Results 21 to 30 of about 129,362 (255)

Cullin-RING Ubiquitin Ligases in Neurodevelopment and Neurodevelopmental Disorders. [PDF]

Biomedicines
Ubiquitination is a dynamic and tightly regulated post-translational modification essential for modulating protein stability, trafficking, and function to preserve cellular homeostasis.
Ashitomi H, Nakagawa T, Nakagawa M, Hosoi T.   +3 more
europepmc   +2 more sources

Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity

Biomolecules, 2022
In recent years, researchers have leveraged the ubiquitin-proteasome system (UPS) to induce selective degradation of proteins by E3 ubiquitin ligases, which has great potential as novel therapeutics for human diseases, including cancer and ...
Bayonle Aminu, Julia Fux, Evan Mallette, Nathaniel Petersen, Wei Zhang   +4 more
doaj   +1 more source

From Drosophila to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease

Cells, 2022
The ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes.
Valérie C. Cabana, Marc P. Lussier
doaj   +1 more source

UBE3A (ubiquitin protein ligase E3A) [PDF]

Atlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on UBE3A (ubiquitin protein ligase E3A), with data on DNA, on the protein encoded, and where the gene is implicated.
Matentzoglu, K, Scheffner, M
openaire   +3 more sources

Functional Domains of the Rsp5 Ubiquitin-Protein Ligase [PDF]

Molecular and Cellular Biology, 1999
RSP5, an essential gene of Saccharomyces cerevisiae, encodes a hect domain E3 ubiquitin-protein ligase. Hect E3 proteins have been proposed to consist of two broad functional domains: a conserved catalytic carboxyl-terminal domain of approximately 350 amino acids (the hect domain) and a large, nonconserved amino-terminal domain containing determinants ...
Joyce C. Yang, Guangli Wang, Jon M. Huibregtse   +2 more
openaire   +3 more sources

How to Inactivate Human Ubiquitin E3 Ligases by Mutation

Frontiers in Cell and Developmental Biology, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Cristina Garcia-Barcena, Nerea Osinalde, Juanma Ramirez, Ugo Mayor, Ugo Mayor   +4 more
doaj   +1 more source

The Biological Function and Roles in Phytohormone Signaling of the F-Box Protein in Plants

Agronomy, 2021
The ubiquitin–proteasome pathway (UPP) is an important protein degradation pathway that can participate in the regulation of the physiological process of organisms by specifically removing abnormal peptides and degrading cell regulators.
Keheng Xu, Nan Wu, Wenbo Yao, Xiaowei Li, Yonggang Zhou, Haiyan Li   +5 more
doaj   +1 more source

Structural insights into the catalysis and regulation of E3 ubiquitin ligases

Nature Reviews Molecular Cell Biology, 2016
Lori Buetow, Danny T Huang
exaly   +2 more sources

The ubiquitin–protein ligase Itch regulates p73 stability [PDF]

The EMBO Journal, 2005
p73, a member of the p53 family of transcription factors, is upregulated in response to DNA damage, inducing cell cycle arrest and apoptosis. Besides indications that this p73 response is post-transcriptional, little is known about the underlying molecular mechanisms of p73 protein degradation.
Gianni Cesareni, Eliana Munarriz, Karen H. Vousden, Douglas R. Green, Gerry Melino, Gerry Melino, Yun Cai Liu, Mario Rossi, Mario Rossi, Vincenzo De Laurenzi, Vincenzo De Laurenzi   +10 more
openaire   +3 more sources

E3 Ubiquitin Ligases as Cancer Targets and Biomarkers

Neoplasia: 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