Immunoelectron microscopy of epitopes on Na,K-ATPase catalytic subunit. Implications for the transmembrane organization of the C-terminal domain.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
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2. Constraints on Models for the Folding of the Na,K-ATPase
3. Topology of Na+,K+-ATPase Identification of the extra- and intracellular hydrophilic loops of the catalytic subunit by specific antibodies
4. Na,K-ATPase extracellular surface probed with a monoclonal antibody that enhances ouabain binding.
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1. Cardiac Sarcoplasmic Reticulum Ca 2+ ‐ ATPase;Comprehensive Physiology;2002-12
2. The thermal unfolding and domain structure of Na+/K+-exchanging ATPase.;European Journal of Biochemistry;2001-10-01
3. Site-directed Chemical Labeling of Extracellular Loops in a Membrane Protein;Journal of Biological Chemistry;2000-06
4. Alanine Scanning Mutagenesis of Oxygen-Containing Amino Acids in the Transmembrane Region of the Na,K-ATPase;Archives of Biochemistry and Biophysics;1999-07
5. Functional Role of Oxygen-Containing Residues in the Fifth Transmembrane Segment of the Na,K-ATPase α Subunit;Archives of Biochemistry and Biophysics;1999-04
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