Results 21 to 30 of about 35,698 (247)

SUMOylation Connects Cell Stress Responses and Inflammatory Control: Lessons From the Gut as a Model Organ

open access: yesFrontiers in Immunology, 2021
Conjugation with the small ubiquitin-like modifier (SUMO) constitutes a key post-translational modification regulating the stability, activity, and subcellular localization of its target proteins.
Jörn Karhausen   +3 more
doaj   +1 more source

Sumoylation of the human histone H4 tail inhibits p300-mediated transcription by RNA polymerase II in cellular extracts

open access: yeseLife, 2021
The post-translational modification of histones by the small ubiquitin-like modifier (SUMO) protein has been associated with gene regulation, centromeric localization, and double-strand break repair in eukaryotes.
Calvin Jon A Leonen   +12 more
doaj   +1 more source

Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity. [PDF]

open access: yesPLoS ONE, 2012
Increasing evidence has pointed to an important role of SUMOylation in cell cycle regulation, especially for M phase. In the current studies, we have obtained evidence through in vitro studies that the master M phase regulator CDK1/cyclin B kinase ...
Yee-Fun Su   +4 more
doaj   +1 more source

Regulation of Smoothened Trafficking and Abundance in Hedgehog Signaling

open access: yesFrontiers in Cell and Developmental Biology, 2022
The GPCR-family protein Smoothened (Smo) is essential for Hedgehog (Hh) signal transduction in both insects and vertebrates. The regulation of subcellular localization and abundance of Smo is a critical step in Hh signaling.
Jianhang Jia, Jin Jiang
doaj   +1 more source

Analysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection. [PDF]

open access: yesPLoS ONE, 2014
Post-translational modification of proteins by members of the small ubiquitin-like modifier (SUMO) is involved in diverse cellular functions. Many viral proteins are SUMO targets and also interact with the cellular SUMOylation system.
Eui Tae Kim   +5 more
doaj   +1 more source

SUMOylation controls the neurodevelopmental function of the transcription factor Zbtb20. [PDF]

open access: yes, 2020
SUMOylation is a dynamic post-translational protein modification that primarily takes place in cell nuclei, where it plays a key role in multiple DNA-related processes.
Hellmann, Klaus Peter   +27 more
core   +1 more source

SUMOylation pathway alteration coupled with downregulation of SUMO E2 enzyme at mucosal epithelium modulates inflammation in inflammatory bowel disease [PDF]

open access: yesOpen Biology, 2017
Post-translational modification pathways such as SUMOylation are integral to all cellular processes and tissue homeostasis. We investigated the possible involvement of SUMOylation in the epithelial signalling in Crohn's disease (CD) and ulcerative ...
Salman Ahmad Mustfa   +11 more
doaj   +1 more source

The E3 Ligase PIAS1 Regulates p53 Sumoylation to Control Stress-Induced Apoptosis of Lens Epithelial Cells Through the Proapoptotic Regulator Bax

open access: yesFrontiers in Cell and Developmental Biology, 2021
Protein sumoylation is one of the most important post-translational modifications regulating many biological processes (Flotho A & Melchior F. 2013. Ann Rev. Biochem. 82:357–85).
Qian Nie   +21 more
doaj   +1 more source

Protein SUMOylation regulates insulin secretion at multiple stages [PDF]

open access: yes, 2019
Type-II Diabetes Mellitus (T2DM) is one of the fastest growing public health issues of modern times, consuming 12% of worldwide health budgets and affecting an estimated 400 million people.
Davey, Jeffrey S.   +2 more
core   +1 more source

A role for SUMO modification in transcriptional repression and activation [PDF]

open access: yes, 2007
Since the discovery of the SUMO (small ubiquitin-related modifier) family of proteins just over a decade ago, a plethora of substrates have been uncovered including many regulators of transcription.
Lyst, M J, Stancheva, I
core   +1 more source

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