Results 41 to 50 of about 101,514 (215)
Methods to Discover and Evaluate Proteasome Small Molecule Stimulators
Molecules, 2019 Protein accumulation has been identified as a characteristic of many degenerative conditions, such as neurodegenerative diseases and aging. In most cases, these conditions also present with diminished protein degradation. The ubiquitin-proteasome system (
Rachel A. Coleman, Darci J. Trader
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Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions
Molecules, 2023 Ubiquitin, a small protein, is well known for tagging target proteins through a cascade of enzymatic reactions that lead to protein degradation. The ubiquitin tag, apart from its signaling role, is paramount in destabilizing the modified protein.
Wojciech Bialek +2 more
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Advanced Science, EarlyView.ABSTRACT Brown and beige adipocytes dissipate energy as heat, yet effective strategies to enhance their mitochondrial efficiency remain limited. Here, we identify Agnuside (AGN) as a selective stabilizer of the complex I assembly factor NDUFAF6. AGN directly binds cytosolic NDUFAF6, suppresses its ubiquitination, prolongs its half‐life, and facilitates
Qingwen Zhao +7 more
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Advanced Science, EarlyView.ABSTRACT Inflammatory bowel disease (IBD) is characterized by dysregulated T cell responses. RNA helicases, including DExD‐box helicase 21 (DDX21), are pivotal in RNA metabolism, but their role in T cell‐mediated pathology during IBD remains unclear. Here, we demonstrate that DDX21 expression in CD4+ T cells correlates with cell cycle and translation ...
Yujuan Zhang +11 more
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The ubiquitin-proteasome system in glioma cell cycle control
Cell Division, 2012 A major determinant of cell fate is regulation of cell cycle. Tight regulation of this process is lost during the course of development and progression of various tumors.
Vlachostergios Panagiotis J +2 more
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Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. [PDF]
PLoS Pathogens, 2007 The specific and covalent addition of ubiquitin to proteins, known as ubiquitination, is a eukaryotic-specific modification central to many cellular processes, such as cell cycle progression, transcriptional regulation, and hormone signaling ...
Aurélie Angot +3 more
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Advanced Science, EarlyView.Lactate in cervical cancer induces HNRNPU K181 lactylation, opposed by NAA50‐mediated acetylation and suppressed by Pazopanib. This lactylation enhances HNRNPU binding to PHGDH pre‐mRNA exon 1, maintaining exon 1‐containing transcripts and mRNA stability, thereby activating serine metabolism.
Chang Zhang +6 more
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Advanced Science, EarlyView.The hyperactivation of PI3K/AKT signaling in PTEN wild‐type triple‐negative breast cancer represents a clinical paradox. We delineate a novel post‐translational regulatory axis wherein the oncogene TSPYL5 competitively antagonizes the deubiquitinase USP10.
Jiaying Shi +8 more
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Frontiers in Cell and Developmental BiologyNeurodegenerative diseases are characterized by the progressive breakdown of neuronal structure and function and the pathological accumulation of misfolded protein aggregates and toxic protein oligomers.
Taylor R. Church +2 more
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Viral Takeover of the Host Ubiquitin System
Frontiers in Cellular and Infection Microbiology, 2011 Like the other more well-characterized post-translational modifications (phosphorylation, methylation, acetylation, acylation, etc.), the attachment of the 76 amino acid ubiquitin (Ub) protein to substrates has been shown to govern countless cellular ...
Jean K Gustin +3 more
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