Results 21 to 30 of about 574,104 (383)
Targeting the Ubiquitin System in Glioblastoma
Frontiers in Oncology, 2020 Glioblastoma is the most common primary brain tumor in adults with poor overall outcome and 5-year survival of less than 5%. Treatment has not changed much in the last decade or so, with surgical resection and radio/chemotherapy being the main options ...
Nico Scholz +3 more
doaj +1 more source
Dynamic regulation of dynein localization revealed by small molecule inhibitors of ubiquitination enzymes [PDF]
Open Biology, 2018 Cytoplasmic dynein is a minus-end-directed microtubule-based motor that acts at diverse subcellular sites. During mitosis, dynein localizes simultaneously to the mitotic spindle, spindle poles, kinetochores and the cell cortex.
Julie K. Monda, Iain M. Cheeseman
doaj +1 more source
eLife, 2021 Cell cycle gene expression programs fuel proliferation and are universally dysregulated in cancer. The retinoblastoma (RB)-family of proteins, RB1, RBL1/p107, and RBL2/p130, coordinately represses cell cycle gene expression, inhibiting proliferation, and
Taylor P Enrico +8 more
doaj +1 more source
A Conditional Yeast E1 Mutant Blocks the Ubiquitin–Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome [PDF]
, 2007 E1 ubiquitin activating enzyme catalyzes the initial step in all ubiquitin-dependent processes. We report the isolation of uba1-204, a temperature-sensitive allele of the essential Saccharomyces cerevisiae E1 gene, UBA1.
Amerik A. Y. +59 more
core +2 more sources
Regulation of ubiquitin and ubiquitin‐like modifiers by phosphorylation [PDF]
The FEBS Journal, 2021 The regulatory influence of ubiquitin is vast, encompassing all cellular processes, by virtue of its central roles in protein degradation, membrane trafficking, and cell signaling. But how does ubiquitin, a 76 amino acid peptide, carry out such diverse, complex functions in eukaryotic cells? Part of the answer is rooted in the high degree of complexity
Nathaniel L. Hepowit +4 more
openaire +3 more sources
Nature Communications, 2021 The autophagic degradation of misfolded and ubiquitinated proteins is important for cellular homeostasis. In this process, which is governed by cargo receptors, ubiquitinated proteins are condensed into larger structures and subsequently become targets ...
E. Turco +6 more
semanticscholar +1 more source
Mechanically transduced immunosorbent assay to measure protein-protein interactions
eLife, 2021 Measuring protein-protein interaction (PPI) affinities is fundamental to biochemistry. Yet, conventional methods rely upon the law of mass action and cannot measure many PPIs due to a scarcity of reagents and limitations in the measurable affinity ranges.
Christopher J Petell +6 more
doaj +1 more source
Dss1 is a 26S proteasome ubiquitin receptor [PDF]
, 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.
Arrigoni +35 more
core +4 more sources
The Ubiquitination Machinery of the Ubiquitin System [PDF]
The Arabidopsis Book, 2014 The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as well as proteins that bind to ubiquitinated proteins leading them to their final fate.
openaire +5 more sources
Sugar-Recognizing Ubiquitin Ligases: Action Mechanisms and Physiology
Frontiers in Physiology, 2019 F-box proteins, the substrate recognition subunits of SKP1–CUL1–F-box protein (SCF) E3 ubiquitin ligase complexes, play crucial roles in various cellular events mediated by ubiquitination.
Yukiko Yoshida +2 more
doaj +1 more source