Role of polyamine structure in inhibition of K + ‐Cl − cotransport in human red cell ghosts
Author:
Affiliation:
1. Department of Medicine, State University of New York, Stony Brook, NY 11794‐8151, USA
Publisher
Wiley
Subject
Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1469-7793.1999.00723.x
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1. Quinine and quinidine inhibit and reveal heterogeneity of K-Cl cotransport in low K sheep erythrocytes
2. Calorimetric studies of the structural transitions of the human erythrocyte membrane. The involvement of spectrin in the A transition
3. Cytosolic protein concentration is the primary volume signal in dog red cells.
4. A new model to describe extrinsic protein binding to phospholipid membranes of varying composition: application to human coagulation proteins
5. Deficiency of Src family kinases Fgr and Hck results in activation of erythrocyte K/Cl cotransport.
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1. K+-Cl− cotransporter 1 (KCC1): a housekeeping membrane protein that plays key supplemental roles in hematopoietic and cancer cells;Journal of Hematology & Oncology;2019-07-11
2. Impedance spectroscopy of human erythrocyte membrane: Effect of frequency at the spectrin denaturation transition temperature;Bioelectrochemistry;2010-06
3. Polyamine effects on cell function: Possible central role of plasma membrane PI(4,5)P2;Journal of Cellular Physiology;2009-09-10
4. Regulation of K-Cl Cotransport: from Function to Genes;Journal of Membrane Biology;2004-11
5. K+-Cl- Cotransport in Vertebrate Red Cells;Red Cell Membrane Transport in Health and Disease;2003
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