Evidence map›Paper›PMID 19865164›Full record

ArticleNature2009

The role of DNA shape in protein-DNA recognition.

Remo Rohs, Sean M West, Alona Sosinsky, Peng Liu, Richard S Mann, Barry Honig

Open access · greenAbstract read
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 634 papers.

0numbers the graph read from it
0cells of the map it votes in
634citing papers in PubMed
23.5field-weighted citation impact, top 1% 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

634 citing papers in PubMed, 1,121 citations in OpenAlex.

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  15. hexABC seeking the physical code of DNA.Nature communications · 2026
    Article
  16. Review
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574 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Remo RohsHoward Hughes Medical Institute, Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biophysics, Columbia University, 1130 Saint Nicholas Avenue, New York, New York 10032, USA.
Sean M West
Alona Sosinsky
Peng Liu
Richard S Mann
Barry Honig
Columbia University · USHoward Hughes Medical Institute · US

Funding

Nation Center: Multi-Scale Study- Cellular Networks(RMI)U54CA121852 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CALIFANO, ANDREA · 2005 to 2015
$37.4M
MOLECULAR GENETICS OF SEGMENT IDENTITYR01GM054510 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MANN, RICHARD S · 1996 to 2015
$5.5M
COMPUTER STUDIES OF PROTEIN STRUCTURE AND FUNCTIONR01GM030518 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HONIG, BARRY H · 1985 to 2020
$4.5M
Howard Hughes Medical InstituteNCI NIH HHS U54 CA121852NIGMS NIH HHS GM54510NIGMS NIH HHS R01 GM030518NIGMS NIH HHS R01 GM054510
6 · The paper itself

Abstract

The recognition of specific DNA sequences by proteins is thought to depend on two types of mechanism: one that involves the formation of hydrogen bonds with specific bases, primarily in the major groove, and one involving sequence-dependent deformations of the DNA helix. By comprehensively analysing the three-dimensional structures of protein-DNA complexes, here we show that the binding of arginine residues to narrow minor grooves is a widely used mode for protein-DNA recognition. This readout mechanism exploits the phenomenon that narrow minor grooves strongly enhance the negative electrostatic potential of the DNA. The nucleosome core particle offers a prominent example of this effect. Minor-groove narrowing is often associated with the presence of A-tracts, AT-rich sequences that exclude the flexible TpA step. These findings indicate that the ability to detect local variations in DNA shape and electrostatic potential is a general mechanism that enables proteins to use information in the minor groove, which otherwise offers few opportunities for the formation of base-specific hydrogen bonds, to achieve DNA-binding specificity.

Indexed as

Nucleic Acid ConformationAnimalsArginineAT Rich SequenceBase SequenceDatabases, FactualDNADNA-Binding ProteinsHydrogen BondingLysineNucleosomesProtein BindingSaccharomyces cerevisiaeStatic ElectricityArginineDNADNA-Binding ProteinsLysineNucleosomes

Identifiers

PMID19865164
PMCPMC2793086
OpenAlexW2012627860

What OpenQuestion holds

Textmetadata
LicenceTDM
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.