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  • 1
    Electronic Resource
    Electronic Resource
    Heats of Formation of α-Phase Silver-Cadmium Alloys (1958)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 62 (1958), S. 325-326 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j150561a019
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  • 2
    Electronic Resource
    Electronic Resource
    DEGRADATION OF CELL PROTEINS AND THE GENERATION OF MHC CLASS I-PRESENTED PEPTIDES (1999)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Immunology 17 (1999), S. 739-779 
    Details
    ISSN: 0732-0582
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Major histocompatibility complex (MHC) class I molecules display on the cell surface 8- to 10-residue peptides derived from the spectrum of proteins expressed in the cells. By screening for non-self MHC-bound peptides, the immune system identifies and then can eliminate cells that are producing viral or mutant proteins. These antigenic peptides are generated as side products in the continual turnover of intracellular proteins, which occurs primarily by the ubiquitin-proteasome pathway. Most of the oligopeptides generated by the proteasome are further degraded by distinct endopeptidases and aminopeptidases into amino acids, which are used for new protein synthesis or energy production. However, a fraction of these peptides escape complete destruction and after transport into the endoplasmic reticulum are bound by MHC class I molecules and delivered to the cell surface. Herein we review recent discoveries about the proteolytic systems that degrade cell proteins, how the ubiquitin-proteasome pathway generates the peptides presented on MHC-class I molecules, and how this process is stimulated by immune modifiers to enhance antigen presentation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.immunol.17.1.739
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  • 3
    Electronic Resource
    Electronic Resource
    Proteolysis and class I major histocompatibility complex antigen presentation (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Immunological reviews 172 (1999), S. 0 
    Details
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary: The class I major histocompatibility complex (MHC class 1) presents 8–10 residue peptides to cytotoxic T lymphocytes. Most of these antigenic peptides are generated during protein degradation in the cytoplasm and are then transported into the endoplasmic reticulum by the transporter associated with antigen processing (TAP), Several lines of evidence have indicated that the proteasome is the major proteolytic activity responsible for generation of antigenic peptides—probably most conclusive has been the finding that specific inhibitors of die proteasome block antigen presentation. However, other proteases (e.g. the signal peptidase) may also generate some epitopes, particularly those on certain MHC class I alleles. The proteasome is responsible for generating the precise C termini of many presented peptides, and appears to be the only activity in ceils that can make this cleavage. In contrast, aminopeptidases in the cytoplasm and endoplasmic reticulum can trim the N terminus of extended peptides to their proper size. Interestingly, the cellular content of proteases involved in the production and destruction of antigenic peptides is modified by inter-feron-γ (IFN-γ) treatment of cells, IFN-γ indicates the expression of three new proteasome β submits that are preferentially incorporated into new proteasomes and alter their pattern of peptidase activities. These changes are likely to enhance the yield of peptides with C termini appropriate for MHC binding and have been shown to enhance the presentation of at least some antigens. IFN-γ also upregulates leucine aminopeptidase, which should promote the removal of N-terminal flanking residues of antigenic peptides. Also, this cytokine downregulates the expression of a metallo-proteinase, thimet oligopeptidase that actively destroys many antigenic peptides. Thus, IFN-γ appears to increase the supply of peptides by stimulating their generation and decreasing their destruction. The specificity and content of these various proteases should determine the amount of peptides available for antigen presentation. Also, the efficiency with which a peptide is presented is determined by the protein's half life (e.g. its ubiquitination rate) and the sequences flanking antigenic peptides, which influence the rates of proteolytic cleavage and destruction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-065X.1999.tb01355.x
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  • 4
    Electronic Resource
    Electronic Resource
    EFFECTS OF USE AND DISUSE ON AMINO ACID TRANSPORT AND PROTEIN TURNOVER IN MUSCLE (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 228 (1974), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1974.tb20510.x
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  • 5
    Electronic Resource
    Electronic Resource
    Probing the proteasome pathway (2000)
    [s.l.] : Nature America Inc.
    Nature biotechnology 18 (2000), S. 494-496 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] The degradation of intracellular proteins is a complex process involving in eukaryotes a very large proteolytic complex—the 26S proteasome—and a multistep pathway involving the cofactor ubiquitin that provides exquisite selectivity and precise regulation. In recent years, major ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/75349
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  • 6
    Electronic Resource
    Electronic Resource
    Structural properties of rat serum proteins which correlate with their degradative rates in vivo (1976)
    [s.l.] : Nature Publishing Group
    Nature 262 (1976), S. 514-516 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] There is now strong evidence that the degradative rates of intracellular proteins are determined to a large extent by their conformations5,6. For example, in both animal and bacterial cells, the catabolic rates of different proteins correlate with their relative sensitivities in vitro to purified ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/262514a0
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  • 7
    Electronic Resource
    Electronic Resource
    E. coli contains eight soluble proteolytic activities, one being ATP dependent (1981)
    [s.l.] : Nature Publishing Group
    Nature 292 (1981), S. 652-654 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Although several reports have concerned the isolation of proteases from E. coli, this field is in a confusing state. The so-called 'protease T and 'protease II', which cleave chromo-genic substrates for chymotrypsin and trypsin respectively16'17, show little or no hydrolytic activity against ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/292652a0
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  • 8
    Electronic Resource
    Electronic Resource
    Influence of Heating Rate on Transformations in an 18 per cent Nickel Maraging Steel (1967)
    [s.l.] : Nature Publishing Group
    Nature 213 (1967), S. 170-171 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Heating curves for annealed wire and cylindrical specimens are shown in Figs. 1 and 2, respectively. The inflexion points, denoted by TA, TB, Tc, and TE, are plotted as a function of heating rate in Fig. 3. Up to 40 F/sec these points are displaced to higher temperatures with higher heating rates, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/213170a0
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  • 9
    Electronic Resource
    Electronic Resource
    Protein degradation and protection against misfolded or damaged proteins (2003)
    [s.l.] : Nature Publishing Group
    Nature 426 (2003), S. 895-899 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The ultimate mechanism that cells use to ensure the quality of intracellular proteins is the selective destruction of misfolded or damaged polypeptides. In eukaryotic cells, the large ATP-dependent proteolytic machine, the 26S proteasome, prevents the accumulation of non-functional, potentially ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature02263
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  • 10
    Electronic Resource
    Electronic Resource
    Not just research tools—proteasome inhibitors offer therapeutic promise (2002)
    [s.l.] : Nature Publishing Group
    Nature medicine 8 (2002), S. 338-340 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Twenty-five years ago, mammalian cells were shown to contain a highly unusual system for the selective degradation of proteins, now known as the ubiquitin-proteasome pathway. This system was shown to require ATP, unlike any proteolytic enzyme then known, and is not membrane-enclosed, unlike ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0402-338
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