Polarity protein AF6 functions as a modulator of necroptosis by regulating ubiquitination of RIPK1 in liver diseases

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: Polarity protein AF6 functions as a modulator of necroptosis by regulating ubiquitination of RIPK1 in liver diseases ; volume:14 ; number:10 ; day:12 ; month:10 ; year:2023 ; pages:1-15 ; date:10.2023
Cell death & disease ; 14, Heft 10 (12.10.2023), 1-15, 10.2023

Creator: Xinyu, Wang
Qian, Wen
Yanjun, Wu
Jingwen, Kong
Keying, Xu
Jiazheng, Jiao
Haibing, Zhang
Kai, Wang
Xiao, Xu
Lixing, Zhan

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41419-023-06170-8

URN: urn:nbn:de:101:1-2024010121060893077918

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:29 AM CEST

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Associated

Xinyu, Wang
Qian, Wen
Yanjun, Wu
Jingwen, Kong
Keying, Xu
Jiazheng, Jiao
Haibing, Zhang
Kai, Wang
Xiao, Xu
Lixing, Zhan
SpringerLink (Online service)

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CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing

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ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis

5-iodotubercidin sensitizes cells to RIPK1-dependent necroptosis by interfering with NFκB signaling

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USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

Epstein-Barr virus encoded latent membrane protein 1 suppresses necroptosis through targeting RIPK1/3 ubiquitination

Poly-ubiquitination in TNFR1-mediated necroptosis

RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development

Hochschulschrift

The role of RIPK1 ubiquitination during inflammatory and cell death signaling

CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing

Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1

ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis

5-iodotubercidin sensitizes cells to RIPK1-dependent necroptosis by interfering with NFκB signaling

Influenza virus infection activates TAK1 to suppress RIPK3-independent apoptosis and RIPK1-dependent necroptosis

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

Epstein-Barr virus encoded latent membrane protein 1 suppresses necroptosis through targeting RIPK1/3 ubiquitination

Poly-ubiquitination in TNFR1-mediated necroptosis

RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development

Hochschulschrift

The role of RIPK1 ubiquitination during inflammatory and cell death signaling

CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing

Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1

ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis

5-iodotubercidin sensitizes cells to RIPK1-dependent necroptosis by interfering with NFκB signaling

Influenza virus infection activates TAK1 to suppress RIPK3-independent apoptosis and RIPK1-dependent necroptosis

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

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Polarity protein AF6 functions as a modulator of necroptosis by regulating ubiquitination of RIPK1 in liver diseases

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Other Objects (12)

Epstein-Barr virus encoded latent membrane protein 1 suppresses necroptosis through targeting RIPK1/3 ubiquitination

Poly-ubiquitination in TNFR1-mediated necroptosis

RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development

The role of RIPK1 ubiquitination during inflammatory and cell death signaling

CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing

Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1

ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis

5-iodotubercidin sensitizes cells to RIPK1-dependent necroptosis by interfering with NFκB signaling

Influenza virus infection activates TAK1 to suppress RIPK3-independent apoptosis and RIPK1-dependent necroptosis

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

Epstein-Barr virus encoded latent membrane protein 1 suppresses necroptosis through targeting RIPK1/3 ubiquitination

Poly-ubiquitination in TNFR1-mediated necroptosis

RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development

The role of RIPK1 ubiquitination during inflammatory and cell death signaling

CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing

Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1

ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis

5-iodotubercidin sensitizes cells to RIPK1-dependent necroptosis by interfering with NFκB signaling

Influenza virus infection activates TAK1 to suppress RIPK3-independent apoptosis and RIPK1-dependent necroptosis

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

Epstein-Barr virus encoded latent membrane protein 1 suppresses necroptosis through targeting RIPK1/3 ubiquitination

Poly-ubiquitination in TNFR1-mediated necroptosis

RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development

The role of RIPK1 ubiquitination during inflammatory and cell death signaling

CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing

Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1

ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis

5-iodotubercidin sensitizes cells to RIPK1-dependent necroptosis by interfering with NFκB signaling

Influenza virus infection activates TAK1 to suppress RIPK3-independent apoptosis and RIPK1-dependent necroptosis

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

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