Evidence map›Paper›PMID 34358664›Full record

ArticleInsect biochemistry and molecular biology2021

Charge substitutions at the voltage-sensing module of domain III enhance actions of site-3 and site-4 toxins on an insect sodium channel.

Qing Zhu, Yuzhe Du, Yoshiko Nomura, Rong Gao, Zixuan Cang, Guo-Wei Wei, Dalia Gordon, Michael Gurevitz, James Groome, Ke Dong

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Insect biochemistry and molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 6 institutions in 4 countries.

Qing ZhuKey Lab of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Key Laboratory of Control Technology and Standard for Agro-product Safety and Quality, Ministry of Agriculture, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing, China; Department of Entomology, Michigan State University, East Lansing, MI, USA.
Yuzhe DuDepartment of Entomology, Michigan State University, East Lansing, MI, USA.
Yoshiko NomuraDepartment of Entomology, Michigan State University, East Lansing, MI, USA.
Rong GaoDepartment of Hygienic Analysis and Detection, School of Public Health, Nanjing Medical University, 818 Tianyuan East Road, Nanjing, Jiangsu, China.
Zixuan CangDepartment of Mathematics, Michigan State University, East Lansing, MI, USA.
Guo-Wei WeiDepartment of Mathematics, Michigan State University, East Lansing, MI, USA.
Dalia GordonDepartment of Plant Molecular Biology & Ecology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv, Israel.
Michael GurevitzDepartment of Plant Molecular Biology & Ecology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv, Israel. Electronic address: mamgur@post.tau.ac.il.
James GroomeDepartment of Biological Sciences, Idaho State University, Pocatello, ID, USA.
Ke DongDepartment of Entomology, Michigan State University, East Lansing, MI, USA; Department of Biology, Duke University, Durham, NC, USA. Electronic address: ke.dong@duke.edu.
Michigan State University · USTel Aviv University · ILDuke University · USIdaho State University · USJiangsu Academy of Agricultural Sciences · CNNanjing Medical University · CN

Funding

Molecular mechanisms of action and resistance of sodium channel-targeting insectiR01GM057440 · NIGMS · MICHIGAN STATE UNIVERSITY · PI DONG, KE, HUGHSON, FREDERICK M · 1999 to 2023
$5.4M
Synergistic integration of topology and machine learning for the predictions of protein-ligand binding affinities and mutation impactsR01GM126189 · NIGMS · MICHIGAN STATE UNIVERSITY · PI WEI, GUOWEI · 2018 to 2021
$1.4M
NIGMS NIH HHS R01 GM057440NIGMS NIH HHS R01 GM126189
6 · The paper itself

Abstract

Scorpion α-toxins bind at the pharmacologically-defined site-3 on the sodium channel and inhibit channel inactivation by preventing the outward movement of the voltage sensor in domain IV (IVS4), whereas scorpion β-toxins bind at site-4 on the sodium channel and enhance channel activation by trapping the voltage sensor of domain II (IIS4) in its outward position. However, limited information is available on the role of the voltage-sensing modules (VSM, comprising S1-S4) of domains I and III in toxin actions. We have previously shown that charge reversing substitutions of the innermost positively-charged residues in IIIS4 (R4E, R5E) increase the activity of an insect-selective site-4 scorpion toxin, Lqh-dprIT

Indexed as

AnimalsCnidarian VenomsDrosophila melanogasterInsect ProteinsOocytesScorpion VenomsSodium ChannelsCnidarian VenomsInsect ProteinsScorpion VenomsSodium ChannelsElectrophysiologyHomology modelingInsect sodium channelMutagenesisScorpion α-toxinScorpion β-toxin

Identifiers

PMID34358664
PMCPMC9376739
OpenAlexW3190727443

What OpenQuestion holds

Textmetadata
LicenceTDM
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.