about
Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosisImplications of binding mode and active site flexibility for inhibitor potency against the salicylate synthase from Mycobacterium tuberculosisThe substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibitionRepurposing the chemical scaffold of the anti-arthritic drug Lobenzarit to target tryptophan biosynthesis in Mycobacterium tuberculosisAlternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosisA covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocketStructures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active SiteStructure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complexInhibiting dihydrodipicolinate synthase across species: towards specificity for pathogens?Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate bindingA tetrameric structure is not essential for activity in dihydrodipicolinate synthase (DHDPS) from Mycobacterium tuberculosis.Anthranilate phosphoribosyltransferase: Binding determinants for 5'-phospho-alpha-d-ribosyl-1'-pyrophosphate (PRPP) and the implications for inhibitor design.Purification, crystallization and preliminary X-ray studies of MbtN (Rv1346) from Mycobacterium tuberculosis.Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups.Thermodynamics of the fragile X mental retardation protein RGG box interactions with G quartet forming RNA.Corrigendum: Repurposing the Chemical Scaffold of the Anti-Arthritic Drug Lobenzarit to Target Tryptophan Biosynthesis inMycobacterium tuberculosisA lipid site shapes the agonist response of a pentameric ligand-gated ion channelModulation of the Erwinia ligand-gated ion channel (ELIC) and the 5-HT3 receptor via a common vestibule site
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description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Genevieve L. Evans
@ast
Genevieve L. Evans
@en
Genevieve L. Evans
@es
Genevieve L. Evans
@nl
Genevieve L. Evans
@sl
type
label
Genevieve L. Evans
@ast
Genevieve L. Evans
@en
Genevieve L. Evans
@es
Genevieve L. Evans
@nl
Genevieve L. Evans
@sl
prefLabel
Genevieve L. Evans
@ast
Genevieve L. Evans
@en
Genevieve L. Evans
@es
Genevieve L. Evans
@nl
Genevieve L. Evans
@sl
P1053
I-7431-2015
P106
P1153
35083360400
P21
P31
P3829
P496
0000-0002-8612-9539