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Mitochondrial Regulation of the 26S Proteasome [PDF]

open access: yesCell 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]

open access: yesPlant 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]

open access: yesLife 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

Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome [PDF]

open access: yesBiomolecules, 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   +3 more
doaj   +2 more sources

Substrate-interacting pore loops of two ATPase subunits determine the degradation efficiency of the 26S proteasome [PDF]

open access: yesNature Communications
The 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]

open access: yesData 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

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

open access: yesPLoS 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   +3 more
doaj   +2 more sources

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

open access: yesChinese 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   +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]

open access: yesPlant 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   +3 more
doaj   +2 more sources

Mechanisms and regulation of substrate degradation by the 26S proteasome [PDF]

open access: yesNature Reviews Molecular Cell Biology
Christine Gee   +2 more
exaly   +2 more sources

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