Evidence map›Paper›PMID 19040357›Full record

ArticleBiological chemistry2009

Aptamers selected against the unglycosylated EGFRvIII ectodomain and delivered intracellularly reduce membrane-bound EGFRvIII and induce apoptosis.

Yingmiao Liu, Chien-Tsun Kuan, Jing Mi, Xiuwu Zhang, Bryan M Clary, Darell D Bigner, Bruce A Sullenger

Abstract read
In one paragraph

Article in Biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

39 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
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  6. Therapeutic Potential of Aptamer-Protein Interactions.ACS pharmacology & translational science · 2022
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  9. Article
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  11. Aptamers and antibodies: rivals or allies in cancer targeted therapy?Exploration of targeted anti-tumor therapy · 2021
    Review
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  13. 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

7 authors at 2 institutions in 1 country.

Yingmiao LiuDepartment of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Chien-Tsun Kuan
Jing Mi
Xiuwu Zhang
Bryan M Clary
Darell D Bigner
Bruce A Sullenger
Duke Medical Center · USDuke University Hospital · US

Funding

"Smart" Nanoparticles for Cancer Therapy and ImagingU54CA119343 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI VAN DYKE, TERRY A · 2005 to 2009
$18.3M
TUMOR SUPPRESSOR GENES IN HUMAN MEDULLOBLASTOMAP50NS020023 · NINDS · DUKE UNIVERSITY · PI BIGNER, DARELL D · 1985 to 2013
$17.3M
TEMODAR RESISTANCE IN CENTRAL NERVOUS SYSTEMP50CA108786 · NCI · DUKE UNIVERSITY · PI BIGNER, DARELL D · 2004 to 2009
$12.3M
TRANSPORT AND DELIVERY OF ANTISNESE OLIGONUCLEOTIDESP01GM059299 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JULIANO, RUDOLPH · 2000 to 2010
$11.7M
BRAIN TUMORS: IMMUNOLOGICAL AND BIOLOGICAL STUDIESR37CA011898 · NCI · DUKE UNIVERSITY · PI BIGNER, DARELL D · 1988 to 2012
$8.1M
NCI NIH HHS 5P50 CA108786-05NCI NIH HHS P50 CA108786NCI NIH HHS R37 CA011898NCI NIH HHS R37 CA 011898-38NCI NIH HHS U54 CA119343NCI NIH HHS U54-CA-119343NIGMS NIH HHS P01 GM059299NINDS NIH HHS 5P50 NS20023-25NINDS NIH HHS P50 NS020023
6 · The paper itself

Abstract

Epidermal growth factor receptor variant III (EGFRvIII) is a glycoprotein uniquely expressed in glioblastoma, but not in normal brain tissues. To develop targeted therapies for brain tumors, we selected RNA aptamers against the histidine-tagged EGFRvIII ectodomain, using an Escherichia coli system for protein expression and purification. Representative aptamer E21 has a dissociation constant (Kd) of 33x10(-9) m, and exhibits high affinity and specificity for EGFRvIII in ELISA and surface plasmon resonance assays. However, selected aptamers cannot bind the same protein expressed from eukaryotic cells because glycosylation, a post-translational modification present only in eukaryotic systems, significantly alters the structure of the target protein. By transfecting EGFRvIII aptamers into cells, we find that membrane-bound, glycosylated EGFRvIII is reduced and the percentage of cells undergoing apoptosis is increased. We postulate that transfected aptamers can interact with newly synthesized EGFRvIII, disrupt proper glycosylation, and reduce the amount of mature EGFRvIII reaching the cell surface. Our work establishes the feasibility of disrupting protein post-translational modifications in situ with aptamers. This finding is useful for elucidating the function of proteins of interest with various modifications, as well as dissecting signal transduction pathways.

Indexed as

ApoptosisRNA Processing, Post-TranscriptionalAnimalsAptamers, NucleotideBase SequenceBlotting, WesternCell LineCell MembraneCell SurvivalEnzyme-Linked Immunosorbent AssayErbB ReceptorsMiceMolecular Sequence DataSELEX Aptamer TechniqueAptamers, Nucleotideepidermal growth factor receptor VIIIErbB Receptors

Identifiers

PMID19040357
PMCPMC3816755
OpenAlexW2062918977

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.