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Screening ubiquitin specific protease activities using chemically synthesized ubiquitin and ubiquitinated peptides

Analytical Biochemistry, 2017
Ubiquitin, a 76 amino acid protein, is a key component that contributes to cellular protein homeostasis. The specificity of this modification is due to a series of enzymes: ligases, attaching the ubiquitin to a lysine, and deubiquitinases, which remove it. More than a hundred of such proteins are implicated in the regulation of protein turnover.
Marine, Bacchi   +9 more
openaire   +2 more sources

[Progress in ubiquitin, ubiquitin chain and protein ubiquitination].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2016
Protein ubiquitination is one of the most important and widely exist protein post-translational modifications in eukaryotic cells, which takes the ubiquitin and ubiquitin chains as signal molecules to covalently modify other protein substrates. It plays an important roles in the control of almost all of the life processes, including gene transcription ...
Qiuyan, Lan   +4 more
openaire   +1 more source

When ubiquitin meets ubiquitin receptors: a signalling connection

Nature Reviews Molecular Cell Biology, 2003
Ubiquitylation is emerging as a versatile device for controlling cellular functions. Here, we propose that monoubiquitylation is rapidly induced by signalling events and allows the establishment of protein-protein interactions between monoubiquitylated proteins and partners that contain distinct ubiquitin-binding domains.
P.P. Di Fiore, S. Polo, K. Hofmann
openaire   +3 more sources

Monitoring MHC Ubiquitination by MARCH Ubiquitin Ligases

2019
Ubiquitination is a reversible process that controls the intracellular transport of many transmembrane molecules. Ubiquitination of MHC I, MHC II, and CD1a by different members of the MARCH family of E3 ubiquitin ligases is a key event in the regulation of the potent immunostimulatory properties of activated dendritic cells. We describe here methods to
openaire   +2 more sources

Principles of Ubiquitin-Dependent Signaling.

Annual Review of Cell and Developmental Biology, 2018
Ubiquitylation is an essential posttranslational modification that controls cell division, differentiation, and survival in all eukaryotes. By combining multiple E3 ligases (writers), ubiquitin-binding effectors (readers), and de-ubiquitylases (erasers ...
E. Oh, D. Akopian, M. Rapé
semanticscholar   +1 more source

Ubiquitination

Annual Review of Cell Biology, 1991
D, Finley, V, Chau
openaire   +2 more sources

The ubiquitin code.

Annual Review of Biochemistry, 2012
D. Komander, M. Rapé
semanticscholar   +1 more source

The ubiquitin system

Nature Medicine, 2000
A. Hershko   +2 more
semanticscholar   +1 more source

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO

Nature, 2002
C. Hoege   +4 more
semanticscholar   +1 more source

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