Evidence map›Paper›PMID 15793585›Full record

ArticleNature structural & molecular biology2005

Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome.

Alphonse I Arunkumar, Vitaly Klimovich, Xiaohua Jiang, Robert D Ott, L Mizoue, Ellen Fanning, Walter J Chazin

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.9field-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

57 citing papers in PubMed, 87 citations in OpenAlex.

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  12. FRETting about the affinity of bimolecular protein-protein interactions.Protein science : a publication of the Protein Society · 2018
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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

7 authors at 1 institution in 1 country.

Alphonse I ArunkumarDepartment of Biochemistry, Vanderbilt University, Nashville Tennessee 37232-8725 USA.
Vitaly Klimovich
Xiaohua Jiang
Robert D Ott
L Mizoue
Ellen Fanning
Walter J Chazin
Vanderbilt University · US

Funding

Structural Basis for RPA Functions in DNA ProcessingR01GM065484 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2003 to 2015
$3.9M
NIGMS NIH HHS R01 GM065484
6 · The paper itself

Abstract

Simian virus 40 (SV40) provides a model system for the study of eukaryotic DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40 replication requires interaction of Tag with the host single-stranded DNA-binding protein, replication protein A (hRPA). The C-terminal domain of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but whether it interacts with Tag is not known. Affinity chromatography and NMR revealed physical interaction between hRPA32C and the Tag origin DNA-binding domain, and a structural model of the complex was determined. Point mutations were then designed to reverse charges in the binding sites, resulting in substantially reduced binding affinity. Corresponding mutations introduced into intact hRPA impaired initiation of replication and primosome activity, implying that this interaction has a critical role in assembly and progression of the SV40 replisome.

Indexed as

Antibodies, MonoclonalBinding SitesDNADNA-Binding ProteinsDNA PrimersDNA RepairDNA ReplicationHumansModels, MolecularMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiaryReplication Protein ASimian virus 40Virus ReplicationAntibodies, MonoclonalDNADNA-Binding ProteinsDNA PrimersReplication Protein ARPA1 protein, human

Identifiers

PMID15793585
PMCPMC2600586
OpenAlexW2010318773

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.