Current Print IssueThe Journal of General Physiology RSS feed -- current issueAll quiet on the neuronal front: NMDA receptor inhibition by prion protein- May 26, 2008http://www.jgp.org/cgi/content/short/131/6/i3?rss=1 KCNQ1 and KCNE1 in the IKs Channel Complex Make State-dependent Contacts in their Extracellular Domains- May 26, 2008 KCNQ1 and KCNE1 (Q1 and E1) associate to form the slow delayed rectifier IKs channels in the heart. A short stretch of eight amino acids at the extracellular end of S1 in Q1 (positions 140–147) harbors six arrhythmia-associated mutations. Some of these mutations affect the Q1 channel function only when coexpressed with E1, suggesting that this Q1 region may engage in the interaction with E1 critical for the IKs channel function. Identifying the Q1E1 contact points here may provide new...http://www.jgp.org/cgi/content/short/131/6/589?rss=1 Voltage-gated Na Channel Selectivity: The Role of the Conserved Domain III Lysine Residue- May 26, 2008http://www.jgp.org/cgi/content/short/131/6/523?rss=1 A Continuum Method for Determining Membrane Protein Insertion Energies and the Problem of Charged Residues- May 26, 2008 Continuum electrostatic approaches have been extremely successful at describing the charged nature of soluble proteins and how they interact with binding partners. However, it is unclear whether continuum methods can be used to quantitatively understand the energetics of membrane protein insertion and stability. Recent translation experiments suggest that the energy required to insert charged peptides into membranes is much smaller than predicted by present continuum theories. Atomistic...http://www.jgp.org/cgi/content/short/131/6/563?rss=1 You Wrote It; You Own It!- May 26, 2008 Authors of papers published in Rockefeller University Press journals (The Journal of Cell Biology, The Journal of Experimental Medicine, or The Journal of General Physiology) now retain copyright to their published work. This permits authors to reuse their own work in any way, as long as they attribute it to the original publication. Third parties may use our published materials under a Creative Commons license, six months after publication.http://www.jgp.org/cgi/content/short/131/6/521?rss=1 Position and Role of the BK Channel alpha Subunit S0 Helix Inferred from Disulfide Crosslinking- May 26, 2008 The position and role of the unique N-terminal transmembrane (TM) helix, S0, in large-conductance, voltage- and calcium-activated potassium (BK) channels are undetermined. From the extents of intra-subunit, endogenous disulfide bond formation between cysteines substituted for the residues just outside the membrane domain, we infer that the extracellular flank of S0 is surrounded on three sides by the extracellular flanks of TM helices S1 and S2 and the four-residue extracellular loop between S3.http://www.jgp.org/cgi/content/short/131/6/537?rss=1 MEC-2 and MEC-6 in the Caenorhabditis elegans Sensory Mechanotransduction Complex: Auxiliary Subunits that Enable Channel Activity- May 26, 2008 The ion channel formed by the homologous proteins MEC-4 and MEC-10 forms the core of a sensory mechanotransduction channel in Caenorhabditis elegans. Although the products of other mec genes are key players in the biophysics of transduction, the mechanism by which they contribute to the properties of the channel is unknown. Here, we investigate the role of two auxiliary channel subunits, MEC-2 (stomatin-like) and MEC-6 (paraoxonase-like), by coexpressing them with constitutively active...http://www.jgp.org/cgi/content/short/131/6/605?rss=1 Prion protein attenuates excitotoxicity by inhibiting NMDA receptors- May 26, 2008http://www.jgp.org/cgi/content/short/131/6/i5?rss=1 |