Evidence map›Paper›PMID 28475174›Full record

ReviewCell death and differentiation2017

Diverse ubiquitin linkages regulate RIP kinases-mediated inflammatory and cell death signaling.

Axel Witt, Domagoj Vucic

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.7field-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

76 citing papers in PubMed, 127 citations in OpenAlex.

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  12. ANKK1 Is a Wnt/PCP Scaffold Protein for Neural F-ACTIN Assembly.International journal of molecular sciences · 2024
    Article
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  20. Functions of the RIP kinase family members in the skin.Cellular and molecular life sciences : CMLS · 2023
    Review

16 more citing papers are in PubMed but not listed here.

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

2 authors.

Axel WittDepartment of Early Discovery Biochemistry, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.
Domagoj VucicDepartment of Early Discovery Biochemistry, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the RIP kinase family are key regulators of inflammation and cell death signaling implicated in maintaining immune responses and proper tissue homeostasis. Increasing evidence points to post-translational modifications of RIP1, RIP2 and RIP3 as being critical for regulating their function. Ubiquitination and the E3 ligases, such as inhibitors of apoptosis (IAP) proteins and LUBAC, that direct substrate selectivity as well as the deubiquitinating enzymes, such as A20 and OTULIN, that reverse these modifications dictate the outcome of RIP kinase signaling. Perturbation of the tightly regulated RIP1, RIP2 and RIP3 ubiquitination can lead to signaling disbalance in TNF, TLR and NOD1/2-controlled pathways and result in severe human pathologies. In this review, we focus on the biological function of ubiquitin-modifying enzymes in the context of RIP1, RIP2 and RIP3 signaling. We also discuss the impact of deregulated ubiquitin networks in RIP1, RIP2 and RIP3 signaling pathways on human health.

Indexed as

Signal TransductionAnimalsCell DeathHumansInflammationModels, BiologicalReceptor-Interacting Protein Serine-Threonine KinasesUbiquitinUbiquitinationReceptor-Interacting Protein Serine-Threonine KinasesUbiquitin

Identifiers

PMID28475174
PMCPMC5520166
OpenAlexW2610913767

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.