Results 271 to 280 of about 3,429,300 (308)

Ubiquitin-Protein Ligases - Novel Therapeutic Targets?

Current Protein and Peptide Science, 2004
Intracellular protein degradation is a tightly regulated process that in many cases is controlled by protein ubiquitylation. The ubiquitin pathway is a major route by which cells not only remove normal proteins at the appropriate time but also abnormally folded normal or mutant, cytoplasmic and membrane, proteins.
Philip A Robinson
exaly   +3 more sources

Ubiquitin–protein ligases in muscle wasting

The International Journal of Biochemistry & Cell Biology, 2005
Muscle wasting occurs when rates of protein degradation outstrip rates of protein synthesis. Accelerated rates of protein degradation develop in atrophying muscle largely through activation of the ubiquitin-proteasome pathway. The complexity of the ubiquitination process, however, has hampered our understanding of how this pathway is activated in ...
Pei Rang, Cao   +2 more
openaire   +2 more sources

The Cullin-RING Ubiquitin-Protein Ligases

Annual Review of Plant Biology, 2011
The posttranslational addition of ubiquitin (Ub) helps control the half-life, localization, and action of many intracellular plant proteins. A primary function is the degradation of ubiquitylated proteins by the 26S proteasome, which in turn plays important housekeeping and regulatory roles by removing aberrant polypeptides and various normal short ...
Zhihua, Hua, Richard D, Vierstra
openaire   +2 more sources

Death of a Protein: The Role of E3 Ubiquitin Ligases in Circadian Rhythms of Mice and Flies

International Journal of Molecular Sciences, 2022
Hai-Ying Mary Cheng   +1 more
exaly  

Roles of Cullin-RING Ubiquitin Ligases in Cardiovascular Diseases

Biomolecules, 2022
Stephanie Diaz, Kankan Wang
exaly  

Ubiquitin-protein ligase E3A

Targeted Protein Database, 2007
openaire   +1 more source

The role of E3 ubiquitin ligases in the development and progression of glioblastoma

Cell Death and Differentiation, 2021
Vincenzo D'Angiolella   +2 more
exaly  

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