Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification and characteristics of a novel aminoglycoside phosphotransferase, APH(3′)-IId, from an MDR clinical isolate of Brucella intermedia

13 Jul 2021

Abstract excerpt

OBJECTIVES: To describe a novel chromosomal aminoglycoside phosphotransferase named APH(3')-IId identified in an MDR Brucella intermedia ZJ499 isolate from a cancer patient. METHODS: Species identity was determined by PCR and MALDI-TOF MS analysis. WGS was performed to determine the genetic elements conferring antimicrobial resistance. Gene cloning, transcriptional analysis and targeted gene deletion, as well as...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Brucella: diagnosis, epidemiology, treatment
Share to Burkholderia infections and melioidosis
Share to Fungal Infections and Studies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34329431
DOI: 10.1093/jac/dkab272

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characteristics of a novel aminoglycoside phosphotransferase, APH(3′)-IId, from an MDR clinical isolate of Brucella intermediaPMID 34329431Read ↗

Identification and characterization of a novel chromosomal aminoglycoside 3’-O-phosphotransferase, APH(3′)-Id, from Kluyvera intermedia DW18 isolated from the sewage of an animal farmSemantic proximity Read ↗

APH(3’)-Ie, an aminoglycoside-modifying enzyme discovered in a rabbit-derived Citrobacter gillenii isolateSemantic proximity Read ↗

Aph(3')-IIc, an aminoglycoside resistance determinant from Stenotrophomonas maltophilia.Semantic proximity Read ↗

Functional characterization of a novel aminoglycoside phosphotransferase, APH(9)-Ic, and its variant from Stenotrophomonas maltophiliaSemantic proximity Read ↗

Aminoglycoside phosphotransferases: proteins, structure, and mechanismSemantic proximity Read ↗

A novel chromosomal aminoglycoside 6′-N-acetyltransferase, AAC(6′)-Io, confers resistance to multiple aminoglycosides identified from Bacillus cereusSemantic proximity Read ↗

aph(3')-IIb, a gene encoding an aminoglycoside-modifying enzyme, is under the positive control of surrogate regulator HpaA.Semantic proximity Read ↗

Structure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophilaSemantic proximity Read ↗

Structural characterization of aminoglycoside 4′‐ O ‐adenylyltransferase ANT(4′)‐IIb from Pseudomonas aeruginosaSemantic proximity Read ↗

Mutant APH(2'')-IIa enzymes with increased activity against amikacin and isepamicin.Semantic proximity Read ↗

Mycobacterial Aminoglycoside Acetyltransferases: A Little of Drug Resistance, and a Lot of Other RolesSemantic proximity Read ↗

Detection of a novel aph(2") allele (aph[2"]-Ie) conferring high-level gentamicin resistance and a spectinomycin resistance gene ant(9)-Ia (aad 9) in clinical isolates of enterococci.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.