Results 1 to 10 of about 33,702 (335)

Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster. [PDF]

open access: yesPLoS ONE, 2015
Protein ubiquitylation is a dynamic process that affects the function and stability of proteins and controls essential cellular processes ranging from cell proliferation to cell death. This process is regulated through the balanced action of E3 ubiquitin
Levente Kovács   +5 more
doaj   +6 more sources

The E3 ligase RAD18-mediated ubiquitination of henipavirus matrix protein promotes its nuclear-cytoplasmic trafficking and viral egress [PDF]

open access: yesEmerging Microbes and Infections
The nuclear-cytoplasmic trafficking of matrix proteins (M) is essential for henipavirus budding, with M protein ubiquitination playing a pivotal role in this dynamic process.
Dongning Jin   +12 more
doaj   +2 more sources

Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase

open access: yeseLife, 2022
The p97/Cdc48 ATPase and its ubiquitin receptors Ufd1-Npl4 are essential to unfold ubiquitylated proteins in many areas of eukaryotic cell biology.
Ryo Fujisawa   +2 more
doaj   +1 more source

Neutron-encoded diubiquitins to profile linkage selectivity of deubiquitinating enzymes

open access: yesNature Communications, 2023
Most insights into deubiquitinase (DUB) substrate specificity originate from studies with isolated di-ubiquitins (diUb), but in cells diUbs with different linkage types coexist.
Bianca D. M. van Tol   +13 more
doaj   +1 more source

Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix. [PDF]

open access: yesPLoS ONE, 2012
Mollusks shell formation is mediated by matrix proteins and many of these proteins have been identified and characterized. However, the mechanisms of protein control remain unknown.
Dong Fang   +8 more
doaj   +1 more source

Mechanism of selective recognition of Lys48-linked polyubiquitin by macrocyclic peptide inhibitors of proteasomal degradation

open access: yesNature Communications, 2023
Post-translational modification of proteins with polyubiquitin chains is a critical cellular signaling mechanism in eukaryotes with implications in various cellular states and processes.
Betsegaw Lemma   +7 more
doaj   +1 more source

Ubiquitin-related modifiers of Arabidopsis thaliana influence root development. [PDF]

open access: yesPLoS ONE, 2014
Ubiquitins are small peptides that allow for posttranslational modification of proteins. Ubiquitin-related modifier (URM) proteins belong to the class of ubiquitin-like proteins. A primary function of URM proteins has been shown to be the sulfur transfer
Florian John   +4 more
doaj   +1 more source

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

open access: yesNature Communications, 2020
LUBAC is involved in adding linear ubiquitin chains to important immune signaling proteins. Here the authors show that this mechanism is effective in inhibiting STAT1-mediated interferon signaling, and that the deubiquitinase OTULIN can remove these ...
Yibo Zuo   +13 more
doaj   +1 more source

A comparative analysis of the ubiquitination kinetics of multiple degrons to identify an ideal targeting sequence for a proteasome reporter. [PDF]

open access: yesPLoS ONE, 2013
The ubiquitin proteasome system (UPS) is the primary pathway responsible for the recognition and degradation of misfolded, damaged, or tightly regulated proteins.
Adam T Melvin   +5 more
doaj   +1 more source

Comparative Genome Analysis Across 128 Phytophthora Isolates Reveal Species-Specific Microsatellite Distribution and Localized Evolution of Compartmentalized Genomes

open access: yesFrontiers in Microbiology, 2022
Phytophthora sp. are invasive groups of pathogens belonging to class Oomycetes. In order to contain and control them, a deep knowledge of their biology and infection strategy is imperative.
Kajal Mandal   +7 more
doaj   +1 more source

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