Evidence map›Paper›PMID 22384805›Full record

ReviewCurrent gene therapy2012

Enzymes to die for: exploiting nucleotide metabolizing enzymes for cancer gene therapy.

Andressa Ardiani, Adam J Johnson, Hongmei Ruan, Marilyn Sanchez-Bonilla, Kinta Serve, Margaret E Black

Open access · bronzeAbstract readReview
In one paragraph

Review in Current gene therapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  10. Antitumor efficacy of combined gene and radiotherapy in animals.Doklady. Biochemistry and biophysics · 2016
    Article
  11. Review
  12. Article
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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 1 institution in 1 country.

Andressa ArdianiSchool of Molecular Biosciences, Washington State University, Pullman, 99164-7520, USA.
Adam J Johnson
Hongmei Ruan
Marilyn Sanchez-Bonilla
Kinta Serve
Margaret E Black
Washington State University · US

Funding

TRAINING IN BIOTECHNOLOGY: EMPHASIS ON PROTEIN CHEMISTRYT32GM008336 · NIGMS · WASHINGTON STATE UNIVERSITY · PI CALL, DOUGLAS R. · 1989 to 2023
$8.9M
IMPROVING SUICIDE GENES FOR CANCER GENE THERAPYR01CA085939 · NCI · WASHINGTON STATE UNIVERSITY · PI BLACK, MARGARET E · 2000 to 2009
$2.3M
NCI NIH HHS R01 CA085939NIGMS NIH HHS T32 GM008336
6 · The paper itself

Abstract

Suicide gene therapy is an attractive strategy to selectively destroy cancer cells while minimizing unnecessary toxicity to normal cells. Since this idea was first introduced more than two decades ago, numerous studies have been conducted and significant developments have been made to further its application for mainstream cancer therapy. Major limitations of the suicide gene therapy strategy that have hindered its clinical application include inefficient directed delivery to cancer cells and the poor prodrug activation capacity of suicide enzymes. This review is focused on efforts that have been and are currently being pursued to improve the activity of individual suicide enzymes towards their respective prodrugs with particular attention to the application of nucleotide metabolizing enzymes in suicide cancer gene therapy. A number of protein engineering strategies have been employed and our discussion here will center on the use of mutagenesis approaches to create and evaluate nucleotide metabolizing enzymes with enhanced prodrug activation capacity and increased thermostability. Several of these studies have yielded clinically important enzyme variants that are relevant for cancer gene therapy applications because their utilization can serve to maximize cancer cell killing while minimizing the prodrug dose, thereby limiting undesirable side effects.

Indexed as

Adenosine DeaminaseEnzymesGenetic TherapyHumansNeoplasmsNucleoside DeaminasesNucleotidasesNucleotidesProdrugsPurine-Nucleoside PhosphorylaseAdenosine DeaminaseEnzymesNucleoside DeaminasesNucleotidasesNucleotidesProdrugsPurine-Nucleoside Phosphorylase

Identifiers

PMID22384805
PMCPMC3551574
OpenAlexW1968373934

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.