Evidence map›Paper›PMID 28701406›Full record

ArticleJournal of virology2017

Structural and Functional Basis for an EBNA1 Hexameric Ring in Epstein-Barr Virus Episome Maintenance.

Julianna S Deakyne, Kimberly A Malecka, Troy E Messick, Paul M Lieberman

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 26 citations in OpenAlex.

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  8. OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023
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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

4 authors at 1 institution in 1 country.

Julianna S DeakyneThe Wistar Institute, Philadelphia, Pennsylvania, USA.
Kimberly A MaleckaThe Wistar Institute, Philadelphia, Pennsylvania, USA.
Troy E MessickThe Wistar Institute, Philadelphia, Pennsylvania, USA tmessick@Wistar.org Lieberman@wistar.org.
Paul M LiebermanThe Wistar Institute, Philadelphia, Pennsylvania, USA tmessick@Wistar.org Lieberman@wistar.org.
The Wistar Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
Regulation of Epstein-Barr Virus LatencyR01CA093606 · NCI · WISTAR INSTITUTE · PI LIEBERMAN, PAUL M. · 2002 to 2022
$6.7M
Epigenetic Regulation of Epstein-Barr Virus Latency ProgramsR01DE017336 · NIDCR · WISTAR INSTITUTE · PI PAUL M. LIEBERMAN · 2005 to 2026
$6.5M
NCI NIH HHS P30 CA010815NCI NIH HHS R01 CA093606NCI NIH HHS T32 CA009171NIDCR NIH HHS R01 DE017336Wellcome TrustWellcome Trust WT096496
6 · The paper itself

Abstract

Epstein-Barr virus (EBV) establishes a stable latent infection that can persist for the life of the host. EBNA1 is required for the replication, maintenance, and segregation of the latent episome, but the structural features of EBNA1 that confer each of these functions are not completely understood. Here, we have solved the X-ray crystal structure of an EBNA1 DNA-binding domain (DBD) and discovered a novel hexameric ring oligomeric form. The oligomeric interface pivoted around residue T585 as a joint that links and stabilizes higher-order EBNA1 complexes. Substitution mutations around the interface destabilized higher-order complex formation and altered the cooperative DNA-binding properties of EBNA1. Mutations had both positive and negative effects on EBNA1-dependent DNA replication and episome maintenance with OriP. We found that one naturally occurring polymorphism in the oligomer interface (T585P) had greater cooperative DNA binding

Indexed as

Binding SitesCell Line, TumorCrystallography, X-RayDNA-Binding ProteinsDNA ReplicationDNA, ViralEpstein-Barr Virus Nuclear AntigensHEK293 CellsHeLa CellsHerpesvirus 4, HumanHistonesHumansMultiprotein ComplexesOrigin Recognition ComplexPlasmidsProtein Structure, TertiaryDNA-Binding ProteinsDNA, ViralEBV-encoded nuclear antigen 1Epstein-Barr Virus Nuclear AntigensHistonesMultiprotein ComplexesOrigin Recognition Complexcooperative bindingDNA-binding domainEBNA1episome maintenanceEpstein-Barr virushexameric ringoligomersOriPviral latency

Identifiers

PMID28701406
PMCPMC5599765
OpenAlexW2736094620

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.