Results 1 to 10 of about 28,143 (190)

Computational identification of ubiquitylation sites from protein sequences [PDF]

open access: yesBMC Bioinformatics, 2008
Background Ubiquitylation plays an important role in regulating protein functions. Recently, experimental methods were developed toward effective identification of ubiquitylation sites.
Ho Shinn-Ying, Tung Chun-Wei
doaj   +2 more sources

Remodeling Membrane Binding by Mono-Ubiquitylation

open access: yesBiomolecules, 2019
Ubiquitin (Ub) receptors respond to ubiquitylation signals. They bind ubiquitylated substrates and exert their activity in situ. Intriguingly, Ub receptors themselves undergo rapid ubiquitylation and deubiquitylation.
Neta Tanner   +3 more
doaj   +2 more sources

Identification of E3 ligase substrates and PROTAC-induced ubiquitylation sites using proximity-based identification of ubiquitin sites (PrIUS) [PDF]

open access: yesCommunications Biology
The ubiquitin system regulates virtually all cellular processes, yet the vast majority of ubiquitylation sites identified in the human proteome cannot be attributed to specific E3 ligases.
Tanner M. Tessier   +9 more
doaj   +2 more sources

Non-proteolytic ubiquitylation in cellular signaling and human disease

open access: yesCommunications Biology, 2022
International audienceAbstract Ubiquitylation is one of the most common post-translational modifications (PTMs) of proteins that frequently targets substrates for proteasomal degradation.
Izabela Sumara   +2 more
exaly   +2 more sources

Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass

open access: yesNature Cell Biology, 2012
Protein ubiquitylation has emerged as a key regulatory mechanism in DNA-damage signalling and repair pathways. We report a proteome-wide, site-specific survey of ubiquitylation changes after ultraviolet irradiation, identifying numerous upregulated and ...
Petra Beli   +2 more
exaly   +2 more sources

The role of the nucleus in the control of mitochondrial precursor proteins in yeast. [PDF]

open access: yesProtein Sci
Abstract Mitochondria are essential organelles of eukaryotic cells, with vital roles in energy production, biosynthesis of macromolecules, and intracellular signaling. Their function depends on a complex proteome with proteins targeted to different mitochondrial sub‐compartments.
Ritzenhofen K   +3 more
europepmc   +2 more sources

Construction of a robust sepsis prognostic classifier based on E3 ubiquitin ligase-related genes [PDF]

open access: yesFrontiers in Molecular Biosciences
Sepsis is a life-threatening disease with high mortality and one of the leading causes of death worldwide. Although studies have shown that ubiquitylation is closely related to the occurrence and development of sepsis, the prognostic and diagnostic value
Haiyan Xue   +4 more
doaj   +2 more sources

Aging and diet alter the protein ubiquitylation landscape in the mouse brain

open access: yesNature Communications
Post-translational modifications (PTMs) regulate protein homeostasis, but how aging impacts PTMs remains unclear. Here, we used mass spectrometry to reveal changes in hundreds of protein ubiquitylation, acetylation, and phosphorylation sites in the mouse
Antonio Marino   +7 more
doaj   +2 more sources

Global, site-resolved analysis of ubiquitylation occupancy and turnover rate reveals systems properties

open access: yesCell
Ubiquitylation regulates most proteins and biological processes in a eukaryotic cell. However, the site-specific occupancy (stoichiometry) and turnover rate of ubiquitylation have not been quantified.
Shankha Satpathy   +2 more
exaly   +2 more sources

Biotinylation Interferes with Protein Ubiquitylation and Turnover in Arabidopsis-A Cautionary Insight for Proximity Labeling in Ubiquitylation Proteome Studies. [PDF]

open access: yesInt J Mol Sci
Nearly all eukaryotic proteins are turned over by the ubiquitin (Ub)-26S proteasome system (UPS). Despite its broad cellular roles, only a handful of UPS members, particularly the Ub E3 ligases that specifically recognize a protein for ubiquitylation ...
Li Y, Yu P, Hua Z.
europepmc   +2 more sources

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