scholarly article | Q13442814 |
P2093 | author name string | Richard N Armstrong | |
Terry P Lybrand | |||
Daniel W Brown | |||
Eric Dawson | |||
Rachel E Rigsby | |||
P2860 | cites work | Phosphonoformate: a minimal transition state analogue inhibitor of the fosfomycin resistance protein, FosA. | Q45123405 |
Functional analysis of active site residues of the fosfomycin resistance enzyme FosA from Pseudomonas aeruginosa | Q45291346 | ||
Enzyme control of small-molecule coordination in FosA as revealed by 31P pulsed ENDOR and ESE-EPR. | Q46532476 | ||
Elucidation of a monovalent cation dependence and characterization of the divalent cation binding site of the fosfomycin resistance protein (FosA). | Q54093237 | ||
Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin. | Q54590227 | ||
Characterization of spontaneous fosfomycin (phosphonomycin)-resistant cells of Escherichia coli B in vitro | Q54621230 | ||
Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase | Q68060212 | ||
Phosphonomycin, a New Antibiotic Produced by Strains of Streptomyces | Q72475705 | ||
Phosphonomycin: structure and synthesis | Q72531472 | ||
Where will new antibiotics come from? | Q79817299 | ||
Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+) | Q27639636 | ||
Predicting the evolution of antibiotic resistance genes | Q28257796 | ||
Backbone-dependent rotamer library for proteins. Application to side-chain prediction | Q28267713 | ||
FosB, a cysteine-dependent fosfomycin resistance protein under the control of sigma(W), an extracytoplasmic-function sigma factor in Bacillus subtilis | Q28359895 | ||
Antibacterial resistance worldwide: causes, challenges and responses | Q29620008 | ||
Isolation and characterization of mutations affecting the transport of hexose phosphates in Escherichia coli | Q30451453 | ||
The mechanism of action of fosfomycin (phosphonomycin) | Q34214482 | ||
Structure, catalytic mechanism, and evolution of the glutathione transferases | Q34419894 | ||
Fosfomycin resistance proteins: a nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily | Q34482492 | ||
Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases | Q36855782 | ||
Plasmid-encoded fosfomycin resistance | Q37187074 | ||
Formation of an adduct between fosfomycin and glutathione: a new mechanism of antibiotic resistance in bacteria | Q39832506 | ||
Tn292l, a transposon encoding fosfomycin resistance | Q39984364 | ||
EPR study of substrate binding to the Mn(II) active site of the bacterial antibiotic resistance enzyme FosA: a better way to examine Mn(II). | Q43905726 | ||
P433 | issue | 2 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biophysics | Q7100 |
P304 | page(s) | 277-83 | |
P577 | publication date | 2007-08-15 | |
P1433 | published in | Archives of Biochemistry and Biophysics | Q635818 |
P1476 | title | A model for glutathione binding and activation in the fosfomycin resistance protein, FosA | |
P478 | volume | 464 |
Q99579591 | Characterization of the genomically encoded fosfomycin resistance enzyme from Mycobacterium abscessus |
Q34200026 | Chemical and Chemoenzymatic syntheses of bacillithiol: a unique low-molecular-weight thiol amongst low G + C Gram-positive bacteria. |
Q41909814 | Evolution of the antibiotic resistance protein, FosA, is linked to a catalytically promiscuous progenitor |
Q33369396 | Expression of Xhdsi-1VOC, a novel member of the vicinal oxygen chelate (VOC) metalloenzyme superfamily, is up-regulated in leaves and roots during desiccation in the resurrection plant Xerophyta humilis (Bak) Dur and Schinz |
Q34882983 | Glutathione transferases in bacteria. |
Q27679869 | Structural and Chemical Aspects of Resistance to the Antibiotic Fosfomycin Conferred by FosB from Bacillus cereus |
Search more.