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Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance
The structure–function relationship of the nicotinic acetylcholine receptor (AChR) has been effectively studied by the combination of complementary DNA manipulation and single-channel currentExpand
Localization in the II-III Loop of the Dihydropyridine Receptor of a Sequence Critical for Excitation-Contraction Coupling*
Skeletal and cardiac muscles express distinct isoforms of the dihydropyridine receptor (DHPR), a type of voltage-gated Ca2+ channel that is important for excitation-contraction (EC) coupling.Expand
Sphingosine 1-Phosphate (S1P) Regulates Vascular Contraction via S1P3 Receptor: Investigation Based on a New S1P3 Receptor Antagonist
Sphingosine 1-phosphate (S1P) induces diverse biological responses in various tissues by activating specific G protein-coupled receptors (S1P1–S1P5 receptors). The biological signaling regulated byExpand
A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptor
The channel pore of the nicotinic acetylcholine receptor (AChR) has been investigated by analysing single‐channel conductances of systematically mutatedTorpedo receptors expressed in Xenopus oocytes.Expand
Rings of anionic amino acids as structural determinants of ion selectivity in the acetylcholine receptor channel
To gain an insight into the molecular basis of the weak but significant selectivity among alkali metal cations of the nicotinic acetylcholine receptor (AChR) channel, we have determinedExpand
Location of a δ-subunit region determining ion transport through the acetylcholine receptor channel
The combination of complementary DNA expression and single-channel current analysis provides a powerful tool for studying the structure–function relationship of the nicotinic acetylcholine receptorExpand
A circular dichroism study of preferential hydration and alcohol effects on a denatured protein, pig calpastatin domain I.
Pig calpastatin domain I (CSD1), a proteinase inhibitor that specifically blocks activity of calpain I and II, is a good candidate protein for studying conformational variations in the denatured formExpand
The compact and expanded denatured conformations of apomyoglobin in the methanol‐water solvent
We have performed a detailed study of methanol‐induced conformational transitions of horse heart apomyoglobin (apoMb) to investigate the existence of the compact and expanded denatured states. AExpand
Novel interaction of the voltage-dependent sodium channel (VDSC) with calmodulin: does VDSC acquire calmodulin-mediated Ca2+-sensitivity?
The voltage-dependent sodium channel (VDSC) interacts with intracellular molecules to modulate channel properties and localizations in neuronal cells. To study protein interactions, we applied yeastExpand
Amyloid‐like aggregates of a plant protein: a case of a sweet‐tasting protein, monellin
We report here a novel case of amyloid‐like aggregation of a plant protein. A sweet‐tasting protein, monellin, experiences an irreversible heat denaturation at pH 2.5 and 85°C. Addition of 100 mMExpand