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:

Xie Yiheng,Morimoto Takashi

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 14 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

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

3. Role of Phylogenetically Conserved Amino Acids in Folding of Na,K-ATPase;Biochemistry;2001-05-25

4. The functional role of beta subunits in oligomeric P-type ATPases;Journal of Bioenergetics and Biomembranes;2001

5. Sodium pumps in the Malpighian tubule of Rhodnius sp.;Anais da Academia Brasileira de Ciências;2000-09

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