Results 251 to 260 of about 230,401 (303)

CBL ubiquitin ligase targets translation as a degrader E3. [PDF]

Chem Sci
Wicks AT, Buetow L, Suzuki T, Schmidt T, Lilla S, Macmillan-Jones A, Turney J, Gohlke A, Bushell M, Hock AK, Huang DT.   +10 more
europepmc   +1 more source

The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation

Farnung J, Slobodyanyuk E, Wang PY, Blodgett LW, Lin DH, von Gronau S, Schulman BA, Bartel DP.   +7 more
europepmc   +1 more source

Molecular determinants underlying substrate receptor specificity of human CRL4B E3 ubiquitin ligase

Mohamed WI, Rabl J, Qureshi BM, Leitner A, Uliana F, Kazemzadeh A, Radwan N, Peter M.   +7 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

A giant ubiquitin ligase

Nature Chemical Biology, 2021
The structure of a giant ubiquitin E3 ligase sheds light on its activation in a substrate-dependent manner and shows how a single E3 enzyme uses distinct recognition modules to confer substrate specificity.
openaire   +2 more sources

On ubiquitin ligases and cancer

Human Mutation, 2005
Protein kinase genes account for almost 10% of all currently known cancer genes, highlighting the role of signal transduction in oncogenesis. A reexamination of the literature and available databases shows that E3 ubiquitin ligases are also key mediators of tumorigenesis. Altogether kinase and E3 genes represent more than 15% of the known cancer genes,
Beckmann JS, Maurer F, Delorenzi M, Falquet L   +3 more
openaire   +3 more sources

E3 ubiquitin ligases

Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
openaire   +2 more sources

Ubiquitin Ligases in Malignant Lymphoma

Leukemia & Lymphoma, 2004
The highly controlled degradation of proteins via the ubiquitin-proteasome pathway represents a key mechanism for cell regulation and homeostasis. Ubiquitin-dependent proteolysis, carried out in large part by the E3 ubiquitin ligases, is a critical mode of post-translational modification that is important in regulation of cell cycle progression, signal
Megan S, Lim, Kojo S J, Elenitoba-Johnson   +1 more
openaire   +2 more sources

Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase

Science, 2005
Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the ...
Ken, Cadwell, Laurent, Coscoy
openaire   +2 more sources

RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination

Biochemical and Biophysical Research Communications, 2010
Modification of proteins by ubiquitination plays important roles in various cellular processes. During this process, the target specificity is determined by ubiquitin ligases. Here we identify RNF220 (RING finger protein 220) as a novel ubiquitin ligase for Sin3B. As a conserved RING protein, RNF220 can bind E2 and mediate auto-ubiquitination of itself.
Qinghua, Kong, Wanli, Zeng, Jingyang, Wu, Wanling, Hu, Chaocui, Li, Bingyu, Mao   +5 more
openaire   +2 more sources

Ubiquitin Ligases and the Immune Response

Annual Review of Immunology, 2004
Ubiquitin (Ub)-protein conjugation represents a novel means of posttranscriptional modification in a proteolysis-dependent or -independent manner. E3 Ub ligases play a key role in governing the cascade of Ub transfer reactions by recognizing and catalyzing Ub conjugation to specific protein substrates.
openaire   +2 more sources