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	1.	Aspartic acid 397 in subunit B of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae forms part of a sodium-binding site, is involved in cation selectivity, and affects cation-binding site cooperativity. [electronic resource] by Shea, Michael E Juárez, Oscar Cho, Jonathan Barquera, Blanca Producer: 20131231 In: The Journal of biological chemistry vol. 288 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	2.	The role and specificity of the catalytic and regulatory cation-binding sites of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae. [electronic resource] by Juárez, Oscar Shea, Michael E Makhatadze, George I Barquera, Blanca Producer: 20110928 In: The Journal of biological chemistry vol. 286 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	3.	A mutation in Na(+)-NQR uncouples electron flow from Na(+) translocation in the presence of K(+). [electronic resource] by Shea, Michael E Mezic, Katherine G Juárez, Oscar Barquera, Blanca Producer: 20150408 In: Biochemistry vol. 54 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	4.	Dehalococcoides mccartyi strain JNA dechlorinates multiple chlorinated phenols including pentachlorophenol and harbors at least 19 reductive dehalogenase homologous genes. [electronic resource] by Fricker, Ashwana D LaRoe, Sarah L Shea, Michael E Bedard, Donna L Producer: 20150710 In: Environmental science & technology vol. 48 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)