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5 Glutamate Dehydrogenases
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The Tarantula Toxins ProTx-II and Huwentoxin-IV Differentially Interact with Human Nav1.7 Voltage Sensors to Inhibit Channel Activation and Inactivation
TLDR
Whereas ProTx-II and HW TX-IV binding determinants on domain-II may overlap, domain II plays a much more crucial role for HWTX-IV, and contrary to what has been proposed to be a guiding principle of sodium channel pharmacology, molecules do not have to exclusively target the domain IV voltage-sensor to influence sodium channel inactivation.
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Molecular interactions of the gating modifier toxin ProTx-II with NaV 1.5: implied existence of a novel toxin binding site coupled to activation.
TLDR
The data establish that, contrary to prior assumptions, ProTx-II does not bind to the previously characterized neurotoxin site 4, thus making it a novel probe of activation gating in Na(v) channels with potential to shed new light on this process.
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AnkB, a Periplasmic Ankyrin-Like Protein inPseudomonas aeruginosa, Is Required for Optimal Catalase B (KatB) Activity and Resistance to Hydrogen Peroxide
TLDR
The cloned ankB gene, encoding an ankyrin-like protein in Pseudomonas aeruginosa, is cloned and it is suggested that AnkB may form an antioxidant scaffolding with KatB in the periplasm at the cytoplasmic membrane, thus providing a protective lattice work for optimal H( 2)O(2) detoxification.
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ProTx-I and ProTx-II: gating modifiers of voltage-gated sodium channels.
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A Specific Interaction between the Cardiac Sodium Channel and Site-3 Toxin Anthopleurin B*
The polypeptide neurotoxin anthopleurin B (ApB) isolated from the venom of the sea anemone Anthopleura xanthogrammica is one of a family of toxins that bind to the extracellular face of…
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Site-3 sea anemone toxins: molecular probes of gating mechanisms in voltage-dependent sodium channels.
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Inhibition of the activation pathway of the T-type calcium channel Ca(V)3.1 by ProTxII.
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High Affinity Dimerization by Ski Involves Parallel Pairing of a Novel Bipartite α-Helical Domain*
c-Ski protein possesses a C-terminal dimerization domain that was deleted during the generation of v-ski, and has been implicated in the increased potency of c-ski in cellular transformation compared…
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Differential Phospholipid Binding by Site 3 and Site 4 Toxins
TLDR
It is concluded that toxins that modify inactivation kinetics via binding to NaV1.x site 3 lack the ability to bind phospholipids, whereas site 4 toxins, which modify activation, have this activity.
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