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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.
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Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins [PDF]

open access: possibleAnnual Review of Cell and Developmental Biology, 2006
Following the discovery of protein modification by the small, highly conserved ubiquitin polypeptide, a number of distinct ubiquitin-like proteins (Ubls) have been found to function as protein modifiers as well. These Ubls, which include SUMO, ISG15, Nedd8, and Atg8, function as critical regulators of many cellular processes, including transcription ...
Oliver Kerscher   +2 more
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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

The ubiquitin system

Trends in Biochemical Sciences, 1997
Eukaryotes contain a highly conserved multi-enzyme system that covalently links ubiquitin to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, a large ATP-dependent protease.
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Ubiquitin and Ubiquitin-like Modifiers in Plants

Journal of Plant Biology, 2011
Posttranslational modifications of proteins by small polypeptides including ubiquitination, neddylation (related to ubiquitin (RUB) conjugation), and sumoylation are implicated in plant growth and development, and they regulate protein degradation, location, and interaction with other proteins.
Hans J. Bohnert   +5 more
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Is This Protein Ubiquitinated?

2005
Covalent modification of proteins with ubiquitin plays an important role in a wide array of cellular processes (Hershko and Ciechanover, 1998; Pickart, 2004). For this reason an increasing number of investigators in diverse research fields are confronted with the question whether their favorite proteins are ubiquitinated.
Christian Tagwerker, Peter K. Kaiser
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Ubiquitination

Annual Review of Cell and Developmental Biology, 1991
D, Finley, V, Chau
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Targeting the monocytic ubiquitin system with extracellular ubiquitin

Immunology & Cell Biology, 2006
Recent findings suggest that extracellular ubiquitin has pleiotropic effects on host defence mechanisms, but its cellular mechanism of action is not yet understood. Using fluorescence and in vivo confocal microscopy, we observed uptake of N‐terminal fluorescein‐labelled ubiquitin into human PBMC and MonoMac 6 cells. Immunoblotting experiments indicated
Thomas Hirsch   +2 more
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