Current Print IssueThe Journal of General Physiology RSS feed -- current issueAtomic Constraints between the Voltage Sensor and the Pore Domain in a Voltage-gated K+ Channel of Known Structure- May 26, 2008 In voltage-gated K+ channels (Kv), membrane depolarization promotes a structural reorganization of each of the four voltage sensor domains surrounding the conducting pore, inducing its opening. Although the crystal structure of Kv1.2 provided the first atomic resolution view of a eukaryotic Kv channel, several components of the voltage sensors remain poorly resolved. In particular, the position and orientation of the charged arginine side chains in the S4 transmembrane segments remain...http://www.jgp.org/cgi/content/short/131/6/549?rss=1 Presynaptic type III neuregulin1-ErbB signaling targets alpha7 nicotinic acetylcholine receptors to axons- May 26, 2008http://www.jgp.org/cgi/content/short/131/6/i4?rss=1 NGF Inhibits MKCNQ Currents and Selectively Alters Neuronal Excitability in Subsets of Sympathetic Neurons Depending on their MKCNQ Current Background- May 26, 2008 MKCNQ currents play a critical role in the determination of neuronal excitability. Many neurotransmitters and peptides modulate MKCNQ current and neuronal excitability through their G protein–coupled receptors. Nerve growth factor (NGF) activates its receptor, a member of receptor tyrosine kinase (RTK) superfamily, and crucially modulates neuronal cell survival, proliferation, and differentiation. In this study, we studied the effect of NGF on the neuronal (rat superior cervical ganglion,.http://www.jgp.org/cgi/content/short/131/6/575?rss=1 Surface Expression of Epithelial Na Channel Protein in Rat Kidney- May 26, 2008 Expression of epithelial Na channel (ENaC) protein in the apical membrane of rat kidney tubules was assessed by biotinylation of the extracellular surfaces of renal cells and by membrane fractionation. Rat kidneys were perfused in situ with solutions containing NHS-biotin, a cell-impermeant biotin derivative that attaches covalently to free amino groups on lysines. Membranes were solubilized and labeled proteins were isolated using neutravidin beads, and surface β and ENaC subunits were...http://www.jgp.org/cgi/content/short/131/6/617?rss=1 |