Results 271 to 280 of about 596,162 (342)

ASB9 promotes ubiquitin-mediated degradation of TNP2 to facilitate histone-to-protamine transition in humans and mice. [PDF]

open access: yesProc Natl Acad Sci U S A
Zhao S   +16 more
europepmc   +1 more source

Ubiquitin-specific peptidase-19 links TDP-43 aggregation to ER stress. [PDF]

open access: yesProc Natl Acad Sci U S A
Yan Y   +10 more
europepmc   +1 more source
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Building and decoding ubiquitin chains for mitophagy

Nature Reviews Molecular Cell Biology, 2018
Jeffrey W Harper   +2 more
exaly   +2 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

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.
J, Jahngen-Hodge   +3 more
openaire   +2 more sources

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.
E G, Mimnaugh, P, Bonvini, L, Neckers
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   +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

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