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The Rem, Rem2, Rad, and Gem/Kir (RGK) GTPases, comprise a subfamily of small Ras-related GTP-binding proteins, and have been shown to potently inhibit high voltage-activated Ca(2+) channel current following overexpression. Although the molecular mechanisms underlying RGK-mediated Ca(2+) channel regulation remains controversial, recent studies suggest that(More)
The second extracellular loop (LFWQYFVGKRTVPPGECFIQFLSEPTITFGTAI, aa 205-237) of muscarinic acetylcholine 3 receptor (M3R) has been reported to be an epitope for autoantibodies generated during certain autoimmune disorders, including Sjögren's syndrome (SS). Autoantibodies against M3R(228-237) have been shown to interfere with the function of M3R. However,(More)
In the centrosymmetric trinuclear cation of the title compound, [Co₃(C₄H(8)N₄)₆(H₂O)₆](C₁₀H₆O₆S₂)Cl₄, the three Co(II) atoms are bridged by six triazole mol-ecules via the N atoms in the 1,2-positions. The central Co(II) atom, lying on an inversion center, is coordinated by six triazole N atoms while the terminal Co(II) atoms are coordinated by three(More)
GTPases of the Ras-related RGK family are negative regulators of high voltage-activated (HVA) Ca2+ channel activity. In this study, we examined the role of calmodulin (CaM) association in Rem-mediated Ca2+ channel inhibition. We found that the Rem/CaM interaction is Ca2+-dependent, and that truncation of the Rem C-terminus before position 277 prevents CaM(More)
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