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Sarah R. Clippinger, Paige E. Cloonan, Wei Wang, Lina Greenberg, W. Tom Stump, Paweorn Angsutararux, Jeanne M. Nerbonne, Michael J. Greenberg
Clippinger et al. examine a mutation in troponin T that causes hypertrophic cardiomyopathy and demonstrate that increased molecular mechanics drive the early disease pathogenesis, leading to secondary activation of mechanobiological signaling pathways.
Zhuyuan Chen, Georg Kuenze, Jens Meiler, Cecilia M. Canessa
Acid-sensing ion channels (ASIC) play central roles in the central and peripheral nervous systems. In this paper, Chen et al. show that changes to a single arginine of a human ASIC both affect the efficacy of proton-mediated gating and delay the desensitization of the channel.
Farbod Fazlollahi, Jorge J. Santini Gonzalez, Steven J. Repas, Benjamin D. Canan, George E. Billman, Paul M.L. Janssen
Fazlollahi et al. show that contraction and relaxation remain tightly coupled in intact canine myocardium after exercise training and/or myocardial infarction. They postulate that the action of cardiac myosin binding protein C on actin and myosin may play a key role in this process.
Mohammad-Reza Ghovanloo, Koushik Choudhury, Tagore S. Bandaru, Mohamed A. Fouda, Kaveh Rayani, Radda Rusinova, Tejas Phaterpekar, Karen Nelkenbrecher, Abeline R. Watkins, Damon Poburko, Jenifer Thewalt, Olaf S. Andersen, Lucie Delemotte, Samuel J. Goodchild, Peter C. Ruben
Ghovanloo et al. combined in silico and in vitro approaches to determine the mechanism by which CBD inhibits the skeletal muscle Na+ channel Nav1.4. Their findings suggest that CBD acts directly, by binding inside the Nav1.4 pore, as well as indirectly, by modulating membrane elasticity.
Chiara Stronczek, Stephan Lange, Belinda Bullard, Sebastian Wolniak, Emma Börgeson, Olga Mayans, Jennifer R. Fleming
Stronczek et al. analyze the structure of the titin-N2A poly-Ig segment, a key signaling element in the sarcomere. They reveal a unique topography for the I81-I83 tandem, but they could not confirm the presence of Ca2+ binding sites in I81-I83 or the interaction of N2A with actin.
Leticia G. Marmolejo-Murillo, Iván A. Aréchiga-Figueroa, Eloy G. Moreno-Galindo, Tania Ferrer, Rodrigo Zamora-Cárdenas, Ricardo A. Navarro-Polanco, José A. Sánchez-Chapula, Aldo A. Rodríguez-Menchaca
Inward rectification of Kir channels is attributed to a voltage-dependent block of the channel pore by intracellular cations. Marmolejo-Murillo et al. identify a new intrinsic gating mechanism powered by the K+-flux in Kir4.1/Kir5.1 channels, which induces voltage-dependent inward rectification.
Marcos Matamoros, Colin G. Nichols
Matamoros and Nichols show that mutations in a transmembrane domain outside of the selectivity filter of the KirBac1.1 K+ channel affect ion transport, suggesting that channel selectivity is determined by the physical interaction between different domains.

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