Amino acid residues required for fast Na(+)-channel inactivation: charge neutralizations and deletions in the III-IV linker (Q37301144)

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English	Amino acid residues required for fast Na(+)-channel inactivation: charge neutralizations and deletions in the III-IV linker	scientific article

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19 August 2017

title

Amino acid residues required for fast Na(+)-channel inactivation: charge neutralizations and deletions in the III-IV linker (English)

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19 August 2017

author

Alan Goldin

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author name string

D E Patton

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1

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50451

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19 August 2017

J W West

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2

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Europe PubMed Central

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50451

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19 August 2017

W A Catterall

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3

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50451

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19 August 2017

A L Goldin

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4

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50451

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19 August 2017

language of work or name

English

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publication date

1 November 1992

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50451

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19 August 2017

published in

Proceedings of the National Academy of Sciences of the United States of America

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50451

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19 August 2017

volume

89

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Europe PubMed Central

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50451

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19 August 2017

issue

22

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50451

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19 August 2017

page(s)

10905-10909

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50451

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19 August 2017

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A neutral amino acid change in segment IIS4 dramatically alters the gating properties of the voltage-dependent sodium channel

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Asymmetric electrostatic effects on the gating of rat brain sodium channels in planar lipid membranes

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Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel

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A cluster of hydrophobic amino acid residues required for fast Na(+)-channel inactivation

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Sodium channel gating in clonal pituitary cells. The inactivation step is not voltage dependent

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Evidence for the involvement of more than one mRNA species in controlling the inactivation process of rat and rabbit brain Na channels expressed in Xenopus oocytes

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Phosphorylation affects voltage gating of the delayed rectifier K+ channel by electrostatic interactions

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Changes in sodium channel gating produced by point mutations in a cytoplasmic linker

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Slow inactivation of the sodium conductance in squid giant axons. Pronase resistance

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A phosphorylation site in the Na+ channel required for modulation by protein kinase C

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Identification of an intracellular peptide segment involved in sodium channel inactivation

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reference URL

https://pubmed.ncbi.nlm.nih.gov/1332059

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structural parts involved in activation and inactivation of the sodium channel

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https://pubmed.ncbi.nlm.nih.gov/1332059

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12 December 2020

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Slow changes in currents through sodium channels in frog muscle membrane

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based on heuristic

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Identifiers

DOI

10.1073/PNAS.89.22.10905

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stated in

Europe PubMed Central

PMC publication ID

50451

retrieved

19 August 2017

ADS bibcode

1992PNAS...8910905P

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PMC publication ID

50451

1 reference

stated in

Europe PubMed Central

PMC publication ID

50451

retrieved

19 August 2017

PubMed publication ID

1332059

1 reference

stated in

Europe PubMed Central

PMC publication ID

50451

retrieved

19 August 2017

ResearchGate publication ID

21823769

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