Results 31 to 40 of about 164,092 (257)

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

Life 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, Christian Reinbold, Marc Kschonsak, Anton Khmelinskii, Laura Armbruster, Thomas Ruppert, Michael Knop   +6 more
doaj   +1 more source

Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von hippel-lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities [PDF]

, 2014
E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success.
Adams J., Alessio Ciulli, Bochevarov A. D., Buckley D. L., Buckley D. L., Buckley D. L., Bunnage M. E., Carles Galdeano, Ciechanover A., Cohen P., David M. Dias, Demo S. D., Dias D. M., Hon W. C., Inge Van Molle, Ipek Birced, Louie R. J., Manalo D. J., Morgan S. Gadd, Muchnik E., Nalepa G., Pedro Soares, Pellecchia M., Rabinowitz M. H., Rentsch A., Salvatore Scaffidi, Sarah Hewitt, Semenza G.L., Tetko I. V., Van Molle I., Wells J. A., Zhang W.   +31 more
core   +5 more sources

Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins [PDF]

, 2008
Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail.
Deshaies, Raymond J., Elsasser, Suzanne, Finley, Daniel, Goh, Amanda M., Howley, Peter M., Verma, Rati, Walters, Kylie J.   +6 more
core   +6 more sources

Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]

, 2012
Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone, Rajalingam, Krishnaraj, Dikic, Ivan   +2 more
core   +2 more sources

Poxvirus Exploitation of the Ubiquitin-Proteasome System

Viruses, 2010
Ubiquitination plays a critical role in many cellular processes. A growing number of viruses have evolved strategies to exploit the ubiquitin-proteasome system, including members of the Poxviridae family. Members of the poxvirus family have recently been
Alastair Teale, Qian Wang, Kristin Burles, Michele Barry, Kelly Mottet, Nicholas van Buuren   +5 more
doaj   +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

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

Pathophysiological mechanisms of statin‐associated myopathies: possible role of the ubiquitin‐proteasome system

Journal of Cachexia, Sarcopenia and Muscle, 2020
Background Statins are the cornerstone of pharmacotherapy for atherosclerotic cardiovascular disease. While these drugs are generally safe, treatment adherence is not optimal in a considerable proportion of patients because of the adverse effects on ...
Amirhossein Sahebkar, Arrigo F.G. Cicero, Paolo Di Giosia, Irene Pomilio, Cosimo Andrea Stamerra, Paolo Giorgini, Claudio Ferri, Stephan vonHaehling, Maciej Banach, Tannaz Jamialahmadi   +9 more
doaj   +1 more source

The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a. [PDF]

, 2013
p53 and its major E3 ligase Mdm2 are both ubiquitinated and targeted to the proteasome for degradation. Despite the importance of this in regulating the p53 pathway, little is known about the mechanisms of proteasomal recognition of ubiquitinated p53 and
A Arlt, A Haririnia, A Hishiya, A Peth, A Sparks, AK Hock, AM Ruschak, AS Fatimababy, B Cross, C Brignone, C Wojcik, CF Cheok, D Finley, D Pei, EG Mimnaugh, G Lozano, GL Bond, H Fu, H Fu, H Higashitsuji, H Hiyama, H Inuzuka, H Inuzuka, H Kawahara, HT Kim, I Dikic, J Boehringer, J Das, J Hamazaki, JD Oliner, JD Shaughnessy Jr., JM Stommel, JM Winget, K Husnjak, K Itahana, L Bedford, LF Stevenson, LJ Crawford, LK Linares, LR Dick, LT Vassilev, M Elangovan, M Elangovan, M Isasa, M K Saville, M Kaur, M Wade, M Wade, MD Kaeser, MF Kleijnen, MH Glickman, MJ Lee, MK Saville, MP Bousquet-Dubouch, N Allende-Vega, N Allende-Vega, N Allende-Vega, N Gallastegui, NP Dantuma, NP Dantuma, P Robertson, P Sdek, P Young, PG Santamaria, Q Xu, Q Zhu, R Kulikov, R Verma, S Carter, S Dayal, S Dayal, S Elsasser, S Glockzin, S Menendez, S Nickell, S Raasi, SJ Wei, T Kaneko, T Mayor, T Szlanka, TA Gomez, V Su, VD Nair, XM Sun, Y Jin, Y Kravtsova-Ivantsiv, Y Midorikawa, Y Saeki, Y Wan, YA Lam, YH Shen, YV Wang, Z Lipinszki, Z Lipinszki   +93 more
core   +3 more sources

Site-Specific Proteasome Inhibitors

Biomolecules, 2021
Proteasome is a multi-subunit protein degradation machine, which plays a key role in the maintenance of protein homeostasis and, through degradation of regulatory proteins, in the regulation of numerous cell functions. Proteasome inhibitors are essential
Alexei F. Kisselev
doaj   +1 more source