Evidence map›Paper›PMID 42850283›Full record

ArticleCell death and differentiation2026

Death domain-mediated higher-order oligomerization of RIPK1 drives TNF-induced signaling.

Ying Chen, Jianwei Li, Yaw Bia Tan, Lihua Lai, Ping Liu, Ita Novita Sari, Anandhkumar Raju, Vinh Thang Huynh, Amhed Missael Vargas Velazquez, Samuel Jianjie Yeo and 2 more

Abstract read
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In one paragraph

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

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

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

12 authors.

Ying Chen *Institute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore. e0010760@u.nus.edu.ORCID http://orcid.org/0000-0001-7489-8309
Jianwei Li *Central Laboratory, The Affiliated Yongchuan Hospital of Chongqing Medical University, Chongqing, China.
Yaw Bia Tan *Lee Kong Chian School of Medicine, Nanyang Technological University, EMB 03-07, 59 Nanyang Drive, Singapore, 636921, Singapore.
Lihua LaiInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.
Ping LiuLee Kong Chian School of Medicine, Nanyang Technological University, EMB 03-07, 59 Nanyang Drive, Singapore, 636921, Singapore.
Ita Novita SariInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.ORCID http://orcid.org/0000-0001-9475-7992
Anandhkumar RajuInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.
Vinh Thang HuynhInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.
Amhed Missael Vargas VelazquezInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.
Samuel Jianjie YeoInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.ORCID http://orcid.org/0000-0002-7145-1082
Dahai LuoLee Kong Chian School of Medicine, Nanyang Technological University, EMB 03-07, 59 Nanyang Drive, Singapore, 636921, Singapore. LuoDahai@ntu.edu.sg.ORCID http://orcid.org/0000-0001-7637-7275
Vinay TergaonkarInstitute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore. vinay.tergaonkar@gmail.com.ORCID http://orcid.org/0000-0001-9009-0844

Funding

MOH | National Medical Research Council (NMRC) MOH-001333-00National Research Foundation Singapore (National Research Foundation-Prime Minister's office, Republic of Singapore) NRF-CRP26-2021-0001
6 · The paper itself

Abstract

RIPK1 paradoxically orchestrates pro-survival and pro-death pathways through its scaffolding and kinase activities. Downstream of TNFR1, RIPK1 initiates the formation of two distinct multiprotein complexes: complex I for cell survival and complex IIa/IIb for apoptosis or necroptosis. However, the molecular architecture that initiates RIPK1-mediated assembly of these multiprotein signaling complexes remains unknown. Here, we elucidate the filamentous structure of the death domain of RIPK1 (

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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.