Results 211 to 220 of about 13,489 (251)
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Late Events in the Assembly of 20S Proteasomes
Journal of Structural Biology, 1998Electron microscopy and STEM mass measurements have been used to characterize late intermediates in the assembly pathway of wildtype and mutant Rhodococcus proteasomes. A proteolytically inactive and processing-incompetent mutant, betaK33A, allowed a short-lived late intermediate of the pathway to be captured, the preholoproteasome.
Mayr, U. +4 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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Biochemistry, 2023
ABSTRACT PI31 ( P roteasome I nhibitor of 31 ,000 Daltons) is a 20S proteasome binding protein originally identified as an in vitro inhibitor of 20S proteasome proteolytic activity.
Jason Wang +2 more
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ABSTRACT PI31 ( P roteasome I nhibitor of 31 ,000 Daltons) is a 20S proteasome binding protein originally identified as an in vitro inhibitor of 20S proteasome proteolytic activity.
Jason Wang +2 more
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Anti‐20S proteasome autoantibodies inhibit proteasome stimulation by proteasome activator PA28
Arthritis & Rheumatism, 2006AbstractObjectiveThe ubiquitin‐proteasome system plays a central role in cellular homeostasis as well as in regulation of the inflammatory and stress responses. However, the occurrence of autoantibodies against 20S proteasome has, to date, been considered to be a nonspecific epiphenomenon in patients with autoimmune disorders. This study was undertaken
Michael, Brychcy +6 more
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Proteasome Activator PA28 and Its Interaction with 20 S Proteasomes
Archives of Biochemistry and Biophysics, 1996An activator of the 20 S proteasome has been purified to apparent homogeneity from rabbit erythrocytes, liver, and skeletal muscle. The activator displays an M(r) of about 200,000 upon sizing chromatography and, as judged by gel electrophoresis under denaturing conditions, is composed of two species of subunit of about equal abundance and with M(r) of ...
L, Kuehn, B, Dahlmann
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Biochemistry, 2002
The proteasome is a major cytosolic proteolytic assembly, essential for the physiology of eukaryotic cells. Both the architecture and enzymatic properties of the 20S proteasome are relatively well understood. However, despite longstanding interest, the integration of structural and functional properties of the proteasome into a coherent model ...
Pawel A, Osmulski, Maria, Gaczynska
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The proteasome is a major cytosolic proteolytic assembly, essential for the physiology of eukaryotic cells. Both the architecture and enzymatic properties of the 20S proteasome are relatively well understood. However, despite longstanding interest, the integration of structural and functional properties of the proteasome into a coherent model ...
Pawel A, Osmulski, Maria, Gaczynska
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Chaperone Activities of the 26S and 20S Proteasome
Current Protein & Peptide Science, 2005The accumulation of misfolded or damaged proteins causes the failure of normal cell structure and functions necessary for growth and viability. To abort this adverse development, defective proteins must be rapidly repaired by molecular chaperones or destroyed by energy-dependent cytoplasmic proteases.
Mihiro, Yano +4 more
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1998
The 26 S proteasome—discussed in Chapter 6—is the central protease of the ubiquitin pathway of protein degradation. The core of this 2-MDa enzyme is formed by the 20 S proteasome (Peters et al., 1993), a barrel-shaped protease of about 700 kDa, which is the subject of this chapter (Fig. 1). Whereas the 26 S proteasome degrades folded proteins in an ATP-
Lupas, A., Baumeister, W.
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The 26 S proteasome—discussed in Chapter 6—is the central protease of the ubiquitin pathway of protein degradation. The core of this 2-MDa enzyme is formed by the 20 S proteasome (Peters et al., 1993), a barrel-shaped protease of about 700 kDa, which is the subject of this chapter (Fig. 1). Whereas the 26 S proteasome degrades folded proteins in an ATP-
Lupas, A., Baumeister, W.
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STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Annual Review of Biochemistry, 1996The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20S (700-kDa) proteasome contains multiple peptidase activities that function through a new type of proteolytic mechanism involving a threonine active site.
O, Coux, K, Tanaka, A L, Goldberg
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Development of lipopeptides for inhibiting 20S proteasomes
Bioorganic & Medicinal Chemistry Letters, 2006Proteasomes are responsible for the cytoplasmic turnover of the vast majority of proteins including regulatory proteins. We have synthesized lipopeptides a new class of non-covalent inhibitors of the 20S proteasome and assayed their inhibitory capacities.
Basse, Nicolas +6 more
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