Evidence map›Paper›PMID 41498337›Full record

ArticleThe Biochemical journal2026

De novo cyclic peptides allow visualisation of the monomeric and functional amyloid conformations of the kinase RIPK3.

Jessica A Buchanan, Olivia Lavidis, Nicholas Shields, Katriona Harrison, Huy T Nguyen, Richard J Payne, Toby Passioura, Megan Steain, Margaret Sunde

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In one paragraph

Article in The Biochemical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Jessica A BuchananSchool of Medical Sciences and Sydney Infectious Diseases, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-8263-3850
Olivia LavidisSchool of Medical Sciences and Sydney Infectious Diseases, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0009-0001-3184-0155
Nicholas ShieldsSchool of Medical Sciences and Sydney Infectious Diseases, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0003-2990-0478
Katriona HarrisonSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0001-5174-5449
Huy T NguyenSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0001-8962-9291
Richard J PayneSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-3618-9226
Toby PassiouraSydney Analytical Core Research Facility, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-6089-5067
Megan SteainSchool of Medical Sciences and Sydney Infectious Diseases, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-7631-4204
Margaret SundeSchool of Medical Sciences and Sydney Infectious Diseases, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-0150-3203

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor interacting protein kinase 3 (RIPK3) is a central regulator of necroptosis and a key mediator of inflammatory signalling. Its function is orchestrated through RIP homotypic interaction motif (RHIM)-dependent interactions with other RHIM-containing adapter proteins, forming amyloid-structured necrosomes that trigger kinase activation and subsequently lead to immunogenic cell lysis. Necroptosis eliminates infected or damaged cells and provokes a strong inflammatory response. Dysregulated necroptosis is implicated in chronic inflammatory diseases and associated with ischaemic injury. Despite separate structural elucidation of the isolated RIPK3 kinase domain and the amyloid fibrils formed by the RIPK3 RHIM-containing region, visualising full-length human RIPK3 in live cells remains challenging due to a lack of specific tools. To address this, we employed random non-standard peptide integrated discovery (RaPID) mRNA display to identify cyclic peptides that bind the RHIM-containing region of RIPK3 during its assembly into amyloid fibrils. Three peptides were selected for characterisation and demonstrate utility in visualising RIPK3 in human cells. These peptides represent promising tools for probing RIPK3 localisation and modulating its function.

Indexed as

AmyloidPeptides, CyclicReceptor-Interacting Protein Serine-Threonine KinasesHumansProtein ConformationAmyloidPeptides, CyclicReceptor-Interacting Protein Serine-Threonine KinasesRIPK3 protein, humanamyloidnecroptosispeptidesRIPK3self-assembly

Identifiers

PMID41498337
PMCPMC12905488

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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.