Results 241 to 250 of about 80,587 (292)
Advanced Science, EarlyView.A tiny RNA tips the scales of cardiac injury in aging. piR‐4913 recruits OGT to Drp1 and drives its O‐GlcNAcylation at Thr604, promoting excessive mitochondrial fission that aggravates ischemia‐reperfusion injury. Ischemic postconditioning silences this pathway to restore mitochondrial balance and protect the aged myocardium, revealing piR‐4913 as a ...
Xiangyu Zhao +11 more
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Characterization of Fully Recombinant Human 20S and 20S-PA200 Proteasome Complexes
Molecular Cell, 2019 Proteasomes are essential in all eukaryotic cells. However, their function and regulation remain considerably elusive, particularly those of less abundant variants.
Paula Da Fonseca, Ana Toste Rêgo
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Biochimie, 2001
26S proteasomes are multi-subunit protease complexes responsible for the turnover of short-lived proteins. Proteasomal degradation starts with the autocatalytic maturation of the 20S core particle. Here, we summarize different models of proteasome assembly.
E, Krüger, P M, Kloetzel, C, Enenkel
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26S proteasomes are multi-subunit protease complexes responsible for the turnover of short-lived proteins. Proteasomal degradation starts with the autocatalytic maturation of the 20S core particle. Here, we summarize different models of proteasome assembly.
E, Krüger, P M, Kloetzel, C, Enenkel
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Autocatalytic processing of the 20S proteasome
Nature, 1996The Ntn (N-terminal nucleophile) hydrolases are enzymes with an unusual four-layer alpha + beta fold. The amino-terminal residue (cysteine, serine or threonine) of the mature protein is the catalytic nucleophile, and its side chain is activated for nucleophilic attack by transfer of its proton to the free N terminus, although other active-site residues
Seemüller, E. +2 more
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In vitro Activation of the 20S Proteasome
Enzyme and Protein, 2017The effect of chemical compounds like sodium dodecyl sulfate (SDS), fatty acid esters of glycerol, carnitine and coenzyme A, phospholipids, histones, polylysines as well as homobifunctional chemical cross-linkers on the various proteolytic activities of mammalian proteasomes have been tested. Most of the reagents enhance these activities, and some, e.g.
B, Dahlmann +5 more
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Regulation of Autophagic Flux by the 20S Proteasome [PDF]
Cell Chemical Biology, 2019 The proteolytic arm of the protein homeostasis network is maintained by both the ubiquitin-proteasome system (UPS) and autophagy. A well-balanced crosstalk between the two catabolic pathways ensures energy-efficient maintenance of cellular function. Our current understanding of the crosstalk between the UPS and autophagy is centered around substrate ...
Jetze J Tepe
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Purification of 20S Proteasomes
2003Proteasomes are large multicatalytic proteinases located in the nuclei and cytoplasm of all eukaryotic cells. Proteasomes are composed of four heptameric rings stacked to form a hollow cylinder (length 16–20 nm, diameter 11–12 nm). The outer two rings are composed of α-subunits, while β-subunits, which contain the active sites, comprise the inner two ...
J R, Beyette, T, Hubbell, J J, Monaco
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Structure and assembly of the 20S proteasome
Cellular and Molecular Life Sciences CMLS, 1998The barrel-shaped 20S proteasome is one of the two components of a larger 26S particle, the multicatalytic 2000-kDa protease complex. The proteolytic sites are located in the inner chamber of the 20S particle and are only accessible via narrow entrances.
W L, Gerards +3 more
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Purification of the Eukaryotic 20S Proteasome
Current Protocols in Protein Science, 2001AbstractThe 20S proteasome is the catalytic core of the major extralysosomal proteolytic system of the cell. Combination of the 20S proteasome with a complex of regulatory proteins forms the 26S proteasome, which in turn is responsible for the recognition and degradation of ubiquitin‐protein conjugates.
S, Wilk, W E, Chen
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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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