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Signaling path of the action of AVP on distal K+ secretion
(Blackwell Publishing, 2004-08-01)
Background. Previous studies from our laboratory have shown that luminal perfusion with arginine vasopressin (AVP) stimulates distal tubule secretory potassium flux (J(K)) via V1 receptors (Am J Physiol 278: F809- F816, ...
Modulation of the MaxiK Potassium Channel by the Coexpression of its β1 and β2 subunitsMODULACIÓN DEL CANAL DE POTASIO MAXIK POR LA COEXPRESIÓN DE SUS SUBUNIDADES β1 Y β2Modulatión of the maxik potassium channel by the coexpressión of its β1 and β2 subunitsmodulación del canal de potasió maxik por la coexpresión de sus subunidades β1 y β2
(2004)
The high conductance, calcium-activated potassium (MaxiK) channel is widely expressed among mammalian tissues. The activity of the channel is increased by membrane depolarization and by increases in intracellular calcium ...
Maxi-K channels contribute to urinary potassium excretion in the ROMK-deficient mouse model of Type II Bartter's syndrome and in adaptation to a high-K diet
(2006-07-12)
Type II Bartter's syndrome is a hereditary hypokalemic renal salt-wasting disorder caused by mutations in the ROMK channel (Kir1.1; Kcnj1), mediating potassium recycling in the thick ascending limb of Henle's loop (TAL) ...
Maxi-K channels contribute to urinary potassium excretion in the ROMK-deficient mouse model of Type II Bartter's syndrome and in adaptation to a high-K diet
(2006-07-12)
Type II Bartter's syndrome is a hereditary hypokalemic renal salt-wasting disorder caused by mutations in the ROMK channel (Kir1.1; Kcnj1), mediating potassium recycling in the thick ascending limb of Henle's loop (TAL) ...
Effect of uroguanylin on potassium and bicarbonate transport in rat renal tubules
(Natl Research Council Canada-n R C Research Press, 2014)
Signaling path of the action of AVP on distal K+ secretion
(Blackwell Publishing, 2014)
Structural Determinants in the Interaction of Shaker Inactivating Peptide and a Ca2+-Activated K+ Channel
(1994)
Shaker B inactivating peptide (BP) binds to its receptor in maxi Kca channels obstructing the flow of ions through them. The interaction between Kca channels and BP mutants, with different net charge and hydrophobicity, ...