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Journal ArticleDOI

The ubiquitin-proteasome proteolytic pathway

Aaron Ciechanover
- 07 Oct 1994 - 
- Vol. 79, Iss: 1, pp 13-21
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TLDR
Two studies clearly demonstrate that the ubiquitin-proteasome system is involved not only in complete destruction of its protein substrates, but also in limited proteolysis and posttranslational processing in which biologically active peptides or fragments are generated.
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This article is published in Cell.The article was published on 1994-10-07. It has received 1783 citations till now. The article focuses on the topics: Ubiquitin ligase & Proteasome.

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Citations
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Journal ArticleDOI

The Ubiquitin System

TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
Journal ArticleDOI

NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses

TL;DR: Recently, significant advances have been made in elucidating the details of the pathways through which signals are transmitted to the NF-kappa B:I kappa B complex in the cytosol and their implications for the study of NF-Kappa B.
Journal ArticleDOI

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

TL;DR: Mutations in the newly identified gene appear to be responsible for the pathogenesis of Autosomal recessive juvenile parkinsonism, and the protein product is named ‘Parkin’.
Journal ArticleDOI

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

TL;DR: It is clear now that degradation of cellular proteins is a highly complex, temporally controlled, and tightly regulated process that plays major roles in a variety of basic pathways during cell life and death as well as in health and disease.
Journal ArticleDOI

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

TL;DR: The mechanism of mitochondrial RIRR highlights the central role of mitochondria-formed ROS, and all of the known ROS-producing sites and their relevance to the mitochondrial ROS production in vivo are discussed.
References
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Journal ArticleDOI

The Ubiquitin System

TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
Journal ArticleDOI

The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53

TL;DR: It is demonstrated that the E6 proteins of the oncogenic HPVs that bind p53 stimulate the degradation of p53, which results in selective degradation of cellular proteins such as p53 with negative regulatory functions provides a novel mechanism of action for dominant-acting oncoproteins.
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Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis

TL;DR: The rapid degradation of injected alpha- and beta-casein as well as the inverse correlation of PEST regions with intracellular stability indicate that the presence of these regions can result in the rapid intrace cellular degradation of the proteins containing them.
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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

TL;DR: Peptide aldehydes that inhibit major peptidase activities of the 20S and 26S proteasomes are shown to reduce the degradation of protein and ubiquitinated protein substrates by 26S particles.
Journal ArticleDOI

Cyclin is degraded by the ubiquitin pathway

TL;DR: Cyclin degradation is the key step governing exit from mitosis and progress into the next cell cycle, and anaphase may be triggered by the recognition of cyclin by the ubiquitin-conjugating system.
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