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Q44539325-C3BC3C93-D18B-447A-A9E3-6956764CE08F
Q44539325-C3BC3C93-D18B-447A-A9E3-6956764CE08F
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http://www.wikidata.org/entity/statement/Q44539325-C3BC3C93-D18B-447A-A9E3-6956764CE08F
Structure of the HERG K+ channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation.
P2860
Q44539325-C3BC3C93-D18B-447A-A9E3-6956764CE08F
BestRank
Statement
http://www.wikidata.org/entity/statement/Q44539325-C3BC3C93-D18B-447A-A9E3-6956764CE08F
rank
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type
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wasDerivedFrom
27c74e6cc6403b7473a53a977e52570c7362e77d
P2860
Extracellular sodium interacts with the HERG channel at an outer pore site.