Evidence map›Paper›PMID 23650904›Full record

ArticleACS chemical neuroscience2013

Glutaraldehyde cross-linked glutamate oxidase coated microelectrode arrays: selectivity and resting levels of glutamate in the CNS.

Jason J Burmeister, Verda A Davis, Jorge E Quintero, Francois Pomerleau, Peter Huettl, Greg A Gerhardt

Open access · greenAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2013. 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
1.3field-weighted citation impact, top 23% 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, 46 citations in OpenAlex.

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  14. A Novel Microbiosensor Microarray for ContinuousFrontiers in neuroscience · 2018
    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.

Jason J BurmeisterDepartment of Anatomy and Neurobiology, Parkinson's Disease Translational Research Center of Excellence, University of Kentucky, Lexington, KY 40536-0098, United States.
Verda A Davis
Jorge E Quintero
Francois Pomerleau
Peter Huettl
Greg A Gerhardt
University of Kentucky · US

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
KENTUCKY CENTER FOR CLINICAL AND TRANSLATIONAL SCIENCEUL1RR033173 · NCRR · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2011 to 2011
$3.5M
Tonic and Phasic Glutamate Release from Psychomotor StimulantsR21DA033796 · NIDA · UNIVERSITY OF KENTUCKY · PI GERHARDT, GREG A. · 2012 to 2013
$364k
NCATS NIH HHS UL1 TR000117NCRR NIH HHS UL1 RR033173NCRR NIH HHS UL1RR033173-01NIDA NIH HHS R21DA033796-01
6 · The paper itself

Abstract

Glutaraldehyde is widely used as a cross-linking agent for enzyme immobilization onto microelectrodes. Recent studies and prior reports indicate changes in enzyme activity and selectivity with certain glutaraldehyde cross-linking procedures that may jeopardize the performance of microelectrode recordings and lead to falsely elevated responses in biological systems. In this study, the sensitivity of glutaraldehyde cross-linked glutamate oxidase-based microelectrode arrays to 22 amino acids was tested and compared to glutamate. As expected, responses to electroactive amino acids (Cys, Tyr, Trp) were detected at both nonenzyme-coated and enzyme-coated microelectrodes sites, while the remaining amino acids yielded no detectable responses. Electroactive amino acids were effectively blocked with a m-phenylene diamine (mPD) layer and, subsequently, no responses were detected. Preliminary results on the use of poly(ethylene glycol) diglycidyl ether (PEGDE) as a potentially more reliable cross-linking agent for the immobilization of glutamate oxidase onto ceramic-based microelectrode arrays are reported and show no significant advantages over glutaraldehyde as we observe comparable selectivities and responses. These results support that glutaraldehyde-cross-linked glutamate oxidase retains sufficient enzyme specificity for accurate in vivo brain measures of tonic and phasic glutamate levels when immobilized using specific "wet" coating procedures.

Indexed as

Amino Acid OxidoreductasesBiosensing TechniquesCross-Linking ReagentsEnzymes, ImmobilizedGlutamic AcidGlutaralMicroelectrodesAmino Acid OxidoreductasesCross-Linking ReagentsEnzymes, ImmobilizedGlutamic AcidGlutaralL-glutamate oxidase

Identifiers

PMID23650904
PMCPMC3656760
OpenAlexW2091424441

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.