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Structural Basis for High-Affinity Trapping of the NaV1.7 Channel in Its Resting State by Tarantula Toxin

Molecular Cell(2020)10.1016/j.molcel.2020.10.039Source: DataRank Database

Structural Basis for High-Affinity Trapping of the NaV1.7 Channel in Its Resting State by Tarantula Toxin is a research paper published in Molecular Cell (2020). On theSindex it has a DataRank of 0. It has been cited 79 times.

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Open Access79 citations

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Enrichment:Funding (6 grants)OA: bronzeTopics (18)IDs (PubMed, PMC)Annotations (2)

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Findable (1/2)

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Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (6)

Lige Tonggu ORCID,Tamer M. Gamal El-Din ORCID,E. McCord,Ning Zheng ORCID,William A. Catterall ORCID

Live enrichment

PubMed:33232657 PMC:PMC8043720

NHLBI NIH HHS

Grant: R01 HL112808

NINDS NIH HHS

Grant: R35 NS111573

NIGMS NIH HHS

Grant: T32 GM007750

NINDS NIH HHS

Grant: R01 NS015751

National Institutes of Health

Howard Hughes Medical Institute

bronzeLicense: http://www.elsevier.com/open-access/userlicense/1.0/

publisherhttp://www.cell.com/article/S1097276520307735/pdf

publisherhttps://api.elsevier.com/content/article/PII:S1097276520307735?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S1097276520307735?httpAccept=text/plain

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/8043720

MeSH Terms

AnimalsHumansSpodopteraSpider VenomsAmino Acid SubstitutionMutation, MissenseNAV1.7 Voltage-Gated Sodium ChannelSf9 Cells

Keywords

AnalgesicsElectrophysiologyPainprotein structurevoltage-gated sodium channelNav1.7Cryo-emTarantulaHuwentoxinGating-modifier Toxins

Structural Basis for High-Affinity Trapping of the NaV1.7 Channel in Its Resting State by Tarantula Toxin

FAIR Checklist

Authors (6)

Funding (6 grants)

Open Access

Topics

Annotations (Europe PMC)