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Flexibility of KorA, a plasmid-encoded, global transcription regulator, in the presence and the absence of its operator.The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1Synthesis of α-Glucan in Mycobacteria Involves a Hetero-octameric Complex of Trehalose Synthase TreS and Maltokinase Pep2Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspinTrp repressor-operator binding: NMR and electrophoretic mobility shift studies of the effect of DNA sequence and corepressor binding on two Trp repressor-operator complexes.Order and disorder in the domain organization of the plasmid partition protein KorB.Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences.Nitroreductase: a prodrug-activating enzyme for cancer gene therapy.A single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its co-regulator KorB.Repression of the Escherichia coli melR promoter by MelR: evidence that efficient repression requires the formation of a repression loop.Binding of the Escherichia coli MelR protein to the melAB promoter: orientation of MelR subunits and investigation of MelR-DNA contacts.DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coliTesting double mutants of the enzyme nitroreductase for enhanced cell sensitisation to prodrugs: effects of combining beneficial single mutations.Transcription activation at the Escherichia coli melAB promoter: interactions of MelR with its DNA target site and with domain 4 of the RNA polymerase sigma subunit.Transcription activation at the Escherichia coli melAB promoter: interactions of MelR with the C-terminal domain of the RNA polymerase alpha subunit.Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme.Steady-state and stopped-flow kinetic studies of three Escherichia coli NfsB mutants with enhanced activity for the prodrug CB1954.NMR studies of the Escherichia coli trp aporepressor. Sequence-specific assignment of the aromatic proton resonances.NMR studies of ion binding to Escherichia coli tRNAPhe.Assignment of the low-field 1H NMR spectrum of Escherichia coli tRNAPhe using nuclear Overhauser effects.H, C and N NMR assignments of self-incompatibility protein homologue 15 from Arabidopsis thalianaProton, carbon-13, and phosphorus-31 nuclear magnetic resonance studies of the dihydrofolate reductase-NADP-folate complex: characterization of three coexisting conformational statesRationalisation of a mechanism for sensing single point variants in target DNA using anthracene-tagged base discriminating probes1H, 13C and 15N assignments of the KorA global transcriptional repressor protein from the low copy number IncP-1 plasmid, RK2Secondary Structure of the C-Terminal DNA-Binding Domain of the Transcriptional Activator NifA fromKlebsiella pneumoniae:Spectroscopic Analyses1H-NMR Assignments and Secondary Structure of Dendroaspin, an RGD-Containing Glycoprotein IIb-IIIa (alphaIIb-beta3) Antagonist with a Neurotoxin Fold1H-NMR studies and secondary structure of the RGD-containing snake toxin, albolabrin
P50
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P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Eva I. Hyde
@ast
Eva I. Hyde
@en
Eva I. Hyde
@es
Eva I. Hyde
@nl
Eva I. Hyde
@sl
type
label
Eva I. Hyde
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Eva I. Hyde
@en
Eva I. Hyde
@es
Eva I. Hyde
@nl
Eva I. Hyde
@sl
prefLabel
Eva I. Hyde
@ast
Eva I. Hyde
@en
Eva I. Hyde
@es
Eva I. Hyde
@nl
Eva I. Hyde
@sl
P106
P1153
56210293000
P21
P31
P496
0000-0003-3440-2799