Results 21 to 30 of about 162,141 (238)

Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy [PDF]

, 2011
Parkin, an E3 ubiquitin ligase implicated in Parkinson's disease, promotes degradation of dysfunctional mitochondria by autophagy. Using proteomic and cellular approaches, we show that upon translocation to mitochondria, Parkin activates the ubiquitin ...
Anh H. Pham, Anna M. Salazar, Chen, Ciechanover, Clark, Cox, David C. Chan, de Godoy, Deng, Deshaies, Ding, Gautier, Gegg, Geisler, Greene, Griparic, Kirkpatrick, Korolchuk, Kuroda, Lee, Matsuda, Michael J. Sweredoski, Narendra, Narendra, Narendra, Narendra, Natalie J. Kolawa, Nickie C. Chan, Okatsu, Ong, Pagliarini, Palacino, Pallanck, Park, Poole, Poole, Rappsilber, Robert L.J. Graham, Shimura, Song, Sonja Hess, Sou, Tai, Tanaka, Twig, Vives-Bauza, Yang, Yao, Ziviani, Ziviani   +49 more
core   +3 more sources

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

mBio, 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, Henrik Gradstedt, Jetta J. Bijlsma   +2 more
doaj   +1 more source

Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain [PDF]

, 2004
To identify previously unknown small molecules that inhibit cell cycle machinery, we performed a chemical genetic screen in Xenopus extracts. One class of inhibitors, termed ubistatins, blocked cell cycle progression by inhibiting cyclin B proteolysis ...
Coffino, Philip, D'Onofrio, Mariapina, Deshaies, Raymond J., Fushman, David, King, Randall W., Peters, Noel R., Sakamoto, Kathleen M., Tochtrop, Gregory P., Varadan, Ranjani, Verma, Rati, Zhang, Mingsheng   +10 more
core   +2 more sources

Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets [PDF]

, 2005
The polyubiquitin receptor Rpn10 targets ubiquitylated Sic1 to the 26S proteasome for degradation. In contrast, turnover of at least one ubiquitin-proteasome system (UPS) substrate, CPY*, is impervious to deletion of RPN10.
Deshaies, Raymond J., Graumann, Johannes, Lipford, J. Russell, Mayor, Thibault, Smith, Geoffrey T.   +4 more
core   +1 more source

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation. [PDF]

, 2019
The 26S proteasome is essential for proteostasis and the regulation of vital processes through ATP-dependent degradation of ubiquitinated substrates. To accomplish the multi-step degradation process, the proteasomes regulatory particle, consisting of lid
Aufderheide, Bard, Bard, Bard, Bashore, Beckwith, Dambacher, de la Peña, Ding, Dong, Eisele, Elsasser, Finley, Glickman, Glickman, Goldstein, Groll, Hershko, Kachroo, Lander, Lasker, Longtine, Matyskiela, Myers, Nemec, Peth, Prakash, Rubin, Smith, Sone, Tomko, Unverdorben, Verma, VerPlank, VerPlank, Wehmer, Wendler, Wenzel, Worden, Worden, Yao, Zhu, Śledź   +42 more
core   +1 more source

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

F1000Research, 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]

F1000Research, 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

Ubiquitination and proteasomal degradation of ATG12 regulates its proapoptotic activity [PDF]

, 2014
During macroautophagy, conjugation of ATG12 to ATG5 is essential for LC3 lipidation and autophagosome formation. Additionally, ATG12 has ATG5-independent functions in diverse processes including mitochondrial fusion and mitochondrial-dependent apoptosis.
Debnath, Jayanta, Giampazolias, Evangelos, Green, Douglas R., Haller, Martina, Hock, Andreas K., Oberst, Andrew, Ryan, Kevin M., Tait, Stephen W. G., Vousden, Karen H.   +8 more
core   +4 more sources

Proteasome Lid Bridges Mitochondrial Stress with Cdc53/Cullin1 NEDDylation Status [PDF]

, 2019
Cycles of Cdc53/Cullin1 rubylation (a.k.a NEDDylation) protect ubiquitin-E3 SCF (Skp1-Cullin1-F-box protein) complexes from self-destruction and play an important role in mediating the ubiquitination of key protein substrates involved in cell cycle ...
Bramasole, L., Gefen, E., Glickman, M. H., Gurevich, S., Jimenez-Morales, D., Johnson, J., Klein, Y., Krogan, N. J., Panat, N., Pick, E., Radzinski, M., Reichmann, D., Reis, N., Rinaldi, T., Sinha, A.   +14 more
core   +1 more source

Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system [PDF]

Open Biology, 2017
Mitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state
Piotr Bragoszewski, Michal Turek, Agnieszka Chacinska   +2 more
doaj   +1 more source