Results 261 to 270 of about 248,818 (307)
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Essays in Biochemistry, 2005
The major enzyme system catalysing the degradation of intracellular proteins is the proteasome system. A central inner chamber of the cylinder-shaped 20 S proteasome contains the active site, formed by N-terminal threonine residues. The 20 S proteasomes are extremely inefficient in degrading folded protein substrates and therefore one or two ...
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The major enzyme system catalysing the degradation of intracellular proteins is the proteasome system. A central inner chamber of the cylinder-shaped 20 S proteasome contains the active site, formed by N-terminal threonine residues. The 20 S proteasomes are extremely inefficient in degrading folded protein substrates and therefore one or two ...
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Cellular and Molecular Life Sciences, 2014
In eukaryotic cells, proteasomes are highly conserved protease complexes and eliminate unwanted proteins which are marked by poly-ubiquitin chains for degradation. The 26S proteasome consists of the proteolytic core particle, the 20S proteasome, and the 19S regulatory particle, which are composed of 14 and 19 different subunits, respectively ...
Zhu Chao, Gu, Cordula, Enenkel
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In eukaryotic cells, proteasomes are highly conserved protease complexes and eliminate unwanted proteins which are marked by poly-ubiquitin chains for degradation. The 26S proteasome consists of the proteolytic core particle, the 20S proteasome, and the 19S regulatory particle, which are composed of 14 and 19 different subunits, respectively ...
Zhu Chao, Gu, Cordula, Enenkel
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2023
The proteasome is a multi-subunit proteolytic complex that functions to degrade normal proteins for physiological regulation and to eliminate abnormal proteins for cellular protection. Generally, the proteasome targets substrate proteins that are marked by attachment of multiple ubiquitin molecules.
Hegde, Ashok N. +3 more
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The proteasome is a multi-subunit proteolytic complex that functions to degrade normal proteins for physiological regulation and to eliminate abnormal proteins for cellular protection. Generally, the proteasome targets substrate proteins that are marked by attachment of multiple ubiquitin molecules.
Hegde, Ashok N. +3 more
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Molecular Biology Reports, 1997
In this report, we examine the involvement of the ubiquitin-proteasome pathway during fusion and differentiation of myoblast primary cell cultures. Up-regulation of proteasome was observed at the maximum fusion rate and was preceded by an increase of unidentified ubiquitin-conjugates.
F, Gardrat +3 more
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In this report, we examine the involvement of the ubiquitin-proteasome pathway during fusion and differentiation of myoblast primary cell cultures. Up-regulation of proteasome was observed at the maximum fusion rate and was preceded by an increase of unidentified ubiquitin-conjugates.
F, Gardrat +3 more
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2002
In contrast to our detailed knowledge of prokaryotic proteasomes, we have only a limited understanding of the prokaryotic regulators and their functional interaction with the proteasome. Most probably, we will soon learn more about the molecular structure and the mechanism of action of the prokaryotic regulators.
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In contrast to our detailed knowledge of prokaryotic proteasomes, we have only a limited understanding of the prokaryotic regulators and their functional interaction with the proteasome. Most probably, we will soon learn more about the molecular structure and the mechanism of action of the prokaryotic regulators.
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Molecular Biology Reports, 1997
Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease ...
Lupas, A. +6 more
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Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease ...
Lupas, A. +6 more
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Proteasomes and immunoproteasomes.
Rivista di biologia, 2011In eukaryotic cells, the protein degradation is a highly regulated and selective process. Membrane-associated or extracellular proteins are degraded in lysosomes, whereas intracellular protein dismantling is primarily non-lysosomal, being realized by complex, not-membrane enclosed and energy-dependent effectors, the proteasomes, localized in both ...
Fietta, Pieranna, Delsante, Giovanni
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1999
The ubiquitin-proteasome pathway is responsible for the regular turnover of a wide variety of proteins and is a critical regulator of many cellular processes. Although this pathway is abundant and ubiquitous, it is also discriminating. This specificity is achieved because there are multiple levels of regulation at work in the pathway.
L M, Grimm, B A, Osborne
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The ubiquitin-proteasome pathway is responsible for the regular turnover of a wide variety of proteins and is a critical regulator of many cellular processes. Although this pathway is abundant and ubiquitous, it is also discriminating. This specificity is achieved because there are multiple levels of regulation at work in the pathway.
L M, Grimm, B A, Osborne
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2012
Cancer is one of the most frightful diseases mostly resulting in mortality; it has recently become more possible to overcome with the help of new therapies. In this direction, carcinogenesis is defined as a complicated process that can include several different factors that contribute to its progress. Proteasome is implicated in cancer studies as it is
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Cancer is one of the most frightful diseases mostly resulting in mortality; it has recently become more possible to overcome with the help of new therapies. In this direction, carcinogenesis is defined as a complicated process that can include several different factors that contribute to its progress. Proteasome is implicated in cancer studies as it is
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Proteasomes and proteasome inhibition in the central nervous system
Free Radical Biology and Medicine, 2001Although the proteasome is responsible for the majority of intracellular protein degradation, and has been demonstrated to play a pivotal role in a diverse array of cellular activities, the role of the proteasome in the central nervous system is only beginning to be elucidated.
Q, Ding, J N, Keller
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