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

Cloning and Characterization of a Novel Trimethoprim-Resistant Dihydrofolate Reductase from a Nosocomial Isolate of Staphylococcus aureus CM.S2 (IMCJ1454)

26 Aug 2005

Abstract excerpt

A novel gene, dfrG, encoding a trimethoprim (TMP)-resistant dihydrofolate reductase (DHFR, designated S3DHFR) was cloned from a clinical isolate of methicillin-resistant Staphylococcus aureus. Escherichia coli expressing dfrG was highly resistant to TMP. Recombinant S3DHFR exhibited DHFR activity that was not inhibited by TMP.

Read the complete abstract on PubMed

Topics

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

Share to Antibiotic Resistance in Bacteria
Share to Antimicrobial Resistance in Staphylococcus
Share to Clostridium difficile and Clostridium perfringens research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 16127079
DOI: 10.1128/aac.49.9.3948-3951.2005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cloning and Characterization of a Novel Trimethoprim-Resistant Dihydrofolate Reductase from a Nosocomial Isolate of Staphylococcus aureus CM.S2 (IMCJ1454)PMID 16127079Read ↗

Toward Broad Spectrum Dihydrofolate Reductase Inhibitors Targeting Trimethoprim Resistant Enzymes Identified in Clinical Isolates of Methicillin Resistant Staphylococcus aureusSemantic proximity Read ↗

Emergence of trimethoprim resistance gene dfrG in Staphylococcus aureus causing human infection and colonization in sub-Saharan Africa and its import to EuropeSemantic proximity Read ↗

Towards the understanding of resistance mechanisms in clinically isolated trimethoprim-resistant, methicillin-resistant Staphylococcus aureus dihydrofolate reductaseSemantic proximity Read ↗

Integron-Associated DfrB4, a Previously Uncharacterized Member of the Trimethoprim-Resistant Dihydrofolate Reductase B Family, Is a Clinically Identified Emergent Source of Antibiotic ResistanceSemantic proximity Read ↗

Mutations in the dihydrofolate reductase gene of trimethoprim-resistant isolates of Streptococcus pneumoniaeSemantic proximity Read ↗

Novel trimethoprim resistance gene dfrA34 identified in Salmonella Heidelberg in the USASemantic proximity Read ↗

Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim.Semantic proximity Read ↗

The Structural and Functional Basis for Recurring Sulfa Drug Resistance Mutations in Staphylococcus aureus Dihydropteroate SynthaseSemantic proximity Read ↗

Prospective screening of novel antibacterial inhibitors of dihydrofolate reductase for mutational resistance.Semantic proximity Read ↗

In vitro development of resistance to a novel fluoroquinolone, DW286, in methicillin-resistant Staphylococcus aureus clinical isolates.Semantic proximity Read ↗

Increased hydrophobic interactions of iclaprim with Staphylococcus aureus dihydrofolate reductase are responsible for the increase in affinity and antibacterial activitySemantic proximity Read ↗

Crystal structures of wild-type and mutant methicillin-resistant Staphylococcus aureus dihydrofolate reductase reveal an alternate conformation of NADPH that may be linked to trimethoprim resistance.Semantic proximity Read ↗

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