Results 211 to 220 of about 98,327 (230)
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Illuminating the ubiquitin/proteasome system
Experimental Cell Research, 2010The ubiquitin/proteasome system (UPS) is responsible for the regulated processive degradation of proteins residing in the cytosol, nucleus, and endoplasmic reticulum. The two central players are ubiquitin, a small protein that is conjugated to substrates, and the proteasome, a large multi-subunit proteolytic complex that executes degradation of ...
Florian A, Salomons +2 more
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The ubiquitin proteasome system and schizophrenia
The Lancet Psychiatry, 2020The ubiquitin-proteasome system is a master regulator of neural development and the maintenance of brain structure and function. It influences neurogenesis, synaptogenesis, and neurotransmission by determining the localisation, interaction, and turnover of scaffolding, presynaptic, and postsynaptic proteins.
Luza, Sandra +5 more
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Ubiquitin–Proteasome System in Spermatogenesis
2014Spermatogenesis represents a complex succession of cell division and differentiation events resulting in the continuous formation of spermatozoa. Such a complex program requires precise expression of enzymes and structural proteins which is effected not only by regulation of gene transcription and translation, but also by targeted protein degradation ...
Rohini, Bose +3 more
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Ubiquitin–Proteasome System and mitochondria — Reciprocity
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2011Recently, sporadic links have been published between mitochondria - membrane-confined organelles - and the cytosolic ubiquitin-proteasome system (UPS) for removal of cellular proteins. For example, Fzo1, a mitochondrial outer membrane mitofusin was shown to be ubiquitinated by a ubiquitin ligase, Cdc53(MDM30), and degraded by the proteasome.
Nurit, Livnat-Levanon +1 more
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Autophagy and Ubiquitin-Proteasome System
2019Millions of protein molecules are synthesized per minute in each cell, and simultaneously, millions of protein molecules are degraded. Mutated and misfolded newly synthesized proteins are rapidly degraded to prevent the toxicity caused by the accumulation of these protein fragments.
Yan, Wang, Wei-Dong, Le
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The ubiquitin–proteasome system in cardiomyopathies
Current Opinion in Cardiology, 2011Fine equilibrium between protein synthesis and protein degradation is essential for cell survival and function. After initial synthesis, membrane and secretory proteins are modified, folded, and assembled in the endoplasmic reticulum, whereas other proteins are synthesized and processed in the cytosol.
Saskia, Schlossarek, Lucie, Carrier
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Ubiquitin–proteasome system and Parkinson's diseases
Experimental Neurology, 2005Parkinson's disease (PD) is a progressive neurodegenerative disorder characterized by nigrostriatal dopaminergic degeneration and development of cytoplasmic inclusions known as Lewy bodies. To date, the mechanisms involved in PD pathogenesis are not clearly understood.
Ranjita, Betarbet +2 more
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The ubiquitin-proteasome system and endocytosis
Journal of Cell Science, 1999ABSTRACT Internalization of membrane proteins has been studied for more than three decades without solving all the underlying mechanisms. Our knowledge of clathrin-mediated endocytosis is certainly sufficient to understand the basic principles.
Strous, G J, Govers, R
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Ubiquitin–proteasome system and Parkinson's disease
Movement Disorders, 2006AbstractIncreasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity.
C Warren, Olanow, Kevin St P, McNaught
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