Inactivation of the Na,K-ATPase by modification of Lys-501 with 4-acetamido-4′-isothiocyanatostilbene-2,2′-disulfonic acid (SITS)
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)81470-7/fullpdf
Reference18 articles.
1. Effects of the stilbene derivatives SITS and DIDS on intestinal ATPase activities
2. The effect of anion channel blockers on enzymatic activity of Na+ /K+ -ATPase and the electrogenic Na+ /K+ pump
3. Inhibition and derivatization of the renal sodium-potassium-ATPase by dihydro-4,4'-diisothiocyanatostilbene-2,2'-disulfonate
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1. DIDS inhibits Na-K-ATPase activity in porcine nonpigmented ciliary epithelial cells by a Src family kinase-dependent mechanism;American Journal of Physiology-Cell Physiology;2013-09-01
2. Fluorone dyes have binding sites on both cytoplasmic and extracellular domains of Na,K-ATPase;Biochimica et Biophysica Acta (BBA) - Biomembranes;2013-02
3. Biochemistry of Na,K-ATPase;Annual Review of Biochemistry;2002-06
4. Cys577 Is a Conformationally Mobile Residue in the ATP-binding Domain of the Na,K-ATPase α-Subunit;Journal of Biological Chemistry;1999-08
5. Ligand-Induced Conformational Changes in the Na,K-ATPase ? Subunit;Annals of the New York Academy of Sciences;1997-11
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