Results 21 to 30 of about 18,434,088 (294)

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

Functional analysis of proteasome-associated ubiquitin ligases in plants [PDF]

, 2022
Degradation of intracellular proteins by the ubiquitin-proteasome system (UPS) is a sophisticated mechanism that begins with anchoring ubiquitin molecules to a substrate and ends with proteasome-dependent proteolysis.
Wang, Zhishuo
core   +1 more source

Ubiquitin Proteasome System in Stress and Disease [PDF]

Biochemistry Research International, 2012
The proteasome is an ATP-dependent multisubunit self-compartmentalised protease complex. It is the major regulator of intracellular proteins turnover. The majority of proteins degraded by proteasomes are modified by covalent attachment of polyubiquitin chains.
Dmitry Karpov, Michael H. Glickman, Shoshana Bar-Nun, Philip Coffino   +3 more
doaj   +4 more sources

Regulation of CHK1 by the Ubiquitin–Proteasome System [PDF]

The FEBS Journal, 2020
The checkpoint kinase 1 (CHK1) is a master regulator of genome integrity in vertebrate cells. Despite its important cell cycle functions, its regulation is still incompletely understood. Cassidy et al. provide novel insights on the regulation of the CHK1 abundance by the HECT E3 ligase HUWE1 during unperturbed cell cycle as well as in response to ...
Cartel, Maëlle, Didier, Christine
openaire   +3 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.
Hardwick, Kevin G., Hay, Ronald T., Larsen, Ida B., Kragelund, Birthe B., Tatham, Michael H, Rösner, Heike I, Kragelund, Birthe Brandt, Hay, Ronald T, Kragelund, Birthe B, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Paraskevopoulos, Konstantinos, Brandstrup, Rikke, Larsen, Ida B, Medina, Bethan; id_orcid, Hartmann-Petersen, Rasmus, Gordon, Colin, Rösner, Heike I., Hardwick, Kevin G, Medina, Bethan   +20 more
core   +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.
Dias, David M, Carles Galdeano (1305135), Galdeano, Carles, Dias, David M., David M. Dias (1340694), Van Molle, Inge, Gadd, Morgan Stuart, Ciulli, Alessio, Sarah Hewitt (1340700), Soares, Pedro, Galdeano , Carles, Pedro Soares (393566), Gadd, Morgan S., Salvatore Scaffidi (1340703), Inge Van Molle (1284120), Morgan S. Gadd (149371), Scaffidi, Salvatore, Ipek Birced (1340697), Alessio Ciulli (762789), Hewitt, Sarah, Birced, Ipek   +20 more
core   +1 more source

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

, 2014
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
J Das, S Menendez, Menendez, S., Saville, M. K., S Dayal, Das, J., M K Saville, Dayal, S., A Sparks, Robertson, P., P Robertson, Sparks, A.   +11 more
core   +1 more source

Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators [PDF]

, 2022
The ubiquitin-proteasome system is vital to hormone-mediated developmental and stress responses in plants. Ubiquitin ligases target hormone-specific transcriptional activators (TAs) for degradation, but how TAs are processed by proteasomes remains ...
Grey, Heather, Spoel, Steven H., Mori, Izumi, Wang, Zhishuo, Genschik, Pascal, Nomoto, Mika, Potuschak, Thomas, Mori, Izumi C., Spoel, Steven, Orosa-Puente, Beatriz, Matsuura, Takakazu, Tada, Yasuomi   +11 more
core   +1 more source

Role of the Ubiquitin Proteasome System in the Heart [PDF]

Circulation Research, 2013
Proper protein turnover is required for cardiac homeostasis and, accordingly, impaired proteasomal function appears to contribute to heart disease. Specific proteasomal degradation mechanisms underlying cardiovascular biology and disease have been identified, and such cellular pathways have been proposed to be targets of clinical relevance. This review
J. Pagan, T. Seto, M. Pagano, CITTADINI, ANTONIO   +3 more
openaire   +7 more sources

Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation [PDF]

, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Amanda Denuc, Marfany Gemma, Denuc Isern, Amanda, Burr, A. A., Gemma Marfany, Blount Jessica R., Sokol V Todi, Todi Sokol V., Marfany i Nadal, Gemma, Jessica R Blount, Denuc Amanda, Blount, J. R., Aaron A Burr, Burr Aaron A., Todi, Sokol V.   +14 more
core   +2 more sources