Evidence map›Paper›PMID 17478495›Full record

ArticleNucleic acids research2007

Transcription activator structure reveals redox control of a replication initiation reaction.

Cyril M Sanders, Dmytro Sizov, Philippa R Seavers, Miguel Ortiz-Lombardía, Alfred A Antson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. E2 Tyrosine 102 Regulates MmuPV1 Pathogenesis In Vivo.Pathogens (Basel, Switzerland) · 2025
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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 2 institutions in 1 country.

Cyril M SandersInstitute for Cancer Studies, University of Sheffield, Beech Hill Rd, Sheffield, S10 2RX, UK. c.m.sanders@sheffield.ac.uk
Dmytro Sizov
Philippa R Seavers
Miguel Ortiz-Lombardía
Alfred A Antson
University of York · GBUniversity of Sheffield · GB

Funding

Wellcome Trust 067416
6 · The paper itself

Abstract

Redox changes are one of the factors that influence cell-cycle progression and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive cysteines have been characterized but specific 'sulphydryl switches' in replication proteins remain to be identified. In bovine papillomavirus type-1, DNA replication begins when the viral transcription factor E2 recruits the viral initiator protein E1 to the origin of DNA replication (ori). Here we show that a novel dimerization interface in the E2 transcription activation domain is stabilized by a disulphide bond. Oxidative cross-linking via Cys57 sequesters the interaction surface between E1 and E2, preventing pre-initiation and replication initiation complex formation. Our data demonstrate that as well as a mechanism for regulating DNA binding, redox reactions can control replication by modulating the tertiary structure of critical protein factors using a specific redox sensor.

Indexed as

DNA ReplicationCrystallography, X-RayCysteineDimerizationDNADNA-Binding ProteinsModels, MolecularOxidation-ReductionProtein Structure, TertiaryReplication OriginTrans-ActivatorsViral ProteinsCysteineDNADNA-Binding ProteinsE1 protein, Bovine papillomavirusE2 protein, Bovine papillomavirusTrans-ActivatorsViral Proteins

Identifiers

PMID17478495
PMCPMC1904295
OpenAlexW2131776884

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.