Results 271 to 280 of about 17,362,245 (308)
Stress responses induced by perturbation of the ubiquitin-proteasome system. [PDF]
Trends Biochem SciRai M, Hunt LC, Demontis F.
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Ubiquitin proteasome system (UPS): a crucial determinant of the epigenetic landscape in cancer. [PDF]
EpigenomicsRoy S, Ghosh MK.
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The ubiquitin proteasome system and schizophrenia
The Lancet Psychiatry, 2020 The 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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Cellular and Molecular Life Sciences, 2004
The proteolytic active sites of the 26S proteasome are sequestered within the central chamber of its 20S catalytic core particle. Access to this chamber is through a narrow channel defined by the outer alpha subunits. Free proteasome 20S core particles are found in an autoinhibited state in which the N-termini of neighboring alpha subunits are anchored
Bajorek, Monika, Glickman, M H
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The proteolytic active sites of the 26S proteasome are sequestered within the central chamber of its 20S catalytic core particle. Access to this chamber is through a narrow channel defined by the outer alpha subunits. Free proteasome 20S core particles are found in an autoinhibited state in which the N-termini of neighboring alpha subunits are anchored
Bajorek, Monika, Glickman, M H
+19 more sources
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 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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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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Studies of the Ubiquitin Proteasome System
Current Protocols in Cell Biology, 2006AbstractA concept that has arisen over the last decade is that proteins can, in general, be covalently modified by polypeptides, resulting in alterations in their fate and function. The first‐identified and most well studied of these modifying polypeptides is ubiquitin.
Kevin L, Lorick +4 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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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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