Results 41 to 50 of about 76,539 (287)

Fluorescence-based proteasome activity profiling [PDF]

, 2011
With the proteasome emerging as a therapeutic target for cancer treatment, accurate tools for monitoring proteasome (inhibitor) activity are in demand.
Jong, A., Rodenko, B., Berkers, C.R., Schuurman, K.G., Ovaa, H., Boris Rodenko, Annemieke de Jong, Celia R. Berkers, Karianne G. Schuurman, Huib Ovaa   +9 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

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   +109 more
core   +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

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

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

Assembly, structure, and function of the 26S proteasome [PDF]

Trends in Cell Biology, 2010
The 26S proteasome is a large multiprotein complex involved in the regulated degradation of ubiquitinated proteins in the cell. The 26S proteasome has been shown to control an increasing number of essential biochemical mechanisms of the cellular lifecycle including DNA synthesis, repair, transcription, translation, and cell signal transduction ...
Lynn, Bedford, Simon, Paine, Paul W, Sheppard, R John, Mayer, Jeroen, Roelofs   +4 more
openaire   +2 more sources

Regulation of the 26S proteasome by adenovirus E1A [PDF]

The EMBO Journal, 2000
We have identified the N-terminus of adenovirus early region 1A (AdE1A) as a region that can regulate the 26S proteasome. Specifically, in vitro and in vivo co-precipitation studies have revealed that the 19S regulatory components of the proteasome, Sug1 (S8) and S4, bind through amino acids (aa) 4-25 of Ad5 E1A.
A S, Turnell, R J, Grand, C, Gorbea, X, Zhang, W, Wang, J S, Mymryk, P H, Gallimore   +6 more
openaire   +2 more sources

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

Depleting the 19S proteasome regulatory PSMD1 subunit as a cancer therapy strategy

Cancer Medicine, 2023
Background Proteasome inhibitors are in use in treating certain types of cancers. These drugs inhibit the catalytic activity of the 20S proteasome, shared by all the different proteasome complexes.
Julia Adler, Roni Oren, Yosef Shaul
doaj   +1 more source