Four Hydrophobic Segments in the NH2-terminal Third (H1-H4) of Na,K-ATPase α Subunit Alternately Initiate and Halt Membrane Translocation of the Newly Synthesized Polypeptide
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. [8] Immunoprecipitation of proteins from cell-free translations
2. Na,K-ATPase extracellular surface probed with a monoclonal antibody that enhances ouabain binding.
3. Immunochemical studies of (Na+ + K+)-ATPase using site-specific, synthetic peptide directed antibodies
4. Soluble and enzymatically stable (Na++K+)-ATPase from mammalian kidney consisting predominantly of protomer αβ-units
5. Extensive digestion of Na+,K(+)-ATPase by specific and nonspecific proteases with preservation of cation occlusion sites.
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1. Regulation of Membrane Na+-K+ ATPase in Health and Disease;Regulation of Membrane Na+-K+ ATPase;2015-12-16
2. Amino Acids in the TM4-TM5 Loop of Na,K-ATPase Are Important for Biosynthesis;Annals of the New York Academy of Sciences;2003-04
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4. The functional role of beta subunits in oligomeric P-type ATPases;Journal of Bioenergetics and Biomembranes;2001
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