Evidence map›Paper›PMID 12885638›Full record

ArticleBiophysical journal2003

Tryptophan scanning of D1S6 and D4S6 C-termini in voltage-gated sodium channels.

Sho-Ya Wang, Kaitlin Bonner, Corinna Russell, Ging Kuo Wang

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A Mechanistic Reinterpretation of Fast Inactivation in Voltage-Gated NabioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Effects of FGF14 and NaThe Journal of general physiology · 2019
    Article
  12. Article
  13. Article
  14. Review
  15. Single rat muscle NaProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Pharmacology of the NaProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Small molecule modulation of voltage gated sodium channels.Current opinion in structural biology · 2017
    Review
  18. Regulation of NaThe Journal of general physiology · 2017
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Sho-Ya WangDepartment of Biology, State University of New York at Albany, Albany, New York, USA.
Kaitlin Bonner
Corinna Russell
Ging Kuo Wang
Brigham and Women's Hospital · USAlbany State University · USUniversity at Albany, State University of New York · US

Funding

Activation Gating in Human Heart Na+ ChannelsR01HL066076 · NHLBI · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI WANG, SHO-YA Y · 2001 to 2004
$1.0M
NHLBI NIH HHS HL66076NHLBI NIH HHS R01 HL066076
6 · The paper itself

Abstract

Recent reports suggest that four S6 C-termini may jointly close the voltage-gated cation channel at the cytoplasmic side, probably as an inverted teepee structure. In this study we substituted individually a total of 18 residues at D1S6 and D4S6 C-terminal ends of the rNav1.4 Na(+) channel alpha-subunit with tryptophan (W) and examined their corresponding gating properties when expressed in Hek293t cells along with beta1 subunit. Several W-mutants displayed significant changes in activation, fast inactivation, and/or slow inactivation gating. In particular, five S6 W-mutants showed incomplete fast inactivation with noninactivating maintained currents present. Cysteine (C) substitutions of these five residues resulted in two mutants with slightly more maintained currents. Multiple substitutions at these five positions yielded two mutants (L437C/A438W, L435W/L437C/A438W) that exhibited phenotypes with minimal fast inactivation. Unexpectedly, such inactivation-deficient mutants expressed Na(+) currents as well as did the wild-type. Furthermore, all mutants with impaired fast inactivation exhibited an enhanced slow inactivation phenotype. Implications of these results will be discussed in terms of indirect allosteric modulations via amino acid substitutions and/or a direct involvement of S6 C-termini in Na(+) channel gating.

Indexed as

MutationStructure-Activity RelationshipCell LineHumansIon Channel GatingKidneyMembrane PotentialsMuscle ProteinsMutagenesis, Site-DirectedNAV1.4 Voltage-Gated Sodium ChannelPotassium Channels, Voltage-GatedSodium ChannelsTryptophanMuscle ProteinsNAV1.4 Voltage-Gated Sodium ChannelPotassium Channels, Voltage-GatedSCN4A protein, humanSodium ChannelsTryptophan

Identifiers

PMID12885638
PMCPMC1303212
OpenAlexW2051070430

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.