Results 1 to 10 of about 28,320 (152)
Mitochondrial Regulation of the 26S Proteasome [PDF]
Cell Reports, 2020 Summary: The proteasome is the main proteolytic system for targeted protein degradation in the cell and is fine-tuned according to cellular needs.
Jerzy Adamski +2 more
exaly +7 more sources
Cryo-EM structure of the plant 26S proteasome [PDF]
Plant Communications, 2022 Targeted proteolysis is a hallmark of life. It is especially important in long-lived cells that can be found in higher eukaryotes, like plants. This task is mainly fulfilled by the ubiquitin–proteasome system.
Alexander Schleiffer +2 more
exaly +4 more sources
FAT10 and NUB1L cooperate to activate the 26S proteasome [PDF]
Life Science Alliance, 2023 26S proteasome activation is achieved by the collective binding of the ubiquitin-like modifier FAT10 and its interaction partner NUB1L, causing gate opening in a USP14-independent way.
Florian Brockmann +6 more
doaj +2 more sources
The Logic of the 26S Proteasome [PDF]
Cell, 2017 The ubiquitin proteasome pathway is responsible for most of the protein degradation in mammalian cells. Rates of degradation by this pathway have generally been assumed to be determined by rates of ubiquitylation. However, recent studies indicate that proteasome function is also tightly regulated and determines whether a ubiquitylated protein is ...
Alfred Goldberg
exaly +3 more sources
Reversible phosphorylation of the 26S proteasome [PDF]
Protein & Cell, 2017 The 26S proteasome at the center of the ubiquitin-proteasome system (UPS) is essential for virtually all cellular processes of eukaryotes. A common misconception about the proteasome is that, once made, it remains as a static and uniform complex with ...
Xing Guo, Xiuliang Huang, Mark J. Chen
doaj +3 more sources
Proteasome in action: substrate degradation by the 26S proteasome. [PDF]
Biochem Soc Trans, 2021 Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S proteasome. Additionally, a disordered segment on the substrate — either intrinsic or induced — is critical for proteasome engagement. The proteasome is geared to interact with both of these substrate features and prepare it for degradation.
Sahu I, Glickman MH.
europepmc +4 more sources
Structure characterization of the 26S proteasome [PDF]
Biochimica Et Biophysica Acta - Gene Regulatory Mechanisms, 2011 In all eukaryotic cells, 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. In this review, we focus on structure characterization of the 26S proteasome. Although the progress towards a high-resolution structure of the 26S proteasome has been slow, the recently solved structures of various proteasomal ...
Yifan Cheng
exaly +3 more sources
Structure and Function of the 26S Proteasome [PDF]
Annual Review of Biochemistry, 2018 As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The proteasome's cellular functions range from general protein homeostasis and stress response to the control of vital processes such as cell division and signal transduction ...
Jared Bård +2 more
exaly +5 more sources
Substrate-interacting pore loops of two ATPase subunits determine the degradation efficiency of the 26S proteasome [PDF]
Nature CommunicationsThe 26S proteasome is the major eukaryotic protease responsible for the degradation of misfolded, damaged, and obsolete regulatory proteins. Commitment to degradation occurs when conserved pore loops in the heterohexameric ATPase motor of the proteasome ...
Erika López-Alfonzo +7 more
doaj +2 more sources
20S and 26S proteasome-binding proteins of the rabbit brain: A proteomic dataset [PDF]
Data in Brief, 2021 Fractions of 26S and 20S proteasomes isolated from the rabbit brain by the method of salt fractionation (salt-induced precipitation) contain intrinsic proteasome proteins responsible for assembly of the core particle and regulatory particle of proteasome
Olga Buneeva +4 more
doaj +2 more sources