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

Targeted mutations of Bacillus anthracis dihydrofolate reductase condense complex structure−activity relationships.

Journal of medicinal chemistry - 28 Oct 2010

Beierlein Jennifer M, Karri Nanda G, Anderson Amy C

Abstract excerpt

Several antifolates, including trimethoprim (TMP) and a series of propargyl-linked analogues, bind dihydrofolate reductase from Bacillus anthracis (BaDHFR) with lower affinity than is typical in other bacterial species. To guide lead optimization for BaDHFR, we explored a new approach to determine structure-activity relationships whereby the enzyme is altered and the analogues remain constant, essentially...

Read the complete abstract on PubMed

Topics

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

Share to Alkynes
Share to Bacillus anthracis
Share to Biphenyl Compounds

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Folic Acid Antagonists

Share to Hydrogen Bonding

Share to Pyrimidines

Share to Static Electricity

Share to Tetrahydrofolate Dehydrogenase

Source

Open in PubMed Open full text

Identifiers

PMID: 20882962
DOI: 10.1021/jm100727t
PMCID: PMC3618964

Genes

DHFR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeted mutations of Bacillus anthracis dihydrofolate reductase condense complex structure−activity relationships.PMID 20882962Read ↗

Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: sequence and structural comparison.Semantic proximity Read ↗

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

In vitro efficacy of new antifolates against trimethoprim-resistant Bacillus anthracis.Semantic proximity Read ↗

Structural analysis of dihydrofolate reductases enables rationalization of antifolate binding affinities and suggests repurposing possibilitiesSemantic proximity Read ↗

Molecular modeling toward selective inhibitors of dihydrofolate reductase from the biological warfare agent Bacillus anthracis.Semantic proximity Read ↗

Charged Propargyl-Linked Antifolates Reveal Mechanisms of Antifolate Resistance and Inhibit Trimethoprim-Resistant MRSA Strains Possessing Clinically Relevant MutationsSemantic proximity Read ↗

Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance.Semantic proximity Read ↗

Inhibition of Antibiotic-Resistant Staphylococcus aureus by the Broad-Spectrum Dihydrofolate Reductase Inhibitor RAB1Semantic proximity Read ↗

Winning the arms race by improving drug discovery against mutating targets.Semantic proximity Read ↗

Hybrid Inhibitors of Malarial Dihydrofolate Reductase with Dual Binding Modes That Can Forestall ResistanceSemantic proximity Read ↗

Mutations in rv0678 Confer Low-Level Resistance to Benzothiazinone DprE1 Inhibitors in Mycobacterium tuberculosis.Semantic proximity Read ↗

Achieving the promise and avoiding the peril of chemical probes using genetics.Semantic proximity Read ↗

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