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  • 1
    Electronic Resource
    Electronic Resource
    THE UBIQUITIN SYSTEM (1998)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 67 (1998), S. 425-479 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: Abstract The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes, including cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, and endocytosis. The ubiquitin system has been implicated in the immune response, development, and programmed cell death. Abnormalities in ubiquitin-mediated processes have been shown to cause pathological conditions, including malignant transformation. In this review we discuss recent information on functions and mechanisms of the ubiquitin system. Since the selectivity of protein degradation is determined mainly at the stage of ligation to ubiquitin, special attention is focused on what we know, and would like to know, about the mode of action of ubiquitin-protein ligation systems and about signals in proteins recognized by these systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biochem.67.1.425
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  • 2
    Electronic Resource
    Electronic Resource
    The ubiquitin system (2000)
    [s.l.] : Nature America Inc.
    Nature medicine 6 (2000), S. 1073-1081 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Ubiquitin-mediated protein degradation: The early days Avram Hershko It has been often stated that until recently the ubiquitin system was thought to be mainly a ‘garbage disposal’ for the removal of abnormal or damaged proteins. This statement is certainly not true for those who have ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/80384
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  • 3
    Electronic Resource
    Electronic Resource
    Ubiquitin–mediated proteolysis and male sterility (1996)
    [s.l.] : Nature Publishing Group
    Nature medicine 2 (1996), S. 1188-1190 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Studies in cultured mammalian cells and in yeast have shown that the ubiquitin proteolytic pathway is involved in the regulation of a wide array of fundamental cellular processes including the cell cycle, circadian rhythms, the stress response, morphogenesis of the central nervous system, protein ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm1196-1188
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  • 4
    Electronic Resource
    Electronic Resource
    Linking ubiquitin, parkin and synphilin-1 (2001)
    [s.l.] : Nature Publishing Group
    Nature medicine 7 (2001), S. 1108-1109 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The ubiquitin- and proteasome-mediated degradation of certain intracellular proteins is fundamental to the regulation of basic cellular processes, such as cell-cycle progression, growth and differentiation, as well as the immune and inflammatory responses. The ubiquitin proteolytic system (UPS) ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm1001-1108
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  • 5
    Electronic Resource
    Electronic Resource
    Role of arginine-tRNA in protein degradation by the ubiquitin pathway (1987)
    [s.l.] : Nature Publishing Group
    Nature 326 (1987), S. 808-811 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A nonlysosomal, ATP-dependent proteolytic system from rabbit reticulocytes has been recently characterized and partially purified. One of the components of the system has been identified as ubiquitin9'10, an evolutionarily highly conserved polypep-tide11'13. Ubiquitin becomes conjugated to proteins ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/326808a0
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  • 6
    Electronic Resource
    Electronic Resource
    Ubiquitin-mediated degradation of tyrosine aminotransferase (TAT) in vitro and in vivo (1997)
    Springer
    Molecular biology reports 24 (1997), S. 27-33 
    Details
    ISSN: 1573-4978
    Keywords: ubiquitin ; proteolysis ; tyrosine aminotransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Degradation of a protein via the ubiquitin proteolytic pathway involves two successive steps. Covalent attachment of ubiquitin to the target protein and degradation of the tagged substrate by the 26S proteasome. Most native cellular proteins that are targeted by the ubiquitin system are short-lived transcriptional activators and growth and cell cycle regulators, as well as unstable membrane proteins. In the present study we demonstrate the involvement of the system in the degradation of tyrosine aminotransferase (TAT), a key enzyme in intermediary metabolism. In vitro, we have shown that the native enzyme is conjugated and degraded in a system that requires ATP and ubiquitin. Degradation was monitored by following the decrease of catalytic activity as well as disappearance of the protein molecule. The enzyme could be protected from degradation by association with its specific cofactor, pyridoxal phosphate (PLP). In vivo, we prepared cell extracts from livers of animals in which TAT was induced by starvation and corticosteroid administration. The dramatic increase in the level of the enzyme was accompanied by a concomitant increase in the level of specific TAT-ubiquitin adducts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006896321905
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  • 7
    Electronic Resource
    Electronic Resource
    Degradation of MyoD by the ubiquitin pathway: regulation by specific DNA-binding and identification of a novel site for ubiquitination (1999)
    Springer
    Molecular biology reports 26 (1999), S. 59-64 
    Details
    ISSN: 1573-4978
    Keywords: MyoD ; ubiquitin ; proteolysis ; DNA binding ; N-terminus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract MyoD is a tissue-specific transcriptional activator involvd in skeletal muscle differentiation. It is induced during transition from proliferating, non-differentiated myoblasts to the resting and well differentiated myotubes. Like many other transcriptional regulators, it is short-lived, however, the targeting proteolytic pathway and the underlying regulatory mechanisms involved have remained obscure. Here we show that MyoD is degraded by the ubiquitin system both in vivo and in vitro. In cells, degradation is inhibited by lactacystin, a specific inhibitor of the 20S proteasome. Inhibition is accompanied by accumulation of MyoD-ubiquitin conjugates. In a cell free system, the proteolytic process requires both ATP and ubiquitin and is preceded by formation of MyoD-ubiquitin adducts. Interestingly, the process is inhibited by the specific DNA sequence to which MyoD binds. Analysis of the ubiquitination site has revealed that the N-terminal residue of MyoD is sufficient and essential to promote conjugation and subsequent degradation of the protein: conjugation to internal Lys residues is not necessary. Substitution of all Lys residues did not affect significantly its degradation either in intact cells or in a reconstituted cell free system. Degradation was inhibited by specific proteasome inhibitors and was accompanied by accumulation of ubiquitinated species of the protein. We concluded that the first ubiquitin moiety is attached via its C-terminal Gly to the N-terminal residue of MyoD, and the polyubiquitin chain is then synthesized on Lys48 of this moiety.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006964122190
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  • 8
    Electronic Resource
    Electronic Resource
    Regulation of the ubiquitin-mediated proteolytic pathway: Role of the substrate α-NH2 group and of transfer RNA (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 34 (1987), S. 81-100 
    Details
    ISSN: 0730-2312
    Keywords: ubiquitin ; α-NH2 group ; transfer RNA ; proteolytic pathway ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Degradation of intracellular proteins via the ubiquitin pathway involves several steps. In the initial event, ubiquitin becomes covalently linked to the protein substrate in an ATP-requiring reaction. Following ubiquitin conjugation, the protein moiety of the adduct is selectively degraded with the release of free and reusable ubiquitin. Ubiquitin modification of a variety of protein targets in the cell plays a role in basic cellular functions. Modification of core nucleosomal histones is probably involved in regulation of gene expression at the level of chromatin structure. Ubiquitin attachment to cell surface proteins may play roles in processes of cell-cell interaction and adhesion, and conjugation of ubiquitin to other yet to be identified protein(s) could be involved in the progression of cells through the cell cycle. Despite the considerable progress that has been made in the elucidation of the mode of action and cellular roles of the ubiquitin pathway, many major problems remain unsolved. A problem f central importance is the specificity in the ubiquitin ligation system. Why are certain proteins conjugated and committed for degradation, whereas other proteins are not? A free α-NH2 group is an important feature of the protein structure recognized by the ubiquitin conjugation system, and tRNA is required for the conjugation of ubiquitin to selective proteo-lytic substrates and for their subsequent degradation. These findings can shed light on some of the features of a substrate that render it susceptile to ubiquitin-mediated degradation.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240340203
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  • 9
    Electronic Resource
    Electronic Resource
    Sorting and recycling of cell surface receptors and endocytosed ligands: The asialoglycoprotein and transferrin receptors (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 23 (1983), S. 107-130 
    Details
    ISSN: 0730-2312
    Keywords: receptor recycling ; asialoglycoproteins ; transferring ; iron delivery ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: With few exceptions, receptor-mediated endocytosis of specific ligands is mediated through clustering of receptor-ligand complexes in coated pits on the cell surface, followed by internalizalion of the complex into endocytic vesicles. During this process, ligand-receptor dissociation occurs, most probably in a low pH prelysosomal compartment. In most cases the ligand is ultimately directed to the lysosomes, wherein it is degraded, while the receptor recycles to the cell surface.We have studied the kinetics of internalization and recycling of both the asialoglycoprotein receptor and the transferrin receptor in a human hepatoma cell line. By employing both biochemical and morphological/immunocytochemical approaches, we have gained some insight into the complex mechanisms which govern receptor recycling as well as ligand sorting and targeting. We can, in particular, explain why transferrin is exocytosed intact from the cells, while asialoglycoprotcins are degraded in lysosomes. We have also localized the intra-cellular site at which endocylosed receptor and ligand dissociate.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240230111
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  • 10
    Electronic Resource
    Electronic Resource
    The ubiquitin-mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation (1984)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 24 (1984), S. 27-53 
    Details
    ISSN: 0730-2312
    Keywords: ubiquitin ; intracellular protein degradation ; chromosome function ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: In this review we briefly describe the lysosomal system, consider the evidence for multiplicity of protein degradation pathways in vivo, discuss in detail the ubiquitin-mediated pathway of intracellular ATP-dependent protein degradation, and also the possible significance of ubiquitin-histone conjugates in chromatin. For detailed discussions of the various characteristics and physiological roles of intracellular protein breakdown, the reader is referred to earlier reviews [1-7] and reports of recent symposia [8-10]. Information on the ubiquitin system prior to 1981 was described in an earlier review [11]. Hershko has briefly reviewed more recent information [12].
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240240104
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