Interplay between acetylation and ubiquitination controls PSAT1 protein stability in lung adenocarcinoma

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: Interplay between acetylation and ubiquitination controls PSAT1 protein stability in lung adenocarcinoma ; volume:7 ; number:1 ; day:21 ; month:10 ; year:2024 ; pages:1-15 ; date:12.2024
Communications biology ; 7, Heft 1 (21.10.2024), 1-15, 12.2024

Creator: Liu, Yuhan
Xun, Wenze
Zhao, Tao
Huang, Menglin
Sun, Longhua
Wen, Guilan
Kang, Xiuhua
Wang, Jianbin
Han, Tianyu

Contributor: SpringerLink (Online service)

DOI: 10.1038/s42003-024-07051-2

URN: urn:nbn:de:101:1-2501092124439.665283756830

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

Liu, Yuhan
Xun, Wenze
Zhao, Tao
Huang, Menglin
Sun, Longhua
Wen, Guilan
Kang, Xiuhua
Wang, Jianbin
Han, Tianyu
SpringerLink (Online service)

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

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LINC01559 promotes lung adenocarcinoma metastasis by disrupting the ubiquitination of vimentin

Acetylation- and ubiquitination-regulated SFMBT2 acts as a tumor suppressor in clear cell renal cell carcinoma

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Exosomal circ_0026611 contributes to lymphangiogenesis by reducing PROX1 acetylation and ubiquitination in human lymphatic endothelial cells (HLECs)

N-terminal acetylation can stabilize proteins independent of their ubiquitination

Frequent mutations in acetylation and ubiquitination sites suggest novel driver mechanisms of cancer

HDAC10 switches NLRP3 modification from acetylation to ubiquitination and attenuates acute inflammatory diseases

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

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

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

LINC01559 promotes lung adenocarcinoma metastasis by disrupting the ubiquitination of vimentin

Acetylation- and ubiquitination-regulated SFMBT2 acts as a tumor suppressor in clear cell renal cell carcinoma

The cohesin acetylation cycle controls chromatin loop length through a PDS5A brake mechanism

Exosomal circ_0026611 contributes to lymphangiogenesis by reducing PROX1 acetylation and ubiquitination in human lymphatic endothelial cells (HLECs)

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Interplay between acetylation and ubiquitination controls PSAT1 protein stability in lung adenocarcinoma

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Other Objects (12)

N-terminal acetylation can stabilize proteins independent of their ubiquitination

Frequent mutations in acetylation and ubiquitination sites suggest novel driver mechanisms of cancer

HDAC10 switches NLRP3 modification from acetylation to ubiquitination and attenuates acute inflammatory diseases

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

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

LINC01559 promotes lung adenocarcinoma metastasis by disrupting the ubiquitination of vimentin

Acetylation- and ubiquitination-regulated SFMBT2 acts as a tumor suppressor in clear cell renal cell carcinoma

The cohesin acetylation cycle controls chromatin loop length through a PDS5A brake mechanism

Exosomal circ_0026611 contributes to lymphangiogenesis by reducing PROX1 acetylation and ubiquitination in human lymphatic endothelial cells (HLECs)

N-terminal acetylation can stabilize proteins independent of their ubiquitination

Frequent mutations in acetylation and ubiquitination sites suggest novel driver mechanisms of cancer

HDAC10 switches NLRP3 modification from acetylation to ubiquitination and attenuates acute inflammatory diseases

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

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

LINC01559 promotes lung adenocarcinoma metastasis by disrupting the ubiquitination of vimentin

Acetylation- and ubiquitination-regulated SFMBT2 acts as a tumor suppressor in clear cell renal cell carcinoma

The cohesin acetylation cycle controls chromatin loop length through a PDS5A brake mechanism

Exosomal circ_0026611 contributes to lymphangiogenesis by reducing PROX1 acetylation and ubiquitination in human lymphatic endothelial cells (HLECs)

N-terminal acetylation can stabilize proteins independent of their ubiquitination

Frequent mutations in acetylation and ubiquitination sites suggest novel driver mechanisms of cancer

HDAC10 switches NLRP3 modification from acetylation to ubiquitination and attenuates acute inflammatory diseases

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

Citrullination-acetylation interplay guides E2F-1 activity during the inflammatory response

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

LINC01559 promotes lung adenocarcinoma metastasis by disrupting the ubiquitination of vimentin

Acetylation- and ubiquitination-regulated SFMBT2 acts as a tumor suppressor in clear cell renal cell carcinoma

The cohesin acetylation cycle controls chromatin loop length through a PDS5A brake mechanism

Exosomal circ_0026611 contributes to lymphangiogenesis by reducing PROX1 acetylation and ubiquitination in human lymphatic endothelial cells (HLECs)

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