold and refold to shuttle the replication fork back and forth along the genome, creating a continuous, multimeric DNA strand. The viral initiator protein, NS1, then excises individual genomes from this continuum by nicking and reinitiating synthesis at specific origins present within the hairpin sequences. Using in vitro assays to study ATP-dependent initiation within the right-hand (5') MVM hairpin, we have characterized a HeLa cell factor which is absolutely required to allow NS1 to nick this origin. Unlike parvovirus initiation factor (PIF), the cellular complex which activates NS1 endonuclease activity at the left-hand (3') viral origin, the host factor which activates the right-hand hairpin elutes from phosphocellulose in high salt, has a molecular mass of around 25 kDa, and appears to bind preferentially to structured DNA, suggesting that it might be a member of the high-mobility group 1/2 (HMG1/2) protein family. This prediction was confirmed by showing that purified calf thymus HMG1 and recombinant human HMG1 or murine HMG2 could each substitute for the HeLa factor, activating the NS1 endonuclease in an origin-specific nicking reaction.

Indexed as

AnimalsBase SequenceDNA ReplicationDNA, ViralEndonucleasesHeLa CellsHigh Mobility Group ProteinsHumansMiceMinute Virus of MiceNucleic Acid ConformationViral Nonstructural ProteinsDNA, ViralEndonucleasesHigh Mobility Group ProteinsNS1 protein, minute virus of miceViral Nonstructural Proteins

Identifiers

PMID9765384
PMCPMC110256
OpenAlexW1490559537

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.