Binding site of the bridged macrolides in the Escherichia coli ribosome.
about
Binding and action of CEM-101, a new fluoroketolide antibiotic that inhibits protein synthesisR chi-01, a new family of oxazolidinones that overcome ribosome-based linezolid resistanceThe structure of ribosome-lankacidin complex reveals ribosomal sites for synergistic antibioticsStructures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug actionRevisiting the structures of several antibiotics bound to the bacterial ribosomeThe bacterial ribosome as a target for antibioticsReduced ribosomes of the apicoplast and mitochondrion of Plasmodium spp. and predicted interactions with antibioticsRecombineering reveals a diverse collection of ribosomal proteins L4 and L22 that confer resistance to macrolide antibiotics.In vitro activity of the new fluoroketolide solithromycin (CEM-101) against macrolide-resistant and -susceptible Mycoplasma genitalium strains.The key function of a conserved and modified rRNA residue in the ribosomal response to the nascent peptide.Macrolide-peptide conjugates as probes of the path of travel of the nascent peptides through the ribosome.Impact of P-Site tRNA and antibiotics on ribosome mediated protein folding: studies using the Escherichia coli ribosomeIsolation of translating ribosomes containing peptidyl-tRNAs for functional and structural analysesNew advances in antibiotic development and discovery.The ribosomal peptidyl transferase center: structure, function, evolution, inhibition.Pharmacokinetics of EDP-420 after ascending single oral doses in healthy adult volunteers.Macrolide myths.Natural product scaffolds as leads to drugs.Macrolide antibiotics in the ribosome exit tunnel: species-specific binding and action.The chemistry of peptidyltransferase center-targeted antibiotics: enzymatic resistance and approaches to countering resistance.Insights into the mode of action of novel fluoroketolides, potent inhibitors of bacterial protein synthesisNested PCR-linked capillary electrophoresis and single-strand conformation polymorphisms for detection of macrolide-resistant Mycoplasma pneumoniae in Beijing, ChinaDistinct mode of interaction of a novel ketolide antibiotic that displays enhanced antimicrobial activity.A novel ketolide, RBx 14255, with activity against multidrug-resistant Streptococcus pneumoniae.Refinement of a low-resolution crystal structure to better understand erythromycin interactions on large ribosomal subunit.Unfolded protein exhibits antiassociation activity toward the 50S subunit facilitating 70S ribosome dissociation.
P2860
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P2860
Binding site of the bridged macrolides in the Escherichia coli ribosome.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Binding site of the bridged macrolides in the Escherichia coli ribosome.
@en
type
label
Binding site of the bridged macrolides in the Escherichia coli ribosome.
@en
prefLabel
Binding site of the bridged macrolides in the Escherichia coli ribosome.
@en
P2093
P2860
P1476
Binding site of the bridged macrolides in the Escherichia coli ribosome.
@en
P2093
Alexander S Mankin
Liqun Xiong
Yakov Korkhin
P2860
P304
P356
10.1128/AAC.49.1.281-288.2005
P407
P577
2005-01-01T00:00:00Z