Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim

Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim

Item
http://www.wikidata.org/entity/Q27654074
Towards the understanding of resistance mechanisms in clinically isolated trimethoprim-resistant, methicillin-resistant Staphylococcus aureus dihydrofolate reductaseInhibition of Antibiotic-Resistant Staphylococcus aureus by the Broad-Spectrum Dihydrofolate Reductase Inhibitor RAB1Structural genomics for drug design against the pathogen Coxiella burnetiiSequencing and genetic variation of multidrug resistance plasmids in Klebsiella pneumoniaeAvoidable errors in deposited macromolecular structures: an impediment to efficient data mining.Antifolate agents: a patent review (2006 - 2010).Protein design algorithms predict viable resistance to an experimental antifolateIdentification of novel potential antibiotics against Staphylococcus using structure-based drug screening targeting dihydrofolate reductaseExamination of bacterial inhibition using a catalytic DNANonracemic Antifolates Stereoselectively Recruit Alternate Cofactors and Overcome Resistance in S. aureus.Sulfa and trimethoprim-like drugs - antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors.Antibacterial Antifolates: From Development through Resistance to the Next GenerationAnalysis of Coxiela burnetti dihydrofolate reductase via in silico docking with inhibitors and molecular dynamics simulation.MRSA Isolates from United States Hospitals Carry dfrG and dfrK Resistance Genes and Succumb to Propargyl-Linked Antifolates.Charged Propargyl-Linked Antifolates Reveal Mechanisms of Antifolate Resistance and Inhibit Trimethoprim-Resistant MRSA Strains Possessing Clinically Relevant Mutations.Localized light-induced protein dimerization in living cells using a photocaged dimerizer.Increased substrate affinity in the Escherichia coli L28R dihydrofolate reductase mutant causes trimethoprim resistance.
P2860

Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim

Item
http://www.wikidata.org/entity/Q27654074
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural comparison of chrom ...... potent inhibitor trimethoprim
@ast
Structural comparison of chrom ...... potent inhibitor trimethoprim
@en
Structural comparison of chrom ...... potent inhibitor trimethoprim
@nl
type
label
Structural comparison of chrom ...... potent inhibitor trimethoprim
@ast
Structural comparison of chrom ...... potent inhibitor trimethoprim
@en
Structural comparison of chrom ...... potent inhibitor trimethoprim
@nl
prefLabel
Structural comparison of chrom ...... potent inhibitor trimethoprim
@ast
Structural comparison of chrom ...... potent inhibitor trimethoprim
@en
Structural comparison of chrom ...... potent inhibitor trimethoprim
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Structural comparison of chrom ...... potent inhibitor trimethoprim
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698