Evidence map›Paper›PMID 12138179›Full record

ArticleMolecular and cellular biology2002

Role of the p68 subunit of human DNA polymerase alpha-primase in simian virus 40 DNA replication.

Robert D Ott, Christoph Rehfuess, Vladimir N Podust, Jill E Clark, Ellen Fanning

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. 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
0.7field-weighted citation impact, top 32% 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, 29 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Robert D OttDepartment of Biological Sciences and Vanderbilt-Ingram Cancer Center, Vanderbilt University, Nashville, Tennessee 37232, USA.
Christoph Rehfuess
Vladimir N Podust
Jill E Clark
Ellen Fanning
Vanderbilt University · US

Funding

CONTROL OF SIMIAN VIRUS 40 AND CELLULAR DNA REPLICATIONR01GM052948 · NIGMS · VANDERBILT UNIVERSITY · PI FRIEDMAN, KATHERINE LOUISE · 1995 to 2013
$6.1M
NIGMS NIH HHS GM52948NIGMS NIH HHS R01 GM052948
6 · The paper itself

Abstract

DNA polymerase alpha-primase (pol-prim) is a heterotetramer with DNA polymerase and primase activities. The polymerase (p180) and primase (p48 and p58) subunits synthesize primers and extend them, but the function of the remaining subunit (p68) is poorly understood. Genetic studies in yeast suggested an essential role for the p68 ortholog in early S phase prior to the hydroxyurea-sensitive step, possibly a regulatory role in initiation of DNA replication, but found no evidence for an essential function of p68 later in S phase. To investigate whether the human p68 subunit has an essential role in DNA replication, we examined the ability of a purified trimeric human pol-prim lacking p68 to initiate simian virus 40 DNA replication in vitro and to synthesize and elongate primers on single-stranded DNA in the presence of T antigen and replication protein A (RPA). Both activities of trimeric pol-prim were defective, but activity was recovered upon addition of separately purified p68. Phosphorylation of p68 by cyclin A-dependent protein kinase also inhibited both activities of pol-prim. The data strongly suggest that the p68 subunit is required for priming activity of pol-prim in the presence of RPA and T antigen, both during initiation at the origin and during lagging strand replication.

Indexed as

CDC2-CDC28 KinasesDNA ReplicationAnimalsAntigens, Polyomavirus TransformingCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent KinasesDNA Polymerase IDNA PrimaseHumansMacromolecular SubstancesPhosphorylationProtein Serine-Threonine KinasesProtein Structure, QuaternaryProtein SubunitsRecombinant ProteinsAntigens, Polyomavirus TransformingCDC2-CDC28 KinasesCDK2 protein, humanCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent KinasesDNA polymerase alpha-primaseDNA Polymerase IDNA PrimaseMacromolecular SubstancesProtein Serine-Threonine KinasesProtein SubunitsRecombinant Proteins

Identifiers

PMID12138179
PMCPMC133971
OpenAlexW2092598571

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.