Literature DB >> 17867707

An aminoglycoside microarray platform for directly monitoring and studying antibiotic resistance.

Matthew D Disney1, Olivia J Barrett.   

Abstract

Antibiotic resistance is a major threat to human health. Since resistance to the aminoglycoside class of antibiotics is most commonly caused by enzymatic modification, we developed a high-throughput microarray platform for directly assaying resistance enzyme activity on aminoglycosides. After modification, the array can be hybridized with the therapeutic target, a bacterial rRNA A-site mimic, to study the effect that modification has on binding. Such studies will help identify important factors that contribute to high-affinity recognition of therapeutic targets and low-affinity recognition of and modification by resistance enzymes. This platform may also be useful for screening chemical libraries to discover new antibiotics that evade resistance.

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Year:  2007        PMID: 17867707     DOI: 10.1021/bi701071h

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  16 in total

1.  Studying aminoglycoside modification by the acetyltransferase class of resistance-causing enzymes via microarray.

Authors:  Olivia J Barrett; Alexei Pushechnikov; Meilan Wu; Matthew D Disney
Journal:  Carbohydr Res       Date:  2008-08-22       Impact factor: 2.104

2.  Influencing uptake and localization of aminoglycoside-functionalized peptoids.

Authors:  Melissa M Lee; Jonathan M French; Matthew D Disney
Journal:  Mol Biosyst       Date:  2011-05-24

3.  Studying modification of aminoglycoside antibiotics by resistance-causing enzymes via microarray.

Authors:  Matthew D Disney
Journal:  Methods Mol Biol       Date:  2012

Review 4.  Comprehensive review of chemical strategies for the preparation of new aminoglycosides and their biological activities.

Authors:  Nishad Thamban Chandrika; Sylvie Garneau-Tsodikova
Journal:  Chem Soc Rev       Date:  2018-02-19       Impact factor: 54.564

Review 5.  Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections.

Authors:  Kristin J Labby; Sylvie Garneau-Tsodikova
Journal:  Future Med Chem       Date:  2013-07       Impact factor: 3.808

6.  Defining RNA motif-aminoglycoside interactions via two-dimensional combinatorial screening and structure-activity relationships through sequencing.

Authors:  Sai Pradeep Velagapudi; Matthew D Disney
Journal:  Bioorg Med Chem       Date:  2013-05-07       Impact factor: 3.641

7.  Small molecule microarrays of RNA-focused peptoids help identify inhibitors of a pathogenic group I intron.

Authors:  Lucas P Labuda; Alexei Pushechnikov; Matthew D Disney
Journal:  ACS Chem Biol       Date:  2009-04-17       Impact factor: 5.100

8.  Dual Targeting of Intracellular Pathogenic Bacteria with a Cleavable Conjugate of Kanamycin and an Antibacterial Cell-Penetrating Peptide.

Authors:  Anna Brezden; Mohamed F Mohamed; Manish Nepal; John S Harwood; Jerrin Kuriakose; Mohamed N Seleem; Jean Chmielewski
Journal:  J Am Chem Soc       Date:  2016-08-17       Impact factor: 15.419

9.  Probing a 2-aminobenzimidazole library for binding to RNA internal loops via two-dimensional combinatorial screening.

Authors:  Sai Pradeep Velagapudi; Alexei Pushechnikov; Lucas P Labuda; Jonathan M French; Matthew D Disney
Journal:  ACS Chem Biol       Date:  2012-09-14       Impact factor: 5.100

10.  Two-dimensional combinatorial screening and the RNA Privileged Space Predictor program efficiently identify aminoglycoside-RNA hairpin loop interactions.

Authors:  Dustin J Paul; Steven J Seedhouse; Matthew D Disney
Journal:  Nucleic Acids Res       Date:  2009-09-02       Impact factor: 16.971

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