Results 11 to 20 of about 101,514 (215)

The ubiquitin-proteasome system is required for African swine fever replication. [PDF]

open access: yesPLoS ONE, 2017
Several viruses manipulate the ubiquitin-proteasome system (UPS) to initiate a productive infection. Determined viral proteins are able to change the host's ubiquitin machinery and some viruses even encode their own ubiquitinating or deubiquitinating ...
Lucía Barrado-Gil   +4 more
doaj   +1 more source

Denervation-Induced Activation of the Ubiquitin-Proteasome System Reduces Skeletal Muscle Quantity Not Quality. [PDF]

open access: yesPLoS ONE, 2016
It is well known that the ubiquitin-proteasome system is activated in response to skeletal muscle wasting and functions to degrade contractile proteins. The loss of these proteins inevitably reduces skeletal muscle size (i.e., quantity).
Cory W Baumann   +2 more
doaj   +1 more source

The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo

open access: yesLife Science Alliance, 2023
The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro, whereas FAT10 degradation depends on the 26S proteasome in cellulo, shown by impairing 26S function via Rpt2 knockdown.
Franziska Oliveri   +4 more
doaj   +1 more source

Insulin alleviates degradation of skeletal muscle protein by inhibiting the ubiquitin-proteasome system in septic rats

open access: yesJournal of Inflammation, 2011
Hypercatabolism is common under septic conditions. Skeletal muscle is the main target organ for hypercatabolism, and this phenomenon is a vital factor in the deterioration of recovery in septic patients.
Gao Tao   +8 more
doaj   +1 more source

The Proteasome-Ubiquitin System Is Required for Efficient Killing of Intracellular Streptococcus pneumoniae by Brain Endothelial Cells

open access: yesmBio, 2014
Streptococcus pneumoniae (pneumococcus) is a Gram-positive bacterium that causes serious invasive diseases, such as pneumonia, bacteremia, and meningitis, with high morbidity and mortality throughout the world.
Federico Iovino   +2 more
doaj   +1 more source

Niclosamide prevents the formation of large ubiquitin-containing aggregates caused by proteasome inhibition. [PDF]

open access: yesPLoS ONE, 2010
Protein aggregation is a hallmark of many neurodegenerative diseases and has been linked to the failure to degrade misfolded and damaged proteins. In the cell, aberrant proteins are degraded by the ubiquitin proteasome system that mainly targets short ...
Esther Gies   +9 more
doaj   +1 more source

Proteasome inhibition-enhanced fracture repair is associated with increased mesenchymal progenitor cells in mice.

open access: yesPLoS ONE, 2022
The ubiquitin/proteasome system controls the stability of Runx2 and JunB, proteins essential for differentiation of mesenchymal progenitor/stem cells (MPCs) to osteoblasts.
Hengwei Zhang   +6 more
doaj   +2 more sources

Intracellular Dynamics of the Ubiquitin-Proteasome-System [version 2; referees: 3 approved]

open access: yesF1000Research, 2015
The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene ...
Maisha Chowdhury, Cordula Enenkel
doaj   +1 more source

Intracellular Dynamics of the Ubiquitin-Proteasome-System [v1; ref status: indexed, http://f1000r.es/5o5]

open access: yesF1000Research, 2015
The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene ...
Maisha Chowdhury, Cordula Enenkel
doaj   +1 more source

Up-regulation of ubiquitin–proteasome activity upon loss of NatA-dependent N-terminal acetylation

open access: yesLife Science Alliance, 2022
Inactivation of N-terminal acetyltransferase A is found to alter Rpn4 as well as E3 ligase abundance, causing up-regulation of Ubiquitin–proteasome activity.
Ilia Kats   +6 more
doaj   +1 more source

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