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  • Nature Publishing Group  (8)
  • Annual Reviews  (6)
  • Public Library of Science  (5)
  • American Chemical Society  (2)
  • 1
    Electronic Resource
    Electronic Resource
    THE ACTION OF MOLECULAR CHAPERONES IN THE EARLY SECRETORY PATHWAY (2001)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 35 (2001), S. 149-191 
    Details
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of nearly all secreted proteins, and associated with or housed within the ER are factors required to catalyze their import into the ER and facilitate their folding. To ensure that only properly folded proteins are secreted and to temper the effects of cellular stress, the ER can target aberrant proteins for degradation and/or adapt to the accumulation of misfolded proteins. Molecular chaperones play critical roles in each of these phenomena.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.genet.35.102401.090313
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  • 2
    Electronic Resource
    Electronic Resource
    EMERGING PRINCIPLES OF CONFORMATION-BASED PRION INHERITANCE (2004)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 73 (2004), S. 617-656 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: The prion hypothesis proposes that proteins can act as infectious agents. Originally formulated to explain transmissible spongiform encephalopathies (TSEs), the prion hypothesis has been extended with the finding that several non-Mendelian traits in fungi are due to heritable changes in protein conformation, which may in some cases be beneficial. Although much remains to be learned about the specific role of cellular cofactors, mechanistic parallels between the mammalian and yeast prion phenomena point to universal features of conformation-based infection and inheritance involving propagation of ordered beta-sheet-rich protein aggregates commonly referred to as amyloid. Here we focus on two such features and discuss recent efforts to explain them in terms of the physical properties of amyloid-like aggregates. The first is prion strains, wherein chemically identical infectious particles cause distinct phenotypes. The second is barriers that often prohibit prion transmission between different species. There is increasing evidence suggesting that both of these can be manifestations of the same phenomenon: the ability of a protein to misfold into multiple self-propagating conformations. Even single mutations can change the spectrum of favored misfolded conformations. In turn, changes in amyloid conformation can shift the specificity of propagation and alter strain phenotypes. This model helps explain many common and otherwise puzzling features of prion inheritance as well as aspects of noninfectious diseases involving toxic misfolded proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biochem.72.121801.161837
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  • 3
    Electronic Resource
    Electronic Resource
    EMERGING PRINCIPLES OF CONFORMATION-BASED PRION INHERITANCE (2004)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 73 (2004), S. 617-656 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: The prion hypothesis proposes that proteins can act as infectious agents. Originally formulated to explain transmissible spongiform encephalopathies (TSEs), the prion hypothesis has been extended with the finding that several non-Mendelian traits in fungi are due to heritable changes in protein conformation, which may in some cases be beneficial. Although much remains to be learned about the specific role of cellular cofactors, mechanistic parallels between the mammalian and yeast prion phenomena point to universal features of conformation-based infection and inheritance involving propagation of ordered beta-sheet-rich protein aggregates commonly referred to as amyloid. Here we focus on two such features and discuss recent efforts to explain them in terms of the physical properties of amyloid-like aggregates. The first is prion strains, wherein chemically identical infectious particles cause distinct phenotypes. The second is barriers that often prohibit prion transmission between different species. There is increasing evidence suggesting that both of these can be manifestations of the same phenomenon: the ability of a protein to misfold into multiple self-propagating conformations. Even single mutations can change the spectrum of favored misfolded conformations. In turn, changes in amyloid conformation can shift the specificity of propagation and alter strain phenotypes. This model helps explain many common and otherwise puzzling features of prion inheritance as well as aspects of noninfectious diseases involving toxic misfolded proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biochem.72.121801.161837
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  • 4
    Electronic Resource
    Electronic Resource
    The structural basis of yeast prion strain variants (2007)
    [s.l.] : Nature Publishing Group
    Nature 449 (2007), S. 233-237 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Among the many surprises to arise from studies of prion biology, perhaps the most unexpected is the strain phenomenon whereby a single protein can misfold into structurally distinct, infectious states that cause distinguishable phenotypes. Similarly, proteins can adopt a spectrum of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature06108
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  • 5
    Electronic Resource
    Electronic Resource
    Systems Biology Many things from one (2006)
    [s.l.] : Nature Publishing Group
    Nature 444 (2006), S. 561-562 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The census bureau will tell you that the typical American family has 2.1 children, but there are no families (we hope) that precisely match this mean. Similarly, biologists have come to realize that population-based measurements can obscure critical information about cell-to-cell diversity. The use ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature05407
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  • 6
    Electronic Resource
    Electronic Resource
    The physical basis of how prion conformations determine strain phenotypes (2006)
    [s.l.] : Nature Publishing Group
    Nature 442 (2006), S. 585-589 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A principle that has emerged from studies of protein aggregation is that proteins typically can misfold into a range of different aggregated forms. Moreover, the phenotypic and pathological consequences of protein aggregation depend critically on the specific misfolded form. A striking example ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature04922
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  • 7
    Electronic Resource
    Electronic Resource
    Release of both native and non-native proteins from a cis -only GroEL ternary complex (1996)
    [s.l.] : Nature Publishing Group
    Nature 383 (1996), S. 96-99 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To produce a 'as-only' GroEL complex, which is able to bind polypeptide and GroES on only one and the same ring, we formed a mixed-ring GroEL complex, in which one ring was composed of wild-type subunits and the other of subunits with apical domain substitutions that prevent both polypeptide and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/383096a0
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  • 8
    Electronic Resource
    Electronic Resource
    Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (1993)
    [s.l.] : Nature Publishing Group
    Nature 365 (1993), S. 185-188 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The best characterized disulphide folding pathway of a protein is for the in vitro folding of BPTI7 n (Fig. \a, b). During folding at neutral pH, BPTI accumulates rapidly as one of two intermed-iates. These intermediates, termed N* and N', both contain two native disulphide bonds, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/365185a0
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  • 9
    Electronic Resource
    Electronic Resource
    Origins and kinetic consequences of diversity in Sup35 yeast prion fibers (2002)
    [s.l.] : Nature Publishing Group
    Nature structural biology 9 (2002), S. 389-396 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] A remarkable feature of prions is that infectious particles composed of the same prion protein can give rise to different phenotypes. This strain phenomenon suggests that a single prion protein can adopt multiple infectious conformations. Here we use a novel single fiber growth assay to examine the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb786
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  • 10
    Electronic Resource
    Electronic Resource
    A kinetic explanation for the rearrangement pathway of BPTI folding (1995)
    [s.l.] : Nature Publishing Group
    Nature structural biology 2 (1995), S. 1123-1130 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Bovine pancreatic trypsin inhibitor (BPTI) does not fold by simple sequential formation of its native disulphide bonds. Instead, an initially formed intermediate, termed N', first rearranges to a more stable species in a slow process that requires substantial unfolding. We find that direct ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb1295-1123
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