Results 271 to 280 of about 62,421 (311)

Manipulation of nonclassical ubiquitin signaling by pathogenic bacteria. [PDF]

Curr Opin Microbiol
Kaur Sidhu J, Kubori T, Pruneda JN.
europepmc   +1 more source

K63-linked ubiquitylation of S2P-RNAPII regulates transcription in a DNAPK inter-dependent manner in response to double-strand breaks. [PDF]

Nucleic Acids Res
Pantazi V, Smith P, Pahi ZG, Katona M, Pap A, Darula Z, Fischer R, Vendrell I, Kessler BM, van Vugt MATM, D'Angiolella V, Pankotai T.   +11 more
europepmc   +1 more source

Targeted proteoform degradation for precision drug design, delivery, and therapy. [PDF]

Drug Deliv
Cui C, Zhang H, Wang X, Li N, Zhan X.
europepmc   +1 more source

Turnover of missense mutant cytosolic proteins proceeds in the absence of major quality control E3 ligases. [PDF]

MicroPubl Biol
Baker HA, Grall-Johnson C, Budzyńska PM, Kim J, Mayor T.   +4 more
europepmc   +1 more source

Ubiquitin E3 ligase KLHL6 brings exhausted T-cells back into action. [PDF]

Immun Inflamm
Chen Z, Bullock AN, Kessler BM.
europepmc   +1 more source

The modifier matrix: emerging roles of ubiquitin-like proteins in Alzheimer's disease. [PDF]

Mol Neurodegener Adv
Yan T, Vaquer J, Springer W, Fiesel FC.
europepmc   +1 more source

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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, Hannah J, Kim, Stewart H, Lecker   +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

Essential Roles of E3 Ubiquitin Ligases in p53 Regulation [PDF]

International Journal of Molecular Sciences, 2017
The ubiquitination pathway and proteasomal degradation machinery dominantly regulate p53 tumor suppressor protein stability, localization, and functions in both normal and cancerous cells. Selective E3 ubiquitin ligases dominantly regulate protein levels
Khosrow Rezvani, Sanam Sane, Rezvani Khosrow   +2 more
exaly   +2 more sources