Article Abstract:
ATP-sensitive potassium (K(sub ATP)) channel activity provides a link between cellular energetics and electrical excitability. Crystallographic and electrophysiological studies lead to detailed structural and kinetic models that define the molecular basis of channel activity, and the uncovering of disease-causing mutations of K(sub ATP) explains the molecular basis of disease and leads to a better understanding of the structural basis of channel function.
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Article Abstract:
A yeast protein of relative molecular mass Mr =13,000, named sulphiredoxin, which is conserved in higher eukaryotes is identified. It is proposed that sulphiredoxin reduces cysteine-sulphinic acids by activating phosphorylation followed by a thiol-mediated reduction step.
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Article Abstract:
The crystal structure of the human sulphiredoxin-peroxiredoxin (Srx-PrxI) complex is discussed. The complex is found to exhibit a complex repair embrace while allowing other proteins to bind to peroxiredoxins (Prxs).
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