Results 21 to 30 of about 51,947 (207)

Ubiquitin Receptor RPN13 Mediates the Inhibitory Interaction of Diphenyldihaloketones CLEFMA and EF24 With the 26S Proteasome

Frontiers in Chemistry, 2018
The proteasome is a validated target in drug discovery for diseases associated with unusual proteasomal activity. Here we report that two diphenyldihaloketones, CLEFMA and EF24, inhibit the peptidase activity of the 26S proteasome.
Geeta Rao, Gregory Nkepang, Jian Xu, Hooman Yari, Hailey Houson, Chengwen Teng, Vibhudutta Awasthi   +6 more
doaj   +1 more source

The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain [PDF]

, 2013
The plant cytotoxin ricin enters mammalian cells by receptor-mediated endocytosis, undergoing retrograde transport to the endoplasmic reticulum (ER) where its catalytic A chain (RTA) is reductively separated from the holotoxin to enter the cytosol and ...
Spooner, Robert A., Roberts, David M, Roberts, Lynne M, Lord, J Michael, Cook, Jonathan P., Pietroni, Paola, Roberts, David M., Lord, Mike, Roberts, L. M. (Lynne M.), Spooner, Robert A, Vasisht, Nishi, Hartmann-Petersen, Rasmus, Cook, Jonathan P   +12 more
core   +1 more source

Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution.

PLoS ONE, 2015
Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization.
Diego Sbardella, Grazia Raffaella Tundo, Francesca Sciandra, Manuela Bozzi, Magda Gioia, Chiara Ciaccio, Umberto Tarantino, Andrea Brancaccio, Massimo Coletta, Stefano Marini   +9 more
doaj   +1 more source

Early cysteine-dependent inactivation of 26S proteasomes does not involve particle disassembly

Redox Biology, 2018
Under oxidative stress 26S proteasomes suffer reversible disassembly into its 20S and 19S subunits, a process mediated by HSP70. This inhibits the degradation of polyubiquitinated proteins by the 26S proteasome and allows the degradation of oxidized ...
Martín Hugo, Ioanna Korovila, Markus Köhler, Carlos García-García, J. Daniel Cabrera-García, Anabel Marina, Antonio Martínez-Ruiz, Tilman Grune   +7 more
doaj   +1 more source

Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain. [PDF]

PLoS ONE, 2013
Proteostasis is critical for the maintenance of life. In neuronal cells an imbalance between protein synthesis and degradation is thought to be involved in the pathogenesis of neurodegenerative diseases during aging.
Carolin Giannini, Alexander Kloß, Sabrina Gohlke, Michele Mishto, Thomas P Nicholson, Paul W Sheppard, Peter-Michael Kloetzel, Burkhardt Dahlmann   +7 more
doaj   +1 more source

Cic1p/Nsa3p is required for synthesis and nuclear export of 60S ribosomal subunits [PDF]

, 2003
Cic1p/Nsa3p was previously reported to be associated with the 26S proteasome and required for the degradation of specific substrates, but was also shown to be associated with early pre-60S particles and to be localized to the nucleolus.
Tollervey, D, D. Tollervey, Oeffinger, M, Bozzoni, I, M. Oeffinger, Fatica, A, BOZZONI, Irene, FATICA, Alessandro   +7 more
core   +1 more source

Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome [PDF]

, 2017
<p>The 26S proteasome is the macromolecular machine responsible for ATP/ubiquitin dependent degradation. As aberration in proteasomal degradation has been implicated in many human diseases, structural analysis of the human 26S proteasome complex is
Novitsky, E., Leitner, A., Baumeister, W, Greenberg, C., Andreas Schweitzer, Sali, A., Nanni, Paolo, Sakata, Eri, Abdullah Kahraman, Dixon, Jack E, Huszagh, A., Aebersold, R., Wolfgang Baumeister, Yang, Y, Greenberg, CH, Dixon, J., Schweitzer, A, Engel, JL, Schweitzer, A (8134524), Yang, Y., Dixon, JE (8134563), Xiaorong Wang, Guo, X (8134560), Wang, Xiaorong, Huang, L., Yang, Y (8134545), Chopra, N., Beck, F, Dixon, JE, Nanni, P (8134554), Ruedi Aebersold, Baumeister, Wolfgang, Cimermancic, P., Jack E. Dixon, Paolo Nanni, Andrej Sali, Charles Greenberg, Sali, A, Wang, X (5387767), Florian Beck, Nikita Chopra, Guo, X., Greenberg, CH (8134533), Sakata, E., Kahraman, A., Wang, X, Chopra, Nikita, Greenberg, Charles, Guo, X, Huszagh, AS, Engel, JL (8134530), Beck, F., Nanni, P, Scott D. Rychnovsky, Aebersold, R, Alexander Leitner, Huang, Lan, Lan Huang, Huang, L (8134575), Novitsky, Eric J, Yingying Yang, Rychnovsky, SD (8134566), Eri Sakata, Eric J. Novitsky, Baumeister, W., Yu, C, Alexander S. Huszagh, Sali, A (5802812), Cimermancic, Peter, Schweitzer, A., Yu, C., Beck, F (8134539), Leitner, A, Peter Cimermancic, Rychnovsky, SD, Chopra, N, Sali, Andrej, Beck, Florian, Clinton Yu, Rychnovsky, S., Leitner, A (8134551), Yu, C (5821973), Novitsky, EJ (8134548), Engel, J., Rychnovsky, Scott D, Xing Guo, Yang, Yingying, Sakata, E, Schweitzer, Andreas, Wang, X., Kahraman, A (8134557), Chopra, N (8134527), James L. Engel, Nanni, P., Novitsky, EJ, Cimermancic, P (8134521), Cimermancic, P, Guo, Xing, Baumeister, W (8134572), Aebersold, Ruedi, Huszagh, AS (8134536), Huszagh, Alexander S, Aebersold, R (8134569), Sakata, E (8134542), Leitner, Alexander, Yu, Clinton, Engel, James L, Kahraman, A, Huang, L, Kahraman, Abdullah, Guo X, Engel, James L., Kahraman A, Beck F, Leitner A, Dixon, Jack E., Huszagh AS, Nanni P, Rychnovsky, Scott D., Cimermancic P, Baumeister W, Huszagh, Alexander S., Yu C, Engel JL, Rychnovsky SD, Chopra N, Huang L, Wang X, Greenberg C, Yang Y, Aebersold R, Novitsky EJ, Aebersold, Rudolf; id_orcid, Dixon JE, Novitsky, Eric J., Sali A, Sakata E, Schweitzer A   +137 more
core   +1 more source

Ubiquitin-Like protein 5 interacts with the silencing suppressor p3 of rice stripe virus and mediates its degradation through the 26S proteasome pathway.

PLoS Pathogens, 2020
Ubiquitin like protein 5 (UBL5) interacts with other proteins to regulate their function but differs from ubiquitin and other UBLs because it does not form covalent conjugates.
Binghua Chen, Lin Lin, Yuwen Lu, Jiejun Peng, Hongying Zheng, Qiankun Yang, Shaofei Rao, Guanwei Wu, Junmin Li, Zhuo Chen, Baoan Song, Jianping Chen, Fei Yan   +12 more
doaj   +1 more source

Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster [PDF]

, 2003
The regulatory complex of the 26S proteasome is responsible for the selective recognition and binding of multiubiquitinated proteins. It was earlier shown that the subunit S5a/Rpn10/p54 of the regulatory complex is the only cellular protein capable of ...
Andó, István, Deák, Péter, Kurucz, Éva, Udvardy, Andor, Kiss, István, Haracska, Lajos, Virágh, Erika, Szlanka, Tamás   +7 more
core   +1 more source

Phosphatase UBLCP1 controls proteasome assembly [PDF]

Open Biology, 2017
Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase.
Shuangwu Sun, Sisi Liu, Zhengmao Zhang, Wang Zeng, Chuang Sun, Tao Tao, Xia Lin, Xin-Hua Feng   +7 more
doaj   +1 more source