Evidence map›Paper›PMID 24293651›Full record

ArticleNucleic acids research2014

Conformations of p53 response elements in solution deduced using site-directed spin labeling and Monte Carlo sampling.

Xiaojun Zhang, Ana Carolina Dantas Machado, Yuan Ding, Yongheng Chen, Yan Lu, Yankun Duan, Kenneth W Tham, Lin Chen, Remo Rohs, Peter Z Qin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. 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
1.9field-weighted citation impact, top 14% 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, 25 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

10 authors at 1 institution in 1 country.

Xiaojun ZhangDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA and Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.
Ana Carolina Dantas Machado
Yuan Ding
Yongheng Chen
Yan Lu
Yankun Duan
Kenneth W Tham
Lin Chen
Remo Rohs
Peter Z Qin
University of Southern California · US

Funding

NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
Inferring regulatory circuitry from microarray dataR01HG003008 · NHGRI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI BUSSEMAKER, HARMEN J · 2004 to 2020
$7.0M
Structural and Functional Versatility of NFATR01GM064642 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, LIN · 2005 to 2014
$2.5M
Multi-scale modeling of genetic variation in a developmental networkU01GM103804 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DEPACE, ANGELA H, MARJORAM, PAUL · 2013 to 2016
$2.0M
Structure, dynamics, and function of the packaging RNAR01GM069557 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI QIN, PETER Z · 2006 to 2010
$1.4M
Acquisition of a Pulse Electron Paramagnetic Resonance SpectrometerS10RR028992 · NCRR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI QIN, PETER Z · 2010 to 2010
$1.0M
NCRR NIH HHS 2U54RR022220NCRR NIH HHS RR028992NHGRI NIH HHS R01 HG003008NIGMS NIH HHS GM069557NIGMS NIH HHS R01 GM064642NIGMS NIH HHS R01GM064642NIGMS NIH HHS U01 GM103804NIGMS NIH HHS U01GM103804
6 · The paper itself

Abstract

The tumor suppressor protein p53 regulates numerous signaling pathways by specifically recognizing diverse p53 response elements (REs). Understanding the mechanisms of p53-DNA interaction requires structural information on p53 REs. However, such information is limited as a 3D structure of any RE in the unbound form is not available yet. Here, site-directed spin labeling was used to probe the solution structures of REs involved in p53 regulation of the p21 and Bax genes. Multiple nanometer distances in the p21-RE and BAX-RE, measured using a nucleotide-independent nitroxide probe and double-electron-electron-resonance spectroscopy, were used to derive molecular models of unbound REs from pools of all-atom structures generated by Monte-Carlo simulations, thus enabling analyses to reveal sequence-dependent DNA shape features of unbound REs in solution. The data revealed distinct RE conformational changes on binding to the p53 core domain, and support the hypothesis that sequence-dependent properties encoded in REs are exploited by p53 to achieve the energetically most favorable mode of deformation, consequently enhancing binding specificity. This work reveals mechanisms of p53-DNA recognition, and establishes a new experimental/computational approach for studying DNA shape in solution that has far-reaching implications for studying protein-DNA interactions.

Indexed as

Response ElementsDNAElectron Spin Resonance SpectroscopyMonte Carlo MethodNucleic Acid ConformationProtein BindingProtein Structure, TertiarySpin LabelsTumor Suppressor Protein p53DNASpin LabelsTumor Suppressor Protein p53

Identifiers

PMID24293651
PMCPMC3936745
OpenAlexW2114308174

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.