Results 21 to 30 of about 47,588 (257)

AIRE Functions As an E3 Ubiquitin Ligase [PDF]

open access: yesThe Journal of Experimental Medicine, 2004
Autoimmune regulator (AIRE) gene mutation is responsible for the development of autoimmune-polyendocrinopathy-candidiasis ectodermal dystrophy, an organ-specific autoimmune disease with monogenic autosomal recessive inheritance. AIRE is predominantly expressed in medullary epithelial cells of the thymus and is considered to play important roles in the ...
Uchida, Daisuke   +11 more
openaire   +2 more sources

WWP2 is an E3 ubiquitin ligase for PTEN [PDF]

open access: yesNature Cell Biology, 2011
PTEN, a lipid phosphatase, is one of the most frequently mutated tumour suppressors in human cancer. Several recent studies have highlighted the importance of ubiquitylation in regulating PTEN tumour-suppressor function, but the enzymatic machinery required for PTEN ubiquitylation is not clear.
Subbareddy, Maddika   +6 more
openaire   +2 more sources

RING Domain E3 Ubiquitin Ligases

open access: yesAnnual Review of Biochemistry, 2009
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J.   +1 more
openaire   +3 more sources

E3 Ubiquitin Ligases as Cancer Targets and Biomarkers

open access: yesNeoplasia: An International Journal for Oncology Research, 2006
E3 ubiquitin ligases are a large family of proteins that are engaged in the regulation of the turnover and activity of many target proteins. Together with ubiquitinactivating enzyme El and ubiquitin-conjugating enzyme E2, E3 ubiquitin ligases catalyze ...
Yi Sun
doaj   +1 more source

TRIM32 is an E3 ubiquitin ligase for dysbindin [PDF]

open access: yesHuman Molecular Genetics, 2009
Mutations in the gene encoding tripartite motif protein 32 (TRIM32) cause two seemingly diverse diseases: limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11(BBS11). Although TRIM32 is involved in protein ubiquitination, its substrates and the molecular consequences of disease-causing ...
Locke, Matthew   +3 more
openaire   +3 more sources

The roles of E3 ubiquitin ligases in cancer progression and targeted therapy

open access: yesClinical and Translational Medicine, 2023
Ubiquitination is one of the most important post‐translational modifications which plays a significant role in conserving the homeostasis of cellular proteins.
Chibuzo Sampson   +6 more
doaj   +1 more source

E3 ubiquitin ligases in the acute leukemic signaling pathways

open access: yesFrontiers in Physiology, 2022
Acute leukemia is a common hematologic tumor with highly genetic heterogeneity, and many factors are involved in the pathogenesis and drug-resistance mechanism.
Qianru Zhan   +4 more
doaj   +1 more source

Research Progress on the Role of E3 Ubiquitin Ligases in Regulating the Growth, Development and Stress Response of Fruits and Vegetables [PDF]

open access: yesShipin Kexue
Protein ubiquitination, an important post-translational modification, plays a wide role in the life activities of eukaryotic cells. E3 ubiquitin ligases specifically recognize target proteins in the ubiquitin-proteasome degradation system and play a ...
DING Jun, LI Fujun, LI Xiao’an, ZHANG Xinhua
doaj   +1 more source

Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum

open access: yesScientific Reports, 2021
The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein.
Bhaskar Sharma   +2 more
doaj   +1 more source

Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]

open access: yesPLoS ONE, 2013
The ubiquitin-signaling pathway utilizes E1 activating, E2 conjugating, and E3 ligase enzymes to sequentially transfer the small modifier protein ubiquitin to a substrate protein.
Donald E Spratt   +2 more
doaj   +1 more source

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