Results 1 to 10 of about 1,958,216 (236)

SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease

open access: yesFrontiers in Molecular Biosciences, 2021
SUMOylation is a transient posttranslational modification with small-ubiquitin like modifiers (SUMO1, SUMO2 and SUMO3) covalently attached to their target-proteins via a multi-step enzymatic cascade.
Paul W. Hotz   +2 more
doaj   +2 more sources

Discovery of TAK-981, a First-in-Class Inhibitor of SUMO-Activating Enzyme for the Treatment of Cancer

open access: hybridJournal of Medicinal Chemistry, 2021
SUMOylation is a reversible post-translational modification that regulates protein function through covalent attachment of small ubiquitin-like modifier (SUMO) proteins. The process of SUMOylating proteins involves an enzymatic cascade, the first step of
Steven Langston   +52 more
openalex   +2 more sources

Super-resolution study of PIAS SUMO E3-ligases in hippocampal and cortical neurons

open access: yesEuropean Journal of Histochemistry, 2021
The SUMOylation machinery is a regulator of neuronal activity and synaptic plasticity. It is composed of SUMO isoforms and specialized enzymes named E1, E2 and E3 SUMO ligases.
Andrea Conz   +4 more
doaj   +2 more sources

Site-Specific Protein Ubiquitylation Using an Engineered, Chimeric E1 Activating Enzyme and E2 SUMO Conjugating Enzyme Ubc9 [PDF]

open access: diamondACS Central Science, 2022
Ubiquitylation—the attachment of ubiquitin (Ub) to proteins in eukaryotic cells—involves a vast number of enzymes from three different classes, resulting in heterogeneous attachment sites and ubiquitin chains.
Gaku Akimoto   +2 more
openalex   +2 more sources

SUMO conjugation – a mechanistic view

open access: yesBiomolecular Concepts, 2017
The regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways.
Pichler Andrea   +3 more
doaj   +2 more sources

Chemical Synthesis of Atomically Tailored SUMO E2 Conjugating Enzymes for the Formation of Covalently Linked SUMO–E2–E3 Ligase Ternary Complexes [PDF]

open access: greenJournal of the American Chemical Society, 2019
E2 conjugating enzymes are the key catalytic actors in the transfer of ubiquitin, SUMO, and other ubiquitin-like modifiers to their substrate proteins.
Yinfeng Zhang   +5 more
openalex   +2 more sources

A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation. [PDF]

open access: yesPLoS ONE, 2015
A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed by E1, E2, and E3 enzymes.
Claudio P Albuquerque   +5 more
doaj   +12 more sources

Not So Slim Anymore—Evidence for the Role of SUMO in the Regulation of Lipid Metabolism

open access: yesBiomolecules, 2020
One of the basic building blocks of all life forms are lipids—biomolecules that dissolve in nonpolar organic solvents but not in water. Lipids have numerous structural, metabolic, and regulative functions in health and disease; thus, complex networks of ...
Amir Sapir
doaj   +2 more sources

Functional expression of diverse post-translational peptide-modifying enzymes in Escherichia coli under uniform expression and purification conditions

open access: yesPLoS ONE, 2022
RiPPs (ribosomally-synthesized and post-translationally modified peptides) are a class of pharmaceutically-relevant natural products expressed as precursor peptides before being enzymatically processed into their final functional forms.
Emerson Glassey   +4 more
doaj   +3 more sources

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