Evidence map›Paper›PMID 30587448›Full record

ArticleBioorganic & medicinal chemistry letters2019

Identification of peptidomimetics as novel chemical probes modulating fibroblast growth factor 14 (FGF14) and voltage-gated sodium channel 1.6 (Nav1.6) protein-protein interactions.

Zhiqing Liu, Paul Wadsworth, Aditya K Singh, Haiying Chen, Pingyuan Wang, Oluwarotimi Folorunso, Pietro Scaduto, Syed R Ali, Fernanda Laezza, Jia Zhou

Abstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Development of Allosteric Modulators of Voltage-Gated NaCurrent topics in medicinal chemistry · 2021
    Review
  6. Differential Modulation of the Voltage-Gated NaFrontiers in molecular biosciences · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Paroxysmal Movement Disorders: Recent Advances.Current neurology and neuroscience reports · 2019
    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

10 authors.

Zhiqing LiuDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Paul WadsworthDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Aditya K SinghDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Haiying ChenDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Pingyuan WangDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Oluwarotimi FolorunsoDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Pietro ScadutoDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Syed R AliDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States.
Fernanda LaezzaDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States. Electronic address: felaezza@utmb.edu.
Jia ZhouDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd, Galveston, Galveston, TX 77555, United States. Electronic address: jizhou@utmb.edu.

Funding

Validation of FGF14 as a New Molecular Target of GSK3R01MH095995 · NIMH · UNIVERSITY OF TEXAS MED BR GALVESTON · PI LAEZZA, FERNANDA · 2012 to 2016
$1.9M
Discovery of Chemical Probes for Psychiatric Disorders and AddictionR01MH111107 · NIMH · UNIVERSITY OF TEXAS MED BR GALVESTON · PI LAEZZA, FERNANDA, ZHOU, JIA · 2016 to 2018
$1.6M
Core Center for Translational Addiction SciencesP30DA028821 · NIDA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI CUNNINGHAM, KATHRYN A. · 2009 to 2010
$1.5M
Training in Pharmacological SciencesT32GM089657 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI HANCOCK, JOHN F · 2010 to 2014
$728k
Clinical and Behavioral Science Training in Aging and Health DisparitiesT32AG051131 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI MARKIDES, KYRIAKOS S · 2015 to 2019
$436k
Malvern MicroCal PEAQ Isothermal Titration CalorimeterS10OD023576 · OD · UNIVERSITY OF TEXAS MED BR GALVESTON · PI RAJARATHNAM, KRISHNA · 2017 to 2017
$120k
NIA NIH HHS T32 AG051131NIDA NIH HHS P30 DA028821NIGMS NIH HHS T32 GM089657NIH HHS S10 OD023576NIMH NIH HHS R01 MH095995NIMH NIH HHS R01 MH111107
6 · The paper itself

Abstract

The voltage-gated sodium (Nav) channel is the molecular determinant of action potential in neurons. Protein-protein interactions (PPI) between the intracellular Nav1.6 C-tail and its regulatory protein fibroblast growth factor 14 (FGF14) provide an ideal and largely untapped opportunity for development of neurochemical probes. Based on a previously identified peptide FLPK, mapped to the FGF14:FGF14 PPI interface, we have designed and synthesized a series of peptidomimetics with the intent of increasing clogP values and improving cell permeability relative to the parental lead peptide. In-cell screening using the split-luciferase complementation (LCA) assay identified ZL0177 (13) as the most potent inhibitor of the FGF14:Nav1.6 channel complex assembly with an apparent IC

Indexed as

Dose-Response Relationship, DrugFibroblast Growth FactorsHumansMolecular ProbesMolecular StructureNAV1.6 Voltage-Gated Sodium ChannelOligopeptidesPeptidomimeticsProtein BindingStructure-Activity Relationshipfibroblast growth factor 14Fibroblast Growth FactorsMolecular ProbesNAV1.6 Voltage-Gated Sodium ChannelOligopeptidesPeptidomimeticsSCN8A protein, humanChemical probesFibroblast growth factorProtein-protein interactionsSplit-luciferase complementation assayVoltage-gated sodium channels

Identifiers

PMID30587448
PMCPMC6748043

What OpenQuestion holds

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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.