Evidence map›Paper›PMID 33712586›Full record

ArticleNature communications2021

The amyloid structure of mouse RIPK3 (receptor interacting protein kinase 3) in cell necroptosis.

Xia-Lian Wu, Hong Hu, Xing-Qi Dong, Jing Zhang, Jian Wang, Charles D Schwieters, Jing Liu, Guo-Xiang Wu, Bing Li, Jing-Yu Lin and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Necroptosis in obesity: a complex cell death event.Apoptosis : an international journal on programmed cell death · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Frontiers in immunology · 2024
    Article
  16. RHIMoving fibrils of death.Cell research · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. The role of RHIM in necroptosis.Biochemical Society transactions · 2022
    Article
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

12 authors at 3 institutions in 2 countries.

Xia-Lian Wu *School of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Hong Hu *School of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Xing-Qi DongSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Jing ZhangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Jian WangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Charles D SchwietersLaboratory of Imaging Sciences, Office of Intramural Research, Center for Information Technology, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-4216-4658
Jing LiuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Guo-Xiang WuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Bing LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Jing-Yu LinSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China.
Hua-Yi WangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China. wanghuayi@shanghaitech.edu.cn.ORCID 0000-0001-6274-3844
Jun-Xia LuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, PR China. lujx@shanghaitech.edu.cn.ORCID 0000-0002-4270-5821
Chinese Academy of Sciences · CNShanghaiTech University · CNNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RIPK3 amyloid complex plays crucial roles during TNF-induced necroptosis and in response to immune defense in both human and mouse. Here, we have structurally characterized mouse RIPK3 homogeneous self-assembly using solid-state NMR, revealing a well-ordered N-shaped amyloid core structure featured with 3 parallel in-register β-sheets. This structure differs from previously published human RIPK1/RIPK3 hetero-amyloid complex structure, which adopted a serpentine fold. Functional studies indicate both RIPK1-RIPK3 binding and RIPK3 amyloid formation are essential but not sufficient for TNF-induced necroptosis. The structural integrity of RIPK3 fibril with three β-strands is necessary for signaling. Molecular dynamics simulations with a mouse RIPK1/RIPK3 model indicate that the hetero-amyloid is less stable when adopting the RIPK3 fibril conformation, suggesting a structural transformation of RIPK3 from RIPK1-RIPK3 binding to RIPK3 amyloid formation. This structural transformation would provide the missing link connecting RIPK1-RIPK3 binding to RIPK3 homo-oligomer formation in the signal transduction.

Indexed as

AmyloidAnimalsBenzothiazolesCell SurvivalDrosophilaHerpesviridaeHumansMiceMolecular Dynamics SimulationNecroptosisProtein ConformationRatsReceptor-Interacting Protein Serine-Threonine KinasesSequence AlignmentSequence Analysis, ProteinSignal TransductionAmyloidBenzothiazolesReceptor-Interacting Protein Serine-Threonine KinasesRipk1 protein, mouseRipk3 protein, mousethioflavin T

Identifiers

PMID33712586
PMCPMC7955032
OpenAlexW3133642667

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.