The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels
Abstract: Tetrodotoxin (TTX) is a highly specific blocker of voltage-gated sodium channels. The dissociation constant of block varies with different channel isoforms. Until recently, channel resistance was thought to be primarily imparted by amino acid substitutions at a single position in domain I....
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2006-04-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/4/3/143/ |
| _version_ | 1818473874204917760 |
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| author | C. Ruben Shana L. Geffeney |
| author_facet | C. Ruben Shana L. Geffeney |
| author_sort | C. Ruben |
| collection | DOAJ |
| description | Abstract: Tetrodotoxin (TTX) is a highly specific blocker of voltage-gated sodium channels. The dissociation constant of block varies with different channel isoforms. Until recently, channel resistance was thought to be primarily imparted by amino acid substitutions at a single position in domain I. Recent work reveals a novel site for tetrodotoxin resistance in the P-region of domain IV. |
| first_indexed | 2024-04-14T04:29:37Z |
| format | Article |
| id | doaj.art-7c9bd2aa69e749e7a39021572f2d5bc2 |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-14T04:29:37Z |
| publishDate | 2006-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-7c9bd2aa69e749e7a39021572f2d5bc22022-12-22T02:12:08ZengMDPI AGMarine Drugs1660-33972006-04-014314315610.3390/md403143The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium ChannelsC. RubenShana L. GeffeneyAbstract: Tetrodotoxin (TTX) is a highly specific blocker of voltage-gated sodium channels. The dissociation constant of block varies with different channel isoforms. Until recently, channel resistance was thought to be primarily imparted by amino acid substitutions at a single position in domain I. Recent work reveals a novel site for tetrodotoxin resistance in the P-region of domain IV.http://www.mdpi.com/1660-3397/4/3/143/neurotoxinTTXNaVinward sodium currentvoltage clamp |
| spellingShingle | C. Ruben Shana L. Geffeney The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels Marine Drugs neurotoxin TTX NaV inward sodium current voltage clamp |
| title | The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels |
| title_full | The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels |
| title_fullStr | The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels |
| title_full_unstemmed | The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels |
| title_short | The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels |
| title_sort | structural basis and functional consequences of interactions between tetrodotoxin and voltage gated sodium channels |
| topic | neurotoxin TTX NaV inward sodium current voltage clamp |
| url | http://www.mdpi.com/1660-3397/4/3/143/ |
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