Results 21 to 30 of about 1,958,325 (325)

Structural basis for the human SENP5’s SUMO isoform discrimination [PDF]

open access: yesNature Communications
Post-translational SUMO modification is a widespread mechanism for regulating protein function within cells. In humans, SUMO-conjugated proteins are partially regulated by the deconjugating activity of six SENP family members. The proteolytic activity of
Lucía Sánchez-Alba   +9 more
doaj   +2 more sources

Host SUMOylation in bacterial infections and immune defense mechanisms [PDF]

open access: yesFrontiers in Microbiology
SUMOylation, the covalent attachment of small ubiquitin-like modifier proteins (SUMO) to lysine residues of target substrates, has emerged as a crucial post-translational modification regulating various cellular processes.
Yuhua Xu   +11 more
doaj   +2 more sources

HPV E6 proteins target Ubc9, the SUMO conjugating enzyme [PDF]

open access: greenVirus Research, 2011
The human papillomavirus oncogenic protein, E6, interacts with a number of cellular proteins, and for some targets, E6 directs their degradation through the ubiquitin-proteasome pathway. Post-translational modification with ubiquitin-like modifiers, such as SUMO, also influences protein activities, protein-protein interactions, and protein stability ...
Phillip Heaton   +3 more
openalex   +4 more sources

Characterization of SUMO-conjugating enzyme mutants in Schizosaccharomyces pombe identifies a dominant-negative allele that severely reduces SUMO conjugation [PDF]

open access: greenBiochemical Journal, 2003
The phenotypes of mutants defective in the Schizosaccharomyces pombe SUMO (small, ubiquitin-like modifier)-conjugating enzyme Hus5 (the homologue of Ubc9) show that it is required for recovery from S-phase arrest. Unlike the case with ubiquitination, where ligases are required, SUMO-conjugating enzymes are sufficient for substrate recognition and ...
Jenny Ho, Felicity Z. Watts
openalex   +4 more sources

SUMO-Conjugating and SUMO-Deconjugating Enzymes from Arabidopsis1 [PDF]

open access: yesPlant Physiology, 2006
Abstract Posttranslational protein modification by the small ubiquitin-like modifier (SUMO) is a highly dynamic and reversible process. To analyze the substrate specificity of SUMO-conjugating and -deconjugating enzymes from Arabidopsis (Arabidopsis thaliana), we reconstituted its SUMOylation cascade in vitro and tested the capacity of ...
T. Colby   +3 more
semanticscholar   +5 more sources

Protein SUMOylation and Its Research Progress in Maize

open access: yesGuangdong nongye kexue, 2023
Small ubiquitin-like modification (SUMOylation) is a crucial post-translational modification of proteins that plays a vital role in various biological processes in plants.
Ruiqiang LAI   +5 more
doaj   +1 more source

Diversification of SUMO-Activating Enzyme in Arabidopsis: Implications in SUMO Conjugation [PDF]

open access: yesMolecular Plant, 2013
Sumoylation is an essential posttranslational modification that participates in many biological processes including stress responses. However, little is known about the mechanisms that control Small Ubiquitin-like MOdifier (SUMO) conjugation in vivo. We have evaluated the regulatory role of the heterodimeric E1 activating enzyme, which catalyzes the ...
L. Castano-Miquel   +6 more
openaire   +4 more sources

Negative Regulation of TLR Inflammatory Signaling by the SUMO-deconjugating Enzyme SENP6

open access: goldPLoS Pathogens, 2013
The signaling of Toll-like receptors (TLRs) induces host defense against microbial invasion. Protein posttranslational modifications dynamically shape the strength and duration of the signaling pathways. It is intriguing to explore whether de-SUMOylation could modulate the TLR signaling.
Xing Liu   +4 more
openalex   +6 more sources

Disruption of SUMO-specific protease 2 induces mitochondria mediated neurodegeneration. [PDF]

open access: yesPLoS Genetics, 2014
Post-translational modification of proteins by small ubiquitin-related modifier (SUMO) is reversible and highly evolutionarily conserved from yeasts to humans.
Jiang Fu   +6 more
doaj   +1 more source

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