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Literature DB >> 30794776

Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin.

Hui Xu, Tianbo Li, Alexis Rohou, Christopher P Arthur, Foteini Tzakoniati, Evera Wong, Alberto Estevez, Christine Kugel, Yvonne Franke, Jun Chen, Claudio Ciferri, David H Hackos, Christopher M Koth, Jian Payandeh.

Abstract

Entities: Gene

Year: 2019 PMID： 30794776 DOI： 10.1016/j.cell.2019.01.047

Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582

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15 in total

1. Comprehensive engineering of the tarantula venom peptide huwentoxin-IV to inhibit the human voltage-gated sodium channel hNa_v1.7.

Authors: Robert A Neff; Mack Flinspach; Alan Gibbs; Amy Y Shih; Natali A Minassian; Yi Liu; Ross Fellows; Ondrej Libiger; Stephanie Young; Michael W Pennington; Michael J Hunter; Alan D Wickenden
Journal: J Biol Chem Date: 2019-12-23 Impact factor: 5.157

2. Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated Na⁺ channels in nanodisc.

Authors: Shuai Gao; William C Valinsky; Nguyen Cam On; Patrick R Houlihan; Qian Qu; Lei Liu; Xiaojing Pan; David E Clapham; Nieng Yan
Journal: Proc Natl Acad Sci U S A Date: 2020-06-08 Impact factor: 11.205

Review 3. Structure-Function and Therapeutic Potential of Spider Venom-Derived Cysteine Knot Peptides Targeting Sodium Channels.

Authors: Fernanda C Cardoso; Richard J Lewis
Journal: Front Pharmacol Date: 2019-04-11 Impact factor: 5.810

4. The HCN channel voltage sensor undergoes a large downward motion during hyperpolarization.

Authors: Gucan Dai; Teresa K Aman; Frank DiMaio; William N Zagotta
Journal: Nat Struct Mol Biol Date: 2019-07-08 Impact factor: 15.369

5. Cell-Free Expression of Sodium Channel Domains for Pharmacology Studies. Noncanonical Spider Toxin Binding Site in the Second Voltage-Sensing Domain of Human Na_v1.4 Channel.

Authors: Mikhail Yu Myshkin; Roope Männikkö; Olesya A Krumkacheva; Dmitrii S Kulbatskii; Anton O Chugunov; Antonina A Berkut; Alexander S Paramonov; Mikhail A Shulepko; Matvey V Fedin; Michael G Hanna; Dimitri M Kullmann; Elena G Bagryanskaya; Alexander S Arseniev; Mikhail P Kirpichnikov; Ekaterina N Lyukmanova; Alexander A Vassilevski; Zakhar O Shenkarev
Journal: Front Pharmacol Date: 2019-09-04 Impact factor: 5.810

Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin.

1. Comprehensive engineering of the tarantula venom peptide huwentoxin-IV to inhibit the human voltage-gated sodium channel hNa_v1.7.

2. Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated Na⁺ channels in nanodisc.

Review 3. Structure-Function and Therapeutic Potential of Spider Venom-Derived Cysteine Knot Peptides Targeting Sodium Channels.

4. The HCN channel voltage sensor undergoes a large downward motion during hyperpolarization.

5. Cell-Free Expression of Sodium Channel Domains for Pharmacology Studies. Noncanonical Spider Toxin Binding Site in the Second Voltage-Sensing Domain of Human Na_v1.4 Channel.

6. Nanodisc technology facilitates identification of monoclonal antibodies targeting multi-pass membrane proteins.

7. Helix breaking transition in the S4 of HCN channel is critical for hyperpolarization-dependent gating.

8. Selective Targeting of Nav1.7 with Engineered Spider Venom-Based Peptides.

9. Cryo-EM structure of the KvAP channel reveals a non-domain-swapped voltage sensor topology.

Review 10. Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses.