Results 1 to 10 of about 12,253 (229)
Sumoylation in Physiology, Pathology and Therapy
Cells, 2022 Sumoylation is an essential post-translational modification that has evolved to regulate intricate networks within emerging complexities of eukaryotic cells.
Umut Sahin +2 more
doaj +2 more sources
SUMOylation modification-mediated cell death
Open Biology, 2021 SUMOylation dynamically conjugates SUMO molecules to the lysine residue of a substrate protein, which depends on the physiological state of the cell and the attached SUMO isoforms.
Zenghua Sheng +4 more
doaj +2 more sources
SUMOylation and De-SUMOylation: Wrestling with Life's Processes [PDF]
Journal of Biological Chemistry, 2008 The small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large number of cellular proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and
Edward T.H. Yeh
openalex +4 more sources
SUMOylation in development and neurodegeneration [PDF]
Development, 2020 In essentially all eukaryotes, proteins can be modified by the attachment of small ubiquitin-related modifier (SUMO) proteins to lysine side chains to produce branched proteins.
T. Yau, Oscar Molina, A. Courey
semanticscholar +4 more sources
Histone sumoylation and chromatin dynamics
Nucleic Acids Research, 2021 Chromatin structure and gene expression are dynamically controlled by post-translational modifications (PTMs) on histone proteins, including ubiquitylation, methylation, acetylation and small ubiquitin-like modifier (SUMO) conjugation.
Hong-Yeoul Ryu, M. Hochstrasser
semanticscholar +3 more sources
The Role of Sumoylation in the Response to Hypoxia: An Overview
Cells, 2020 Sumoylation is the covalent attachment of the small ubiquitin-related modifier (SUMO) to a vast variety of proteins in order to modulate their function. Sumoylation has emerged as an important modification with a regulatory role in the cellular response ...
Chrysa Filippopoulou +2 more
doaj +2 more sources
Human polycomb 2 protein is a SUMO E3 ligase and alleviates substrate-induced inhibition of cystathionine beta-synthase sumoylation. [PDF]
PLoS ONE, 2008 Human cystathionine beta-synthase (CBS) catalyzes the first irreversible step in the transsulfuration pathway and commits homocysteine to the synthesis of cysteine. Mutations in CBS are the most common cause of severe hereditary hyperhomocysteinemia.
Nitish Agrawal, Ruma Banerjee
doaj +3 more sources
RECENT ADVANCES IN POST-TRANSLATIONAL REGULATION OF PLANT DEFENSE RESPONSES BEYOND PHOSPHORYLATION [PDF]
Journal of Plant Development, 2021 During plant-microbe interactions, plant immune signaling relies significantly on post-translational modifications (PTMs) to induce rapid downstream changes.
Tim XING, Ziwei GUO
doaj +1 more source
Frontiers in Cellular and Infection Microbiology, 2022 SUMOylation is one of the post-translational modifications that have recently been described as a key regulator of various cellular, nuclear, metabolic, and immunological processes.
Jhalak Singhal +11 more
doaj +1 more source
Cell Death and Disease, 2023 Glioma is the most common malignant tumor of the central nervous system in adults. The tumor microenvironment (TME) is related to poor prognosis in glioma patients. Glioma cells could sort miRNA into exosomes to modify TME.
Q. Guo +24 more
semanticscholar +1 more source