Evidence map›Paper›PMID 32807966›Full record

ArticleNature chemical biology2020

Structural basis for diamide modulation of ryanodine receptor.

Ruifang Ma, Omid Haji-Ghassemi, Dan Ma, Heng Jiang, Lianyun Lin, Li Yao, Arthur Samurkas, Yuxin Li, Yiwen Wang, Peng Cao and 6 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 125 citations in OpenAlex.

  1. Pesticidal evaluation of novel dual-chiralJournal of enzyme inhibition and medicinal chemistry · 2026
    Article
  2. Cylindrical Crystallization of CaInternational journal of molecular sciences · 2026
    Review
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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

16 authors at 6 institutions in 5 countries.

Ruifang Ma *Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.ORCID http://orcid.org/0000-0002-3663-2240
Omid Haji-Ghassemi *Department of Biochemistry and Molecular Biology, Life Sciences Institute, University of British Columbia, Vancouver, British Columbia, Canada.
Dan Ma *Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.
Heng Jiang *Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.
Lianyun LinTianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.
Li YaoTianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.
Arthur SamurkasTianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.ORCID http://orcid.org/0000-0002-9358-5938
Yuxin LiState Key Laboratory of Elemento-organic Chemistry, Nankai University, Tianjin, China.
Yiwen WangTianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.ORCID http://orcid.org/0000-0003-2069-6685
Peng CaoKey Laboratory of Drug Targets and Drug Leads for Degenerative Diseases, Affiliated Hospital of Integrated Traditional Chinese and Western Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
Shian WuState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, China.ORCID http://orcid.org/0000-0003-4990-6594
Yan ZhangTianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.ORCID http://orcid.org/0000-0003-2031-0631
Takashi MurayamaDepartment of Cellular and Molecular Pharmacology, Juntendo University Graduate School of Medicine, Tokyo, Japan.ORCID http://orcid.org/0000-0002-3845-2980
Bernard MoussianInterfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.ORCID http://orcid.org/0000-0002-2854-9500
Filip Van PetegemDepartment of Biochemistry and Molecular Biology, Life Sciences Institute, University of British Columbia, Vancouver, British Columbia, Canada. filip.vanpetegem@gmail.com.ORCID http://orcid.org/0000-0003-2728-8537
Zhiguang YuchiTianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China. yuchi@tju.edu.cn.ORCID http://orcid.org/0000-0003-2595-9106
Tianjin University · CNNankai University · CNUniversity of British Columbia · CAJuntendo University · JPNanjing University of Chinese Medicine · CNUniversity of Tübingen · DE

Funding

CIHR PJT-159601
6 · The paper itself

Abstract

The diamide insecticide class is one of the top-selling insecticides globally. They are used to control a wide range of pests by targeting their ryanodine receptors (RyRs). Here, we report the highest-resolution cryo-electron microscopy (cryo-EM) structure of RyR1 in the open state, in complex with the anthranilic diamide chlorantraniliprole (CHL). The 3.2-Å local resolution map facilitates unambiguous assignment of the CHL binding site. The molecule induces a conformational change by affecting the S4-S5 linker, triggering channel opening. The binding site is further corroborated by mutagenesis data, which reveal how diamide insecticides are selective to the Lepidoptera group of insects over honeybee or mammalian RyRs. Our data reveal that several pests have developed resistance via two mechanisms, steric hindrance and loss of contact. Our results provide a foundation for the development of highly selective pesticides aimed at overcoming resistance and therapeutic molecules to treat human myopathies.

Indexed as

Amino Acid SequenceAnimalsBeesBinding SitesCalcium Channel BlockersCryoelectron MicroscopyDiamideDrug DevelopmentDrug ResistanceInsecticidesLepidopteraModels, MolecularMutagenesisortho-AminobenzoatesProtein BindingProtein ConformationCalcium Channel BlockerschlorantranilipoleDiamideInsecticidesortho-AminobenzoatesRyanodine Receptor Calcium Release Channel

Identifiers

PMID32807966
OpenAlexW3049630427

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.