Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Single point mutations of the sodium channel drastically reduce the pore permeability without preventing its gating.

European biophysics journal : EBJ - 1 Jan 1991

Pusch M, Noda M, Stühmer W, Numa S, Conti F

Abstract excerpt

1. Two mutants of the sodium channel II have been expressed in Xenopus oocytes and have been investigated using the patch-clamp technique. In mutant E387Q the glutamic acid at position 387 has been replaced by glutamine, and in mutant D384N the aspartic acid at position 384 has been replaced by asparagine. 2. Mutant E387Q, previously shown to be resistant to block by tetrodotoxin (Noda et al. 1989), has a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to DNA
Share to Molecular Sequence Data

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Oocytes

Share to Sodium Channels

Source

Identifiers

PMID: 1660394
DOI: 10.1007/BF01561134

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single point mutations of the sodium channel drastically reduce the pore permeability without preventing its gating.PMID 1660394Read ↗

A tryptophan residue (W736) in the amino-terminus of the P-segment of domain II is involved in pore formation in Na(v)1.4 voltage-gated sodium channels.Semantic proximity Read ↗

Molecular basis of ion permeability in a voltage-gated sodium channel.Semantic proximity Read ↗

Two serial filters determine P2X7R cation selectivity, Ser342 in the central pore and lateral acidic residues at the cytoplasmic interfaceSemantic proximity Read ↗

Altered ionic selectivity of the sodium channel revealed by cysteine mutations within the pore.Semantic proximity Read ↗

A naturally occurring amino acid substitution in the voltage-dependent sodium channel selectivity filter affects channel gating.Semantic proximity Read ↗

Broadband Tuning the Voltage Dependence of a Sodium ChannelSemantic proximity Read ↗

A mutation causing pseudohypoaldosteronism type 1 identifies a conserved glycine that is involved in the gating of the epithelial sodium channel.Semantic proximity Read ↗

Mutational analysis of ion conduction and drug binding sites in the inner mouth of voltage-gated K+ channels.Semantic proximity Read ↗

A mutation in the extracellular domain of the α7 nAChR reduces calcium permeability.Semantic proximity Read ↗

Novel determinants of epithelial sodium channel gating within extracellular thumb domains.Semantic proximity Read ↗

Asymmetric organization of the pore region of the epithelial sodium channel.Semantic proximity Read ↗

A mutation in the pore of the sodium channel alters gating.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.