Results 211 to 220 of about 27,758 (248)
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2002
Despite the fact that the composition of proteasomes purified from different species is almost identical, and the basic components of the proteasome are remarkably conserved among all eukaryotes, there are quite a few additional proteins that show up in certain purifications or in certain screens.
M H, Glickman, V, Maytal
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Despite the fact that the composition of proteasomes purified from different species is almost identical, and the basic components of the proteasome are remarkably conserved among all eukaryotes, there are quite a few additional proteins that show up in certain purifications or in certain screens.
M H, Glickman, V, Maytal
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The 26S proteasome: a dynamic structure
Molecular Biology Reports, 1997The proteasomal system consists of a proteolytic core, the 20S proteasome, which associates in ATP-dependent and independent reactions with endogenous regulators providing specific substrate binding sites, chaperone function and regulation of activity to the protease.
M, Seeger, K, Ferrell, W, Dubiel
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The 26S proteasome: subunits and functions
Molecular Biology Reports, 1997The 26S proteasome is an eukaryotic ATP-dependent, dumbbell-shaped protease complex with a molecular mass of approximately 2000 kDa. It consists of a central 20S proteasome, functioning as a catalytic machine, and two large V-shaped terminal modules, having possible regulatory roles, composed of multiple subunits of 25-110 kDa attached to the central ...
K, Tanaka, C, Tsurumi
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Structural Features of 26S and 20S Proteasomes
Enzyme and Protein, 2017The 26S proteasome is the central protease of the ubiquitindependent pathway of protein degradation and has a highly conserved structure from slime molds to humans. The elongated molecule which has a molecular mass of approximately 2,000 kD is formed by a barrel-shaped 20S core complex and two polar 19S complexes. The 20S complex has C2 symmetry and is
Lupas, A. ; https://orcid.org/0000-0002-1959-4836 +2 more
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Ubiquitinated proteasome inhibitor is a component of the 26 S proteasome complex
Biochemistry, 1992Western blot analysis, using a polyclonal antibody to the 240-kDa endogenous inhibitor of the 20 S proteasome, revealed that the inhibitor is a component of the 26 S complex. Although isolated inhibitor displayed a single 40-kDa band on SDS-PAGE, the antibody detected a 55-kDa component in the 26 S proteasome complex.
X S, Li, J D, Etlinger
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2002
The field of intracellular proteolysis has received increasing attention over the last decade. This is due in large part to the fact that, beyond its classical functions that have been acknowledged for a long time, such as destruction of abnormal proteins or cleavage of precursor polypeptides, it was realized during the 1990s that intracellular ...
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The field of intracellular proteolysis has received increasing attention over the last decade. This is due in large part to the fact that, beyond its classical functions that have been acknowledged for a long time, such as destruction of abnormal proteins or cleavage of precursor polypeptides, it was realized during the 1990s that intracellular ...
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Phosphorylation and Ubiquitination of the 26S Proteasome Complex
Enzyme and Protein, 2017This article reviews recent studies from our laboratory on protein regulators of the proteasome (multicatalytic proteasome complex) in red blood cells. A 240-kD inhibitory component (CF-2) exists in 26S proteasome complexes in a form which is conjugated to ubiquitin.
J D, Etlinger, S X, Li, G G, Guo, N, Li
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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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Molecular mechanisms for activation of the 26S proteasome
2023Summary Various hormones, kinases, and stressors (fasting, heat shock) stimulate 26S proteasome activity. To understand how its capacity to degrade ubiquitylated protein can increase, we studied ZFAND5, which promotes protein degradation during muscle atrophy.
Donghoon, Lee +9 more
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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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