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Amyloidogenic proteins

Here, two different sequences from transth3Tetin were successfully combined into mixed fibrils [54], This is not always the case, however. For amyloidogenic proteins, the ability of other fibrils to act as cross-seeds for growth is known to depend on sequence similarity [55]. Seeding hen lysozyme solutions with seeds formed from closely related sequences (e.g. hen and other lysozymes) led to the largest increases in the rate of formation of fibrils. Consequently, there may be some restrictions on the selection of distinct peptide sequences to produce scaffolds. [Pg.49]

Kelly JW (1996) Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6 11-17. [Pg.281]

Kelly, J. W. (1998). The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106. [Pg.47]

Janowski, R., Kozak, M., Jankowska, E., Grzonka, Z., Grubb, A., Abrahamson, M., and Jaskolski, M. (2001). Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat. Struct. Biol. 8, 316-320. [Pg.276]

Effect of UV Light on Amyloidogenic Proteins Nucleation and Fibril Extension... [Pg.267]

UV-Exposed Amyloidogenic Proteins Form Amyloid Upon Seeding... [Pg.280]

Janowski R, et al. Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nature Struct. Biol. 2001 8 316-320. [Pg.1605]

Kim YS, Randolph TW, Manning MC, Stevens FJ, Carpenter JF. Congo Red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Biol. Chem. 2003 278 10842-10850. [Pg.1605]

Bitan G, Teplow DB. Rapid photochemical cross-linking-a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 2004 37 357-364. [Pg.1621]

The techniques to follow aggregation of amyloidogenic proteins and to determine their molecular conformation range from spectrometric assays (thiohavin T, Congo red) over spectroscopic assays (FTIR and CD) and visualization techniques (AFM and TEM) to methods that provide detailed insight into the atomic coordinates (solid-state NMR and X-ray diffraction). [Pg.2099]

Murphy RM. Kinetics of amyloid formation and membrane in- 55. teraction with amyloidogenic proteins. Biochim. Biophys. Acta 2007 1768 1923. [Pg.2106]


See other pages where Amyloidogenic proteins is mentioned: [Pg.151]    [Pg.199]    [Pg.271]    [Pg.230]    [Pg.267]    [Pg.268]    [Pg.269]    [Pg.271]    [Pg.271]    [Pg.273]    [Pg.273]    [Pg.275]    [Pg.277]    [Pg.279]    [Pg.281]    [Pg.283]    [Pg.283]    [Pg.284]    [Pg.285]    [Pg.287]    [Pg.315]    [Pg.1602]    [Pg.1602]    [Pg.537]    [Pg.205]    [Pg.142]    [Pg.143]    [Pg.151]   
See also in sourсe #XX -- [ Pg.197 ]




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Amyloidogenic

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