Evidence map›Paper›PMID 12930964›Full record

ArticleNucleic acids research2003

Solution measurement of DNA curvature in papillomavirus E2 binding sites.

Jeff M Zimmerman, L James Maher

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 20 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

2 authors at 1 institution in 1 country.

Jeff M ZimmermanDepartment of Biochemistry and Molecular Biology, Mayo Clinic-Rochester, 200 First Street SW, Rochester, MN 55905, USA.
L James Maher
Mayo Clinic · US

Funding

ELECTROSTATIC FORCES IN DNA BENDING BY PROTEINSR01GM054411 · NIGMS · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI MAHER, LOUIS JAMES · 1995 to 2003
$846k
NIGMS NIH HHS GM54411NIGMS NIH HHS R01 GM054411
6 · The paper itself

Abstract

'Indirect readout' refers to the proposal that proteins can recognize the intrinsic three-dimensional shape or flexibility of a DNA binding sequence apart from direct protein contact with DNA base pairs. The differing affinities of human papillomavirus (HPV) E2 proteins for different E2 binding sites have been proposed to reflect indirect readout. DNA bending has been observed in X-ray structures of E2 protein-DNA complexes. X-ray structures of three different E2 DNA binding sites revealed differences in intrinsic curvature. DNA sites with intrinsic curvature in the direction of protein-induced bending were bound more tightly by E2 proteins, supporting the indirect readout model. We now report solution measurements of intrinsic DNA curvature for three E2 binding sites using a sensitive electrophoretic phasing assay. Measured E2 site curvature agrees well the predictions of a dinucleotide model and supports an indirect readout hypothesis for DNA recognition by HPV E2.

Indexed as

Nucleic Acid ConformationAlgorithmsBinding, CompetitiveBinding SitesDNAModels, MolecularOligonucleotidesPapillomaviridaeSolutionsViral ProteinsDNAOligonucleotidesSolutionsViral Proteins

Identifiers

PMID12930964
PMCPMC212797
OpenAlexW2045163977

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.