Interplay between acetylation and ubiquitination controls PSAT1 protein stability in lung adenocarcinoma
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
1 Online-Ressource.
- Sprache
-
Englisch
- Erschienen in
-
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
- Urheber
-
Liu, Yuhan
Xun, Wenze
Zhao, Tao
Huang, Menglin
Sun, Longhua
Wen, Guilan
Kang, Xiuhua
Wang, Jianbin
Han, Tianyu
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1038/s42003-024-07051-2
- URN
-
urn:nbn:de:101:1-2501092124439.665283756830
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:29 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Liu, Yuhan
- Xun, Wenze
- Zhao, Tao
- Huang, Menglin
- Sun, Longhua
- Wen, Guilan
- Kang, Xiuhua
- Wang, Jianbin
- Han, Tianyu
- SpringerLink (Online service)
Ähnliche Objekte (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