Interactions between Fragments of Trypsinized Na,K-ATPase Detected by Thermal Inactivation of Rb+ Occlusion and Dissociation of the M5/M6 Fragment
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
1. Effects of competitive sodium-like antagonists on Na,K-ATPase suggest that cation occlusion from the cytoplasmic surface occurs in two steps
2. Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent.
3. Structural organization, ion transport, and energy transduction of P-type ATPases
4. Location of high affinity Ca2 +-binding sites within the predicted transmembrahe domain of the sarco-plasmic reticulum Ca2+-ATPase
5. Na+,K(+)-ATPase.
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1. Unexpected Effects of K+ and Adenosine Triphosphate on the Thermal Stability of Na+,K+-ATPase;The Journal of Physical Chemistry B;2017-05-10
2. Opposing Effects of Na+ and K+ on the Thermal Stability of Na+,K+-ATPase;The Journal of Physical Chemistry B;2012-02-29
3. Modulation of protein kinase C by curcumin; inhibition and activation switched by calcium ions;British Journal of Pharmacology;2007-01
4. Structural Characterization of Na,K-ATPase from Shark Rectal Glands by Extensive Trypsinization;Biochemistry;2005-12-22
5. Stabilization of trypsin by association to plasma membranes: Implications for tryptic cleavage of membrane-bound Na,K-ATPase;Biochimica et Biophysica Acta (BBA) - Biomembranes;2005-12
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