about
Crystal structure of nickel-containing superoxide dismutase reveals another type of active siteA complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR.Identification of altered function alleles that affect Bacillus subtilis PerR metal ion selectivity.Bacillus licheniformis Contains Two More PerR-Like Proteins in Addition to PerR, Fur, and Zur Orthologues.Zn(II)-Coordinated Quantum Dot-FRET Nanosensors for the Detection of Protein Kinase ActivityDirected evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor.Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro.Enhancement of the cancer targeting specificity of buforin IIb by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker.The protein complex composed of nickel-binding SrnQ and DNA binding motif-bearing SrnR of Streptomyces griseus represses sodF transcription in the presence of nickel.CbiX-homologous protein (CbiXhp), a metal-binding protein, from Streptomyces seoulensis is involved in expression of nickel-containing superoxide dismutase.Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR.The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidationBiochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR
P50
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P50
description
researcher ORCID ID = 0000-0002-1201-8254
@en
wetenschapper
@nl
name
Jin-Won Lee
@ast
Jin-Won Lee
@en
Jin-Won Lee
@es
Jin-Won Lee
@nl
type
label
Jin-Won Lee
@ast
Jin-Won Lee
@en
Jin-Won Lee
@es
Jin-Won Lee
@nl
prefLabel
Jin-Won Lee
@ast
Jin-Won Lee
@en
Jin-Won Lee
@es
Jin-Won Lee
@nl
P31
P496
0000-0002-1201-8254