Amyloidogenic

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. 

Dyrks, T., Dyrks, E., Hartmann, T., Masters, C.L. and Beyreuther, K. (1992). Amyloidogenicity of d A4 and /3 A4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J. Biol. Chem. 267, 18210-18217. 

Bonifacio MJ, Sakaki Y, Saraiva MJ. In vitro amyloid fibril formation from transthyretin the influence of ions and the amyloidogenicity of TTR variants. Biochim Biophys Acta 1996 1316 35 42. 

Jarrett JT, Lansbury PT Jr. Amyloid fibril formation requires a chemically discriminating nucleation event studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 1992 31 12345-12352. 

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

The ROA spectra of native and prehbrillar amyloidogenic human lysozyme are displayed in Figure 7, together with a MOLSCRIPT diagram of the native structure. The ROA spectrum of the native protein is very similar to that of hen lysozyme (Fig. 5). However, large changes have occurred in the ROA spectrum of the prehbrillar intermediate. In particular, the positive 1340 cm-1 ROA band assigned to hydrated... 

Lindgren M, Sorgjerd K, Hammarstrom P (2005) Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy. Biophys J 88(6) 4200-4212... 

Cultured macrophages are able to rapidly refold A 3 peptide into its amyloidogenic conformation, which also supports the hypothesis that macrophages play a causal role in the generation of the plaque core [12,13]. Macrophage-facilitated refolding of amyloidogenic peptides... 

A comparable folding mechanism was found in silks. A seminal study by Li et al. (2001) found that in vitro formation of silk fibrils is conformation dependent and occurred via a nucleation mechanism. Although now established as amyloidogenic (Kenney et al., 2002), the nature of the silk fibril assembly remains unclear. Noteworthy is the evidence for a cross-nucleation ability of silk proteins, supporting the amyloidogenicity of silk (Lundmark et al., 2005). 

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

F, Prediction of Amyloidogenic Regions and Structures of Amyloid Fibrils... 

In view of the consideration that /(-solenoids and /(-arcades may also be structural elements of amyloid fibrils (Kajava et al., 2004 Lazo and Downing, 1998 Margittai and Langen, 2004 Pickersgill, 2003), sequence-based detection and structure prediction of /(-solenoid proteins are pertinent to the identification of amyloidogenic sequences and the elucidation of amyloid fibril structures. As with /(-solenoid domains, amyloidogenic regions of... 

In this context, it is an interesting open question whether natural amyloids (Section IV.A) first form by polymerization of amyloidogenic domains of the full-length proteins whose other domains are subsequendy digested away or whether these proteins are first degraded to fragments that then assemble into amyloid filaments. 

F., and Salmona, M. (1994). Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. / Biol. Chem. 269, 7859-7862. 

Reches, M., and Gazit, E. (2004). Amyloidogenic hexapeptide fragment of medin Homology to functional islet amyloid polypeptide fragments. Amyloid 11, 81-89. 

Tenidis, K., Waldner, M., Bemhagen.J., Fischle, W., Bergmann, M., Weber, M., Merkle, M. L., Voelter, W., Brunner, H., and Kapumiotu, A. (2000). Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. / Mol. Biol. 295, 1055-1071. 

Tsai, H. H., Reches, M., Tsai, C.J., Gunasekaran, K., Gazit, E., and Nussinov, R. (2005). Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation Significant role of Asn ladder. Proc. Natl. Acad. Sci. USA 102, 8174-8179. 

Green, J. D., Kreplak, L., Goldsbury, C., Li Blatter, X., Stolz, M., Cooper, G. S., Seelig, A., Kisder.J., and Aebi, U. (2004b). Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide. / Mol. Biol. 342, 877-887. 

Huff, M. E., Balch, W. E., and Kelly, J. W. (2003). Pathological and functional amyloid formation orchestrated by the secretory pathway. Curr. Opin. Struct. Biol. 13, 674-682. Jansen, R., Dzwolak, W., and Winter, R. (2005). Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 88, 1344-1353. 

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