Evidence map›Paper›PMID 16603489›Full record

ArticleBiophysical journal2006

The DNA binding activity of p53 displays reaction-diffusion kinetics.

Peter Hinow, Carl E Rogers, Christopher E Barbieri, Jennifer A Pietenpol, Anne K Kenworthy, Emmanuele DiBenedetto

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Transcription Factor Dynamics.Cold Spring Harbor perspectives in biology · 2021
    Review
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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

6 authors at 2 institutions in 1 country.

Peter HinowDepartment of Mathematics, Vanderbilt University, and Department of Biochemistry, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Nashville, Tennessee, USA.
Carl E Rogers
Christopher E Barbieri
Jennifer A Pietenpol
Anne K Kenworthy
Emmanuele DiBenedetto
Vanderbilt University · USVanderbilt University Medical Center · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
TrainingU54CA113007 · NCI · VANDERBILT UNIVERSITY · PI QUARANTA, VITO · 2004 to 2014
$19.2M
P53 SIGNALING AND CELLULAR RESPONSE AFTER STRESSR01CA070856 · NCI · VANDERBILT UNIVERSITY · PI PIETENPOL, JENNIFER A · 1997 to 2010
$3.8M
p63 Signaling in Epithelial Cell Growth and CancerR01CA105436 · NCI · VANDERBILT UNIVERSITY · PI PIETENPOL, JENNIFER A · 2004 to 2014
$3.1M
Mathematical Models of Dynamics of Visual TransductionR01GM068953 · NIGMS · VANDERBILT UNIVERSITY · PI DIBENEDETTO, EMMANUELE · 2003 to 2006
$933k
NCI NIH HHS 1-P50-CA113007-02NCI NIH HHS CA68485NCI NIH HHS CA70856NCI NIH HHS P30 CA068485NCI NIH HHS R01 CA070856NCI NIH HHS R01 CA105436NCI NIH HHS U54 CA113007NIEHS NIH HHS ES00267NIEHS NIH HHS P30 ES000267NIGMS NIH HHS 1-R01-GM 68953-01NIGMS NIH HHS R01 GM068953PHS HHS CAS105436
6 · The paper itself

Abstract

The tumor suppressor protein p53 plays a key role in maintaining the genomic stability of mammalian cells and preventing malignant transformation. In this study, we investigated the intracellular diffusion of a p53-GFP fusion protein using confocal fluorescence recovery after photobleaching. We show that the diffusion of p53-GFP within the nucleus is well described by a mathematical model for diffusion of particles that bind temporarily to a spatially homogeneous immobile structure with binding and release rates k1 and k2, respectively. The diffusion constant of p53-GFP was estimated to be Dp53-GFP=15.4 microm2 s-1, significantly slower than that of GFP alone, DGFP=41.6 microm2 s-1. The reaction rates of the binding and unbinding of p53-GFP were estimated as k1=0.3 s-1 and k2=0.4 s-1, respectively, values suggestive of nonspecific binding. Consistent with this finding, the diffusional mobilities of tumor-derived sequence-specific DNA binding mutants of p53 were indistinguishable from that of the wild-type protein. These data are consistent with a model in which, under steady-state conditions, p53 is latent and continuously scans DNA, requiring activation for sequence-specific DNA binding.

Indexed as

Models, BiologicalActive Transport, Cell NucleusBinding SitesCell NucleusComputer SimulationDiffusionDNADNA-Binding ProteinsKineticsModels, ChemicalProtein BindingTumor Suppressor Protein p53DNADNA-Binding ProteinsTumor Suppressor Protein p53

Identifiers

PMID16603489
PMCPMC1479054
OpenAlexW2009071546

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.