Evidence map›Paper›PMID 30367066›Full record

ArticleNature communications2018

A FRET biosensor for necroptosis uncovers two different modes of the release of DAMPs.

Shin Murai, Yoshifumi Yamaguchi, Yoshitaka Shirasaki, Mai Yamagishi, Ryodai Shindo, Joanne M Hildebrand, Ryosuke Miura, Osamu Nakabayashi, Mamoru Totsuka, Taichiro Tomida and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 84 citations in OpenAlex.

  1. Structural and molecular principles of DAMP biology.Nature structural & molecular biology · 2026
    Review
  2. Review
  3. Article
  4. Nanovaccines with ferroptosis, necroptosis and STING-activation for synergistic immunotherapy.Journal of experimental & clinical cancer research : CR · 2026
    Article
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  6. Article
  7. Review
  8. Review
  9. Article
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  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Necroptosis and Its Involvement in Various Diseases.Advances in experimental medicine and biology · 2024
    Article
  19. Homer1 ameliorates ischemic stroke by inhibiting necroptosis-induced neuronal damage and neuroinflammation.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 7 institutions in 2 countries.

Shin MuraiDepartment of Biochemistry, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan.ORCID http://orcid.org/0000-0002-7516-403X
Yoshifumi YamaguchiHibernation Metabolism, Physiology, and Development Group, Environmental Biology Division, Institute of Low Temperature Science, Hokkaido University, Kita 19, Nishi 8, Kita-ku, Sapporo, Hokkaido, 060-0819, Japan.ORCID http://orcid.org/0000-0001-7340-4557
Yoshitaka ShirasakiPrecursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, Chiyoda-ku, Tokyo, 102-0075, Japan.ORCID http://orcid.org/0000-0002-3808-1630
Mai YamagishiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID http://orcid.org/0000-0002-4449-5899
Ryodai ShindoDepartment of Biochemistry, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan.ORCID http://orcid.org/0000-0003-4817-2867
Joanne M HildebrandDivision of Cell Signaling and Cell Death, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.ORCID http://orcid.org/0000-0002-1456-2042
Ryosuke MiuraDepartment of Biochemistry, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan.ORCID http://orcid.org/0000-0003-1249-7803
Osamu NakabayashiDepartment of Biochemistry, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan.ORCID http://orcid.org/0000-0002-3752-6415
Mamoru TotsukaDepartment of Food Science and Technology, Faculty of Applied Life Science, Nippon Veterinary and Life Science University, 1-7-1 Kyonancho, Musashino-shi, Tokyo, 180-8602, Japan.ORCID http://orcid.org/0000-0001-6376-6490
Taichiro TomidaDepartment of Physiology, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan.ORCID http://orcid.org/0000-0002-1950-4896
Satomi Adachi-AkahaneDepartment of Physiology, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan.ORCID http://orcid.org/0000-0002-8218-8523
Sotaro UemuraDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID http://orcid.org/0000-0001-9701-1803
John SilkeDivision of Cell Signaling and Cell Death, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.ORCID http://orcid.org/0000-0002-7611-5774
Hideo YagitaDepartment of Immunology, Juntendo University Graduate School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo, 113-8421, Japan.ORCID http://orcid.org/0000-0003-4279-9343
Masayuki MiuraDepartment of Genetics, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID http://orcid.org/0000-0001-7444-5705
Hiroyasu NakanoDepartment of Biochemistry, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo, 143-8540, Japan. hiroyasu.nakano@med.toho-u.ac.jp.ORCID http://orcid.org/0000-0003-4843-1427
Toho University · JPThe University of Tokyo · JPThe University of Melbourne · AUHokkaido University · JPJapan Science and Technology Agency · JPJuntendo University · JPNippon Veterinary and Life Science University · JP

Funding

Department of Health | National Health and Medical Research Council (NHMRC) GNT1105023Department of Health | National Health and Medical Research Council (NHMRC) GNT1107149Department of Health | National Health and Medical Research Council (NHMRC) GNT1142669Japan Agency for Medical Research and Development (AMED) JP17gm0610004Japan Agency for Medical Research and Development (AMED) JP17gm5010001Japan Society for the Promotion of Science (JSPS) 16H06385Japan Society for the Promotion of Science (JSPS) 16K01378Japan Society for the Promotion of Science (JSPS) 17H04069Japan Society for the Promotion of Science (JSPS) 17K19533Japan Society for the Promotion of Science (JSPS) PRESTO JP17940748Ministry of Education, Culture, Sports, Science, and Technology (MEXT) 15H01366Ministry of Education, Culture, Sports, Science, and Technology (MEXT) 17H05496Ministry of Education, Culture, Sports, Science, and Technology (MEXT) 26110003Ministry of Education, Culture, Sports, Science, and Technology (MEXT) 26110005
6 · The paper itself

Abstract

Necroptosis is a regulated form of necrosis that depends on receptor-interacting protein kinase (RIPK)3 and mixed lineage kinase domain-like (MLKL). While danger-associated molecular pattern (DAMP)s are involved in various pathological conditions and released from dead cells, the underlying mechanisms are not fully understood. Here we develop a fluorescence resonance energy transfer (FRET) biosensor, termed SMART (a sensor for MLKL activation by RIPK3 based on FRET). SMART is composed of a fragment of MLKL and monitors necroptosis, but not apoptosis or necrosis. Mechanistically, SMART monitors plasma membrane translocation of oligomerized MLKL, which is induced by RIPK3 or mutational activation. SMART in combination with imaging of the release of nuclear DAMPs and Live-Cell Imaging for Secretion activity (LCI-S) reveals two different modes of the release of High Mobility Group Box 1 from necroptotic cells. Thus, SMART and LCI-S uncover novel regulation of the release of DAMPs during necroptosis.

Indexed as

Biosensing TechniquesAlarminsAnimalsApoptosisCell MembraneCells, CulturedEndosomal Sorting Complexes Required for TransportGene SilencingHistonesHMGB1 ProteinHumansLuminescent ProteinsMiceMolecular ImagingNecrosisPhosphorylationAlarminsEndosomal Sorting Complexes Required for TransportHistonesHMGB1 ProteinLuminescent ProteinsProtein KinasesReceptor-Interacting Protein Serine-Threonine Kinases

Identifiers

PMID30367066
PMCPMC6203740
OpenAlexW2896390248

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.