Results 11 to 20 of about 299,473 (288)

Identification of proximal SUMO-dependent interactors using SUMO-ID [PDF]

open access: yesNature Communications, 2020
The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment ...
Orhi Barroso-Gomila   +15 more
semanticscholar   +7 more sources

SUMO targeting of a stress-tolerant Ulp1 SUMO protease. [PDF]

open access: yesPLoS ONE, 2018
SUMO proteases of the SENP/Ulp family are master regulators of both sumoylation and desumoylation and regulate SUMO homeostasis in eukaryotic cells. SUMO conjugates rapidly increase in response to cellular stress, including nutrient starvation, hypoxia ...
Jennifer Peek   +8 more
doaj   +4 more sources

Site-specific identification and quantitation of endogenous SUMO modifications under native conditions. [PDF]

open access: yesNature Communications, 2017
Small ubiquitin-like modifier (SUMO) modification regulates numerous cellular processes. Unlike ubiquitin, detection of endogenous SUMOylated proteins is limited by the lack of naturally occurring protease sites in the C-terminal tail of SUMO proteins ...
Ahmad, Alla S   +8 more
core   +3 more sources

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

open access: yesJournal 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
S. Langston   +52 more
semanticscholar   +1 more source

SUMO Interacting Motifs: Structure and Function

open access: yesCells, 2021
Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-related protein family. SUMO modulates protein function through covalent conjugation to lysine residues in a large number of proteins.
T. Yau   +3 more
semanticscholar   +1 more source

Global non-covalent SUMO interaction networks reveal SUMO-dependent stabilization of the non-homologous end joining complex.

open access: yesCell Reports, 2021
In contrast to our extensive knowledge on covalent small ubiquitin-like modifier (SUMO) target proteins, we are limited in our understanding of non-covalent SUMO-binding proteins.
R. González-Prieto   +8 more
semanticscholar   +1 more source

Mechanism and function of DNA replication‐independent DNA‐protein crosslink repair via the SUMO‐RNF4 pathway

open access: yesEMBO Journal, 2021
DNA‐protein crosslinks (DPCs) obstruct essential DNA transactions, posing a serious threat to genome stability and functionality. DPCs are proteolytically processed in a ubiquitin‐ and DNA replication‐dependent manner by SPRTN and the proteasome but can ...
Julio C Y Liu   +15 more
semanticscholar   +1 more source

SUMO is a pervasive regulator of meiosis

open access: yeseLife, 2021
Protein modification by SUMO helps orchestrate the elaborate events of meiosis to faithfully produce haploid gametes. To date, only a handful of meiotic SUMO targets have been identified.
Nikhil R Bhagwat   +12 more
semanticscholar   +1 more source

Therapeutic Potential of Targeting the SUMO Pathway in Cancer

open access: yesCancers, 2021
Simple Summary The small ubiquitin-like modifier (SUMO) pathway regulates the hallmark properties of cancer cells. Moreover, alterations in activity and in levels of SUMO machinery components have been observed in human cancer.
Antti Kukkula   +5 more
semanticscholar   +1 more source

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