Papers associated with autopod (and atp1a1)

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	Role of homologous ASP334 and GLU319 in human non-gastric H,K- and Na,K-ATPases in cardiac glycoside binding., Radkov R., Biochem Biophys Res Commun. April 27, 2007; 356 (1): 142-6.
	FXYD6 is a novel regulator of Na,K-ATPase expressed in the inner ear., Delprat B., J Biol Chem. March 9, 2007; 282 (10): 7450-6.
	Structural and functional properties of two human FXYD3 (Mat-8) isoforms., Bibert S., J Biol Chem. December 22, 2006; 281 (51): 39142-51.
	FXYD7, mapping of functional sites involved in endoplasmic reticulum export, association with and regulation of Na,K-ATPase., Crambert G., J Biol Chem. July 16, 2004; 279 (29): 30888-95.
	Betam, a structural member of the X,K-ATPase beta subunit family, resides in the ER and does not associate with any known X,K-ATPase alpha subunit., Crambert G., Biochemistry. May 28, 2002; 41 (21): 6723-33.
	Structural and functional features of the transmembrane domain of the Na,K-ATPase beta subunit revealed by tryptophan scanning., Hasler U., J Biol Chem. May 11, 2001; 276 (19): 16356-64.
	Intersubunit interactions in human X,K-ATPases: role of membrane domains M9 and M10 in the assembly process and association efficiency of human, nongastric H,K-ATPase alpha subunits (ATP1al1) with known beta subunits., Geering K., Biochemistry. October 17, 2000; 39 (41): 12688-98.
	Transport and pharmacological properties of nine different human Na, K-ATPase isozymes., Crambert G., J Biol Chem. January 21, 2000; 275 (3): 1976-86.
	Regulation of expression and function by subunits of oligomeric P-type ATPases., Béguin P., Acta Physiol Scand Suppl. August 1, 1998; 643 283-7.
	The gamma subunit is a specific component of the Na,K-ATPase and modulates its transport function., Béguin P., EMBO J. July 16, 1997; 16 (14): 4250-60.
	Role of glycosylation and disulfide bond formation in the beta subunit in the folding and functional expression of Na,K-ATPase., Beggah AT., J Biol Chem. April 11, 1997; 272 (15): 10318-26.
	Functional consequences of substitution of the disulfide-bonded segment, Cys127-Cys150, located in the extracellular domain of the Na,K-ATPase beta subunit: Arg148 is essential for the functional expression of Na,K-ATPase., Ueno S., J Biochem. March 1, 1995; 117 (3): 591-6.
	Hydrophobic C-terminal amino acids in the beta-subunit are involved in assembly with the alpha-subunit of Na,K-ATPase., Beggah AT., Biochemistry. December 28, 1993; 32 (51): 14117-24.
	The functional role of the beta-subunit in the maturation and intracellular transport of Na,K-ATPase., Geering K., FEBS Lett. July 22, 1991; 285 (2): 189-93.
	Modulation of Na,K-ATPase expression during early development of Xenopus laevis., Han Y., Dev Biol. May 1, 1991; 145 (1): 174-81.

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