Results 371 to 380 of about 280,422 (406)

Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity.

Annual Review of Immunology, 2000
NF-kappaB (nuclear factor-kappaB) is a collective name for inducible dimeric transcription factors composed of members of the Rel family of DNA-binding proteins that recognize a common sequence motif.
Michael Karin, Y. Ben-Neriah
semanticscholar   +1 more source

Mechanisms underlying ubiquitination.

Annual Review of Biochemistry, 2001
The conjugation of ubiquitin to other cellular proteins regulates a broad range of eukaryotic cell functions. The high efficiency and exquisite selectivity of ubiquitination reactions reflect the properties of enzymes known as ubiquitin-protein ligases ...
C. Pickart
semanticscholar   +1 more source

The measurement of ubiquitin and ubiquitinated proteins

Electrophoresis, 1999
Ubiquitination of key cellular proteins involved in signal transduction, gene transcription and cell-cycle regulation usually condemns those proteins to proteasomal or lysosomal degradation. Additionally, cycles of reversible ubiquitination regulate the function of certain proteins in a manner analogous to phosphorylation.
Len Neckers, P. Bonvini, Edward G. Mimnaugh   +2 more
openaire   +3 more sources

THE UBIQUITIN SYSTEM [PDF]

Annual Review of Biochemistry, 1998
The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes ...
Aaron Ciechanover, Avram Hershko
openaire   +2 more sources

Ubiquitin and ubiquitin conjugates in human lens

Experimental Eye Research, 1992
Ubiquitin, an 8.5 kDa polypeptide found almost universally in plants and animals, is a normal component in the lens. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation. Conjugates for ubiquitin-dependent degradation tend to be of very high molecular mass and are rapidly degraded.
Deanna E. Cyr, Allen Taylor, Eric Laxman, Jessica Jahngen-Hodge   +3 more
openaire   +3 more sources

Activation of Ubiquitin and Ubiquitin-Like Proteins

2010
Attachment of ubiquitin and ubiquitin-like proteins to cellular targets represents a fundamental regulatory strategy within eukaryotes and exhibits remarkably pleiotropic effects on cell function. These posttranslational modifications share a common mechanism comprised of three steps: an activating enzyme to couple ATP hydrolysis to formation of a high-
Frederick C. Streich, Arthur L. Haas
openaire   +2 more sources

In Vitro Ubiquitination: Self-Ubiquitination, Chain Formation, and Substrate Ubiquitination Assays

2016
Ubiquitination of proteins in vitro has evolved as an indispensable tool for the functional analysis of this posttranslational modification. In vitro ubiquitination is particularly helpful to study conjugation mechanisms. The efficiency of the ubiquitination reaction depends in part on the quality of the enzymes utilized.
E. Maspero, S. Polo
openaire   +4 more sources

Ubiquitin and the synapse

Nature Reviews Neuroscience, 2002
Post-translational modification by the attachment of ubiquitin seems to have a crucial role in regulating synaptic structure and function. By controlling the stability, activity and localization of target proteins, this versatile regulatory system can shape the pattern, activity and plasticity of synaptic connections.
Ashok N. Hegde, Aaron DiAntonio
openaire   +3 more sources

One Ubiquitin, Two Ubiquitin, Three Ubiquitin, Four

Science's STKE, 2007
The role of protein ubiquitination is well known in promoting regulated protein degradation. Mukhopadhyay and Riezman review what is known about the contribution of protein ubiquitination in other cellular pathways, including intracellular signaling, endocytosis, and protein sorting. D. Mukhopadhyay, H.
openaire   +2 more sources