Results 221 to 230 of about 27,758 (248)
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Degradation of Ornithine Decarboxylase by the 26S Proteasome
Biochemical and Biophysical Research Communications, 2000Ornithine decarboxylase (ODC) is a key enzyme in polyamine biosynthesis. Turnover of ODC is extremely rapid and highly regulated, and is accelerated when polyamine levels increase. Polyamine-stimulated ODC degradation is mediated by association with antizyme (AZ), an ODC inhibitory protein induced by polyamines. ODC, in association with AZ, is degraded
Y, Murakami +4 more
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Targeting of substrates to the 26S proteasome
The FASEB Journal, 1997The ubiquitin‐proteasome pathway is the principal mechanism for the turnover of shortlived proteins in eukaryotic cells. In this pathway, the covalent ligation of ubiquitin to the substrate is a signal for recognition by the 26S proteasome.
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THE UBIQUITIN 26S PROTEASOME PROTEOLYTIC PATHWAY
Annual Review of Plant Biology, 2004▪ Abstract Much of plant physiology, growth, and development is controlled by the selective removal of short-lived regulatory proteins. One important proteolytic pathway involves the small protein ubiquitin (Ub) and the 26S proteasome, a 2-MDa protease complex.
Jan, Smalle, Richard D, Vierstra
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Viruses and the 26S proteasome: hacking into destruction
Trends in Biochemical Sciences, 2003The discovery that the human papillomavirus E6 oncoprotein could direct the ubiquitination and degradation of the p53 tumour suppressor at the 26S proteasome was the beginning of a new view on virus-host interactions. A decade later, a plethora of viral proteins have been shown to direct host-cell proteins for proteolytic degradation.
Lawrence, Banks +2 more
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Proteasomes. A molecular census of 26S proteasomes in intact neurons.
Science (New York, N.Y.), 2015The 26S proteasome is a key player in eukaryotic protein quality control and in the regulation of numerous cellular processes. Here, we describe quantitative in situ structural studies of this highly dynamic molecular machine in intact hippocampal neurons.
Asano, Shoh +6 more
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The 26S-proteasome: regulation and substrate recognition
Molecular Biology Reports, 1997There is extensive reprogramming of the ATPase regulators of the 26S proteasome before the programmed elimination of the abdominal intersegmental muscles (ISM) after eclosion in Manduca sexta [1]. This extensive ATPase reprogramming only occurs in ISM which are destined to die and not in flight muscle (FM).
S, Dawson +6 more
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Molecular Structures of 20S and 26S Proteasomes
Enzyme and Protein, 2017Eukaryotic proteasomes are unusually large protein complexes with characteristic sets of subunits and have been classified into two isoforms with apparent sedimentation coefficients of 20S and 26S, respectively. The 20S proteasome (previously named the multicatalytic proteinase complex) is a cylindrical particle with a molecular weight (MW) of ...
N, Tanahashi +3 more
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An atomic structure of the human 26S proteasome
Nature Structural & Molecular Biology, 2016We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent α subunits in the ...
Xiuliang, Huang +3 more
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1998
The 26 S proteasome is a large multisubunit complex that degrades intracellular proteins in a nucleotide-dependent reaction. The enzyme is composed of about 30 different proteins. Fourteen subunits are provided by the proteasome and an additional 16 or more subunits are present in a particle that I will call the regulatory complex.
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The 26 S proteasome is a large multisubunit complex that degrades intracellular proteins in a nucleotide-dependent reaction. The enzyme is composed of about 30 different proteins. Fourteen subunits are provided by the proteasome and an additional 16 or more subunits are present in a particle that I will call the regulatory complex.
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Assembly of the regulatory complex of the 26S proteasome
Molecular Biology Reports, 1999The 19S regulatory complex (RC) of 26S proteasomes is a 900-1000 kDa particle composed of 18 distinct subunits (S1-S15) ranging in molecular mass from 25 to 110 kDa. This particle confers ATP-dependence and polyubiquitin (polyUb) recognition to the 26S proteasome.
Gorbea, C. +2 more
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