Fibrillogenesis

Lansbury P T 1999 Evolution of amyloids What normal protein folding oan tell us about fibrillogenesis and disease Proc. Nati Acad. Sci. (USA) 96 3342-4... 

Synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson s disease. J Biol Chem 1999 274 19509-19512. 

Charge SB, de Koning EJ, Clark A. Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro. Biochemistry 1995 34 14588-14593. 

Fraser PE, McLachlan DR, Surewicz WK, Mizzen CA, Snow AD, Nguyen JT, Kirschner DA. Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues. J Mol Biol 1994 244 64-73. 

Soto C, Castano EM, Kumar RA, Beavis RC, Frangione B. Fibrillogenesis of synthetic amyloid-beta peptides is dependent on their initial secondary structure. Neurosci Lett 1995 200 105-108. 

Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid beta-protein. Proc Natl Acad Sci USA 1997 94 7942-7947. 

Walsh DM, Hartley DM, Kusomoto Y, Fezoui Y, Condron MM, Lomakin A, Benedek GB, Selkoe DJ, Teplow DB. Amyloid fi-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999 274 25949-25952. 

Nybo M, Svehag SE, Holm Nielsen E. An ultrastructural study of amyloid intermediates in A beta(l-42) fibrillogenesis. Scand J Immunol 1999 49 219-223. 

Pappolla M, Bozner P, Soto C, Shao H, Robakis NK, Zagorski M, Frangione B, Ghiso J. Inhibition of Alzheimer beta-fibrillogenesis by melatonin. J Biol Chem 1998 273 7185-7188. 

Inouye, H., and Kirschner, D. A. (2000). A // fibrillogenesis Kinetic parameters for fibril formation from Congo red binding./ Struct. Biol. 130, 123-129. 

Cardoso, I., Goldsbury, C. S., Muller, S. A., Olivieri, V., Wirtz, S., Damas, A. M., Aebi, U., and Saraiva, M. J. (2002). Transthyretin fibrillogenesis entails the assembly of monomers A molecular model for in vitro assembled transthyretin amyloid-like fibrils./. Mol. Biol. 317, 683-695. 

Rochet, J. C., and Lansbury, P. T., Jr. (2000). Amyloid fibrillogenesis Themes and variations. Curr. Opin. Struct. Biol. 10, 60-68. 

The discovery of inhibitors of fibrillogenesis has been hampered by the complexity of the folding pathway, the presence of mixed populations of aggregates, and the lack of sensitive markers of each oligomeric species.40 Screening assays based on thioflavin-S fluorescence or Congo-red absorbance have been used to identify inhibitors of aggregation of synthetic Af peptide. The reported compounds suffer from relatively low potency (effective at <10 pM) and "flat" SARs." 43... 

Tau protein interacts with many other proteins that can contribute to abnormal fibrillogenesis. One example is a-synuclein, which induces fibrillization of tau. Coincubation of a-synnclein and tau synergistically promotes fibrillization of both proteins in vitro. Mice with a-synuclein mutation or a tau mutation exhibit filamen-tons inclusions of both proteins, which are abundant neuronal proteins that normally adopt an nnfolded conformation but polymerize into amyloid fibrils in... 

Takahashi Y, Ueno A, MiharaH. Design of a peptide undergoing a-p structrual transition and amyloid fibrillogenesis by the introduction of a hydrophobic defect. Chem Eur J 1998 4 2475-2484. 

Pandya, M. J., Spooner, G. M., Sunde, M., Thorpe, J. R., Rodger, A., and Woolfson, D. N. (2000). Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis. Biochemistry 39, 8728-8734. 

Herrmann, H., and Aebi, U. (1998a). Intermediate filament assembly Fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol. 8, 177-185. 

Work by Haston et al. (2002) also indicates that acidic glycoprotein (AGP) influences Type II collagen fibrillogenesis, where in vitro studies show that low concentrations of AGP produced decreases in fibrillogenesis rate and fibril diameter. High concentrations produced fibrils at a rate and diameter dependent on fucosylation of AGP. Highly fucosylated AGP produced narrow fibrils, and poorly fucosylated AGP produced thicker fibrils. 

Collagen fibrillogenesis in situ Fibril segments become long fibrils as the developing tendon matures. Dev. Dynam. 208, 291-298. 

Helseth, D. L., Jr., Lechner, J. H., and Veis, A. (1979). Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis. Biopolymers 18, 3005-3014. 

Linsenmayer, T. F., Gibney, E., Igoe, F., Gordon, M. K., Fitch, J. M., Fessler, L. I., and Birk, D. E. (1993). Type-V collagen Molecular-structure and fibrillar organization of the chicken alpha-1 (V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis./. Cell Biol. 121, 1181-1189. 

McBride, D.J., Choe, V., Shapiro, J. R., and Brodsky, B. (1997). Altered collagen structure in mouse tail tendon lacking the alpha 2(1) chain./. Mol. Biol. 270, 275-284. Malone, J. P., George, A., and Veis, A. (2004). Type I collagen N-telopeptides adopt an ordered structure when docked to their helix receptor during fibrillogenesis. 

Otter, A., Scott, P. G., and Kotovych, G. (1988). Type-I collagen a-lchain C-telopep-tide—Solution structure determined by 600 MHz proton NMR spectroscopy and implications for its role in collagen fibrillogenesis. Biochemistry 27, 3560-3567. 

Parkinson, J., Kadler, K. E., and Brass, A. (1995). Simple physical model of collagen fibrillogenesis based on diffusion-limited aggregation./. Mol. Biol. 247, 823-831. 

Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and non elastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers. Microfibril arrays are also abundant in dynamic tissues that do not express elastin, such as the ciliary zonules of the eye. Mutations in fibrillin-1—the principal structural component of microfibrils—cause Marfan syndrome, a heritable disease with severe aortic, ocular, and skeletal defects. Isolated fibrillin-rich microfibrils have a complex 56 nm beads-on-a-string appearance the molecular basis of their assembly and... 

In particular, conditions of Aft overproduction or impaired cerebral Aft clearance mechanisms result in elevated Aft levels that promote Aft aggregation, oligomerization, and fibrillogenesis [20]. Deposition of Aft in an insoluble beta-pleated conformation (amyloid) occurs as plaques in the neuropil and as amyloid angiopathy in the cerebral vasculature. The deposition of amyloid initiates a cascade of injurious events, including free radical production, glial activation, and direct neuronal damage. Kinase activation in response to amyloid-induced injury may increase the amount... 

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