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dc.contributor.author
Ramirez, Maria Soledad
dc.contributor.author
Tolmasky, Marcelo E.
dc.date.available
2019-01-07T19:12:52Z
dc.date.issued
2010-09
dc.identifier.citation
Ramirez, Maria Soledad; Tolmasky, Marcelo E.; Aminoglycoside modifying enzymes; Churchill Livingstone; Drug Resistance Updates; 13; 6; 9-2010; 151-171
dc.identifier.issn
1368-7646
dc.identifier.uri
http://hdl.handle.net/11336/67587
dc.description.abstract
Aminoglycosides have been an essential component of the armamentarium in the treatment of life-threatening infections. Unfortunately, their efficacy has been reduced by the surge and dissemination of resistance. In some cases the levels of resistance reached the point that rendered them virtually useless. Among many known mechanisms of resistance to aminoglycosides, enzymatic modification is the most prevalent in the clinical setting. Aminoglycoside modifying enzymes catalyze the modification at different -OH or -NH2 groups of the 2-deoxystreptamine nucleus or the sugar moieties and can be nucleotidyltranferases, phosphotransferases, or acetyltransferases. The number of aminoglycoside modifying enzymes identified to date as well as the genetic environments where the coding genes are located is impressive and there is virtually no bacteria that is unable to support enzymatic resistance to aminoglycosides. Aside from the development of new aminoglycosides refractory to as many as possible modifying enzymes there are currently two main strategies being pursued to overcome the action of aminoglycoside modifying enzymes. Their successful development would extend the useful life of existing antibiotics that have proven effective in the treatment of infections. These strategies consist of the development of inhibitors of the enzymatic action or of the expression of the modifying enzymes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Churchill Livingstone
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Acetyltransferase
dc.subject
Aminoglycoside
dc.subject
Aminoglycoside Modifying Enzyme
dc.subject
Antibiotic Resistance
dc.subject
Antisense
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Bacterial Infection
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Kinase
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Nucleotidyltransferase
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Phosphotransferase
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Rnase H
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Rnase P
dc.subject.classification
Otras Ciencias Biológicas
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Aminoglycoside modifying enzymes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-07T13:33:24Z
dc.journal.volume
13
dc.journal.number
6
dc.journal.pagination
151-171
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Ramirez, Maria Soledad. California State University Fullerton; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; Argentina
dc.description.fil
Fil: Tolmasky, Marcelo E.. California State University Fullerton; Estados Unidos
dc.journal.title
Drug Resistance Updates
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.drup.2010.08.003
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1368764610000385
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2992599/


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