Results 11 to 20 of about 76,539 (287)

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

Molecular Cell, 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. The proteasome subunits Rpn10 and Rpn13 are known to bind ubiquitin, but genetic and biochemical data suggest the existence of at least one ...
Paraskevopoulos, Konstantinos, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Medina, Bethan, Larsen, Ida B., Brandstrup, Rikke, Hardwick, Kevin G., Hay, Ronald T., Kragelund, Birthe Brandt, Hartmann-Petersen, Rasmus, Gordon, Colin   +11 more
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Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome

Biomolecules, 2020
The 26S proteasome is the endpoint of the ubiquitin- and ATP-dependent degradation pathway. Over the years, ATP was regarded as completely essential for 26S proteasome function due to its role in ubiquitin-signaling, substrate unfolding and ensuring its ...
Peter Tsvetkov, Nadav Myers, Julia Adler, Yosef Shaul   +3 more
doaj   +2 more sources

Dietary apigenin potentiates the inhibitory effect of interferon-α on cancer cell viability through inhibition of 26S proteasome-mediated interferon receptor degradation

Food & Nutrition Research, 2016
Background: Type I interferons (IFN-α/β) have broad and potent immunoregulatory and antiproliferative activities. However, it is still known whether the dietary flavonoids exhibit their antiviral and anticancer properties by modulating the function of ...
Sheng Li, Li-juan Yang, Ping Wang, Yu-jiao He, Jun-mei Huang, Han-wei Liu, Xiao-fei Shen, Fei Wang   +7 more
doaj   +2 more sources

Phosphorylation of ATPase subunits of the 26S proteasome [PDF]

FEBS Letters, 1998
The 26S proteasome complex plays a major role in the non‐lysosomal degradation of intracellular proteins. Purified 26S proteasomes give a pattern of more than 40 spots on 2D‐PAGE gels. The positions of subunits have been identified by mass spectrometry of tryptic peptides and by immunoblotting with subunit‐specific antipeptide antibodies.
Mason, Grant G.F., Murray, Rachael Z., Pappin, Daryl, Rivett, A. Jennifer   +3 more
openaire   +4 more sources

A kinetic model for USP14 regulated substrate degradation in 26S proteasome. [PDF]

PLoS Computational Biology
Despite high-resolution structural studies on the USP14-proteasome-substrate complexes, time-resolved cryo-electron microscopy (cryo-EM) results on USP14-regulated allostery of the 26S proteasome are still very limited and a quantitative understanding of
Di Wu, Qi Ouyang, Hongli Wang, Youdong Mao   +3 more
doaj   +2 more sources

UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity [PDF]

Proceedings of the National Academy of Sciences, 2011
Protein degradation by the 26S proteasome is a fundamental process involved in a broad range of cellular activities, yet how proteasome activity is regulated remains poorly understood. We report here that ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) is a 26S proteasome phosphatase that regulates nuclear proteasome activity.
Xing, Guo, James L, Engel, Junyu, Xiao, Vincent S, Tagliabracci, Xiaorong, Wang, Lan, Huang, Jack E, Dixon   +6 more
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Characterization of the brain 26S proteasome and its interacting proteins

Frontiers in Molecular Neuroscience, 2010
Proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons.
Hwan-Ching Tai, Henrike Besche, Alfred L Goldberg, Erin M Schuman, Erin M Schuman   +4 more
doaj   +2 more sources

Research and Therapeutic Advances of 26S Proteasome Subunit 
in Non-small Cell Lung Cancer [PDF]

Chinese Journal of Lung Cancer
Lung cancer is one of the most common cancers worldwide and is the leading cause of cancer deaths. Lung adenocarcinoma is the most common type of lung cancer.
Chenrui MOU, Shaotong ZOU, Chao REN, Zihan YI, Jianlin SHI   +4 more
doaj   +2 more sources

SnRK2.6-mediated phosphorylation stabilizes proteasome regulator 1 (PTRE1) to enhance 26S proteasome activity and coordinate ABA signaling in Arabidopsis [PDF]

Plant Communications
Abscisic acid (ABA) regulates diverse aspects of plant growth, particularly adaptive responses to abiotic stress. Although the ubiquitin–proteasome system is recognized as a pivotal pathway for degrading key components of ABA signaling, the mechanisms ...
Peng-Chao Hao, Ling-Li Zheng, Jin-Shuang Dou, Hong-Wei Xue   +3 more
doaj   +2 more sources

Mechanisms of substrate recognition by the 26S proteasome. [PDF]

Curr Opin Struct Biol, 2021
The majority of regulated protein degradation in eukaryotes is accomplished by the 26S proteasome, the large proteolytic complex responsible for removing regulatory proteins and damaged proteins. Proteins are targeted to the proteasome by ubiquitination, and degradation is initiated at a disordered region within the protein.
Davis C, Spaller BL, Matouschek A.
europepmc   +3 more sources