Zamble, Déborah
Deborah B. Zamble Canadian chemist
VIAF ID: 3150565680106252292 (Personal)
Permalink: http://viaf.org/viaf/3150565680106252292
Preferred Forms
- 100 0 _ ‡a Deborah B. Zamble ‡c Canadian chemist
- 100 1 _ ‡a Zamble, Deborah
-
- 100 1 _ ‡a Zamble, Deborah
-
- 100 1 _ ‡a Zamble, Déborah
4xx's: Alternate Name Forms (7)
Works
Title | Sources |
---|---|
The antibiotic microcin B17 is a DNA gyrase poison: characterisation of the mode of inhibition | |
The biological chemistry of nickel, 2017: | |
Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel | |
The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3. | |
Fluorescence analysis of sulfonamide binding to carbonic anhydrase | |
A high-performance liquid chromatography method for determining transition metal content in proteins | |
A High Throughput Method for the Detection of Metalloproteins on a Microgram Scale | |
HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease | |
Human testis-determining factor SRY binds to the major DNA adduct of cisplatin and a putative target sequence with comparable affinities. | |
It costs more than a nickel | |
The McbB component of microcin B17 synthetase is a zinc metalloprotein. | |
The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB. | |
The "metallo-specific" response of proteins: a perspective based on the Escherichia coli transcriptional regulator NikR. | |
Microbial nickel: cellular uptake and delivery to enzyme centers. | |
The Ni(II)-binding properties of the metallochaperone SlyD. | |
[NiFe]-Hydrogenase Maturation. | |
NikR-operator complex structure and the mechanism of repressor activation by metal ions | |
Ordered binding of retinoic acid and retinoid-X receptors to asymmetric response elements involves determinants adjacent to the DNA-binding domain. | |
pH-responsive DNA-binding activity of Helicobacter pylori NikR. | |
Potassium is critical for the Ni | |
Protease digestion analysis of Escherichia coli NikR: evidence for conformational stabilization with Ni(II). | |
A ratiometric NMR pH sensing strategy based on a slow-proton-exchange (SPE) mechanism | |
Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB. | |
The response of Escherichia coli NikR to nickel: a second nickel-binding site. | |
The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD. | |
Structural and Biological Analysis of the Metal Sites ofEscherichia coliHydrogenase Accessory Protein HypB† | |
Structural basis of the metal specificity for nickel regulatory protein NikR | |
A whole-cell, high-throughput hydrogenase assay to identify factors that modulate [NiFe]-hydrogenase activity | |
YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasis |