Results 11 to 20 of about 164,141 (292)

The Ubiquitin-Proteasome System in Neurodegeneration [PDF]

Antioxidants & Redox Signaling, 2014
Significance: Impairment of the ubiquitin-proteasome system (UPS) has been implicated in the pathogenesis of a wide variety of neurodegenerative disorders, including Alzheimer's, Parkinson's, and Huntington's diseases.
Chris McKinnon, Sarah J. Tabrizi
openaire   +3 more sources

Stressing the ubiquitin-proteasome system [PDF]

Cardiovascular Research, 2009
Unfolded and misfolded proteins are inherently toxic to cells and have to be quickly and efficiently eliminated before they intoxicate the intracellular environment. This is of particular importance during proteotoxic stress when, as a consequence of intrinsic or extrinsic factors, the levels of misfolded proteins are transiently or persistently ...
Nico P, Dantuma, Kristina, Lindsten
openaire   +2 more sources

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

PLoS 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, Inmaculada Galindo, Diego Martínez-Alonso, Sergio Viedma, Covadonga Alonso   +4 more
doaj   +1 more source

The ubiquitin-proteasome system

Journal of Biosciences, 2006
The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic proteins targeted for degradation by this pathway are first 'tagged' by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the ...
Nandi, Dipankar, Tahiliani, Pankaj, Kumar, Anujith, Chandu, Dilip   +3 more
openaire   +4 more sources

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

PLoS 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, Haiming M Liu, LaDora V Thompson   +2 more
doaj   +1 more source

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

Life 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, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas, Michael Basler   +4 more
doaj   +1 more source

Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the pap1 transcription factor [PDF]

, 2012
Here we report the result of a genetic screen for mutants resistant to the microtubule poison methyl benzimidazol-2-yl carbamate (MBC) that were also temperature sensitive for growth.
A Varshavsky, C Gordon, Caroline R. Wilkinson, Christopher J. McInerny, Colin Gordon, CR Wilkinson, Deanna M. Koepp, E Strickland, H Seino, IS Nielsen, Itaru Samejima, K Nagao, M Arioka, M Penney, M Shimanuki, Mairi Wallace, Mary Penney, MH Glickman, R Booher, Rasmus Hartmann-Petersen, RJ Dohmen, S Moreno, Søs G. Mathiassen, T Toda, T Toda, Takashi Toda, TG Turi, V Bailly, WM Toone   +28 more
core   +8 more sources

Dss1 is a 26S proteasome ubiquitin receptor [PDF]

, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Arrigoni, Bohn, Choi, Cornilescu, Deveraux, Dosztányi, Ellisdon, Faza, Finley, Funakoshi, Groll, Hartmann-Petersen, Husnjak, Husnjak, Jossé, Kjaergaard, Kriegenburg, Matsuyama, Mayor, Moreno, Obradovic, Peth, Saeki, Sakata, Schreiner, Seeger, Sone, Spratt, Su, Tomko, Uversky, Verma, Verma, Vogt, Wilkinson, Yang   +35 more
core   +5 more sources

Subnormothermic Perfusion in the Isolated Rat Liver Preserves the Antioxidant Glutathione and Enhances the Function of the Ubiquitin Proteasome System. [PDF]

, 2016
The reduction of oxidative stress is suggested to be one of the main mechanisms to explain the benefits of subnormothermic perfusion against ischemic liver damage. In this study we investigated the early cellular mechanisms induced in isolated rat livers
Alva, Norma, Carbonell, Teresa, Dewey, Shannamar, Gomes, Aldrin V, Sanchez-Nuño, Sergio   +4 more
core   +9 more sources

A Conditional Yeast E1 Mutant Blocks the Ubiquitin–Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome [PDF]

, 2007
E1 ubiquitin activating enzyme catalyzes the initial step in all ubiquitin-dependent processes. We report the isolation of uba1-204, a temperature-sensitive allele of the essential Saccharomyces cerevisiae E1 gene, UBA1.
Amerik A. Y., Babbitt S. E., Bertolaet B. L., Bertolaet B. L., Biggins S., Chen L., Cheng I. H., Ciechanover A., Deshaies R. J., Deveraux Q., Elsasser S., Elsasser S., Elsasser S., Finley D., Funakoshi M., Gandre S., Glickman M. H., Guthrie C., Haas A. L., Haracska L., Hicke L., Hofmann K., Johnson E. S., Kang Y., Kleijnen M. F., Kulka R. G., Lambertson D., Lambertson D., Lowe E. D., Madura K., McGrath J. P., Nazli Ghaboosi, Ortolan T. G., Peng J., Pickart C. M., Raasi S., Raasi S., Rao H., Raymond J. Deshaies, Richly H., Ryu K. S., Saeki Y., Saeki Y., Saeki Y., Salvat C., Schauber C., Schuberth C., Shimada K., Swanson R., Swanson R., van Nocker S., van Nocker S., Verma R., Verma R., Verma R., Walters K. J., Walters K. J., Watkins J. F., Wilkinson C.R.M., William Tansey   +59 more
core   +2 more sources