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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.
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.
Beta 1- and beta 3-subunits can associate with presynthesized alpha-subunits of Xenopus oocyte Na, K-ATPase. , Ackermann U., J Biol Chem. June 25, 1992; 267 (18): 12911-5.
Processing, intracellular transport, and functional expression of endogenous and exogenous alpha-beta 3 Na, K-ATPase complexes in Xenopus oocytes. , Jaunin P., J Biol Chem. January 5, 1992; 267 (1): 577-85.
Trimer formation determines the rate of influenza virus haemagglutinin transport in the early stages of secretion in Xenopus oocytes. , Ceriotti A., J Cell Biol. August 1, 1990; 111 (2): 409-20.
A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro. , Wilson KL ., J Cell Biol. July 1, 1988; 107 (1): 57-68.
Membrane insertion of alpha- and beta-subunits of Na+,K+-ATPase. , Geering K., J Biol Chem. April 25, 1985; 260 (8): 5154-60.