Structure—Reactivity Relationships of Metallothionein, a Unique Metal-Binding Protein
Author:
Publisher
Informa UK Limited
Subject
Inorganic Chemistry
Link
http://www.tandfonline.com/doi/pdf/10.1080/02603598908035801
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1. A CADMIUM PROTEIN FROM EQUINE KIDNEY CORTEX
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1. Differentiated Zn(II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn;Metallomics;2023-10
2. The connection of α- and β-domains in mammalian metallothionein-2 differentiates Zn(II) binding affinities, affects folding, and determines zinc buffering properties;Metallomics;2023-05-05
3. From methodological limitations to the function of metallothioneins - a guide to approaches for determining weak, moderate, and tight affinity zinc sites;Metallomics;2023-04-27
4. The Bioinorganic Chemistry of Mammalian Metallothioneins;Chemical Reviews;2021-10-15
5. An Integrated Mass Spectrometry and Molecular Dynamics Simulations Approach Reveals the Spatial Organization Impact of Metal-Binding Sites on the Stability of Metal-Depleted Metallothionein-2 Species;Journal of the American Chemical Society;2021-09-03
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