selected publications
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article
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Structural consequences of metallothionein dimerization: Solution structure of the isolated Cd-4-alpha-domain and comparison with the holoprotein dimer..
Biochemistry.
42:8403-8410.
22,
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Exchange reactions between albumin-Au(I)-PEt3 complex and Me3PAuCl or iPr(3)PAuCl: P-31 NMR spectroscopic studies..
Inorganic Chemistry.
5:109-116.
2004
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Structure of the Cd-113(3)beta domains from Homarus americanus metallothionein-1: hydrogen bonding and solvent accessibility of sulfur atoms..
Journal of Biological Inorganic Chemistry.
7:713-724.
2002
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The requirements for stable metallothionein clusters examined using synthetic lobster domains..
Marine Environmental Research.
50:93-97.
2000
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Interprotein metal ion exchange between cadmium-carbonic anhydrase and apo- or zinc-metallothionein..
Journal of Biological Inorganic Chemistry.
4:784-790.
1999
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Kinetics of reversible N-ethylmaleimide alkylation of metallothionein and the subsequent metal release..
Journal of Biological Inorganic Chemistry.
2:65-73.
1997
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Stoichiometry and cluster specificity of copper binding to metallothionein - homogeneous metal clusters..
Biochemical Journal.
317:395-402.
15,
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Reaction of CD-111(7)-Metallothionein with EDTA-a Reappraisal..
Journal of Biological Chemistry.
27:5339-5345.
10,
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Characterization of the Cadmium Complex of Peptide 49-61. A putative Nucleation Center for Cadmium-Induced Folding in Rabbit Liver Metallothionein-IIA..
Journal of Biological Inorganic Chemistry.
4:495-507.
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Reactions of Electrophilic Reagents that Target the Thiolate Groups of Metallothionein Clusters: Preferential Reactions with the a-Domain..
Inorganic Chemistry.
38:5655-5659.
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Structure-Reactivity Relationships among Metallothionein Three-Metal Domains: Role of Non-Cystein Amino Acid Residues in Lobster Metallothionein and Human MT-3..
Inorganic Chemistry.
39:6115-6123.
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Structural consequences of metallothionein dimerization: Solution structure of the isolated Cd-4-alpha-domain and comparison with the holoprotein dimer..
Biochemistry.
42:8403-8410.
22,