Evidence map›Paper›PMID 23625637›Full record

ArticleThe Laryngoscope2013

Serine substitution of proline at codon 151 of TP53 confers gain of function activity leading to anoikis resistance and tumor progression of head and neck cancer cells.

Tong-Xin Xie, Ge Zhou, Mei Zhao, Daisuke Sano, Samar A Jasser, Richard G Brennan, Jeffrey N Myers

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Laryngoscope, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

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  8. Molecular crosstalk between cancer and neurodegenerative diseases.Cellular and molecular life sciences : CMLS · 2020
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  16. OncomorphicJournal of cancer therapy · 2014
    Article
  17. Review
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

7 authors at 2 institutions in 1 country.

Tong-Xin XieDepartments of Head and Neck Surgery, University of Texas M D Anderson Cancer Center, Houston, Texas 77030, USA.
Ge Zhou
Mei Zhao
Daisuke Sano
Samar A Jasser
Richard G Brennan
Jeffrey N Myers
The University of Texas MD Anderson Cancer Center · USDuke University · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
Targeting the p53 pathway for reversal of oral premalignancyP50CA097007 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI MYERS, JEFFREY NICHOLAS · 2002 to 2012
$26.1M
Progression of Metastasis of Oral Tongue CancerR01DE014613 · NIDCR · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI MYERS, JEFFREY NICHOLAS · 2003 to 2018
$5.4M
NCI NIH HHS CA016672NCI NIH HHS P30 CA016672NCI NIH HHS P50 CA097007NCI NIH HHS P50CA097007NIDCR NIH HHS R01 DE014613
6 · The paper itself

Abstract

objectives/hypothesisMutation of the TP53 gene occurs in more than half of cases of head and neck squamous cell carcinoma (HNSCC). However, little is known about how specific TP53 mutations affect tumor progression. The objective of this study is to determine the gain of function of mutant p53 with a proline-to-serine substitution at codon 151. STUDY

designLaboratory-based study.

methodsA panel of HNSCC cell lines was determined with anoikis assays, and orthotopic mouse experiments were performed. TP53 was sequenced. The shRNA knockdown and overexpression approaches were used for testing mutant p53 functions. The crystal structure of the p53 protein was analyzed using an in silico approach.

resultsAn anoikis-resistant cell line, Tu138, was found to have a proline-to-serine substitution at codon 151 of TP53, which results in loss of wild-type p53 transcriptional activity. Moreover, the mutant p53 was shown to promote anoikis resistance and soft agar growth. Using an in silico approach based on the crystal structure of wild-type p53 protein, substitution of proline by serine at position 151 would create a cavity in a hydrophobic pocket, the loss of van der Waals contacts, and the thermodynamically unfavorable placement of a polar group, the hydroxyl oxygen atom of the serine, within a hydrophobic region, all of which likely cause a locally altered structure.

conclusionsOur data suggest that mutation at position 151 leads to a structural alteration, which results in significant functional changes in the p53 protein that impact tumor progression.

Indexed as

MutationAnimalsAnoikisBlotting, WesternCarcinoma, Squamous CellCell Line, TumorCodonDisease ProgressionDNA, NeoplasmHead and Neck NeoplasmsMiceMice, NudeNeoplasms, ExperimentalProlineReverse Transcriptase Polymerase Chain ReactionSerineCodonDNA, NeoplasmProlineSerineTumor Suppressor Protein p53

Identifiers

PMID23625637
PMCPMC3664100
OpenAlexW1605143200

What OpenQuestion holds

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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.