Preface -- Widening Spectrum of Prions Causing Neurodegenerative Diseases (Stanley B. Prusiner).-Â{u2B41}myloid Fibril Structures, In Vitro and In Vivo (Robert Tycko).-Â{u3D32}ucture-Activity Relationship of Amyloids (Jason Greenwald and Roland Riek).-Â{u3965}ding and Cross-seeding in Amyloid Diseases (Per Westermark and Gunilla T. Westermark).-Â{u4A25} Prion-like Aspect of Alzheimer Pathology (Sarah K. Fritschi, Bahareh Eftekharzadeh, Giusi Manfredi, Tsuyoshi Hamaguchi, GÃœtz Heilbronner, Amudha Nagarathinam, Franziska Langer, Yvonne S. Eisele, Lary Walker, Mathias Jucker).-Â{u1B79}yloid-β Transmissibility (Duran-Aniotz C, Morales R, Moreno-Gonzalez I, Soto C).-Â{u0CA9}on-like Properties of Assembled Tau Protein (Florence Clavaguera, Markus Tolnay, and Michel Goedert).-Â{u18E3}cumulating Evidence Suggests that ParkinsonÂś Disease is a Prion-like Disorder -- Nolwen L. Rey, Elodie Angot, Christopher Dunning, Jennifer A. Steiner, Patrik Brundin).-Â{u0CAF}pagation and Replication of Misfolded SOD1: Implications for Amyotrophic Lateral Sclerosis (Anne Bertolotti) -- Development of Drugs that Target Proteopathic Seeds Will Require Measurement of Drug Mechanism in Human BrainÂ{u8425}ter T. Lansbury).-Â{u4A25} Role of Functional Prions in the Persistence of Memory Storage (Eric R. Kandel, Irina Derkatch, Elias Pavlopoulos) -- Subject Index.

The misfolding and aggregation of specific proteins is an early and obligatory event in many of the age-related neurodegenerative diseases of humans, and appears to occur many years before the onset of clinical symptoms. The initial cause of this pathogenic cascade and the means whereby disease spreads through the nervous system, remain uncertain. A recent surge of research, first instigated by pathologic similarities between prion disease and Alzheimerâ€{u3824}isease, has increasingly implicated corruptive protein templating, or seeding, as a prime factor in the neurodegenerative process. The prion-like corruption of proteins also characterizes such clinically and etiologically diverse neurological disorders as Parkinsonâ€{u3824}isease, Huntingtonâ€{u3824}isease, amyotrophic lateral sclerosis, and frontotemporal lobar degeneration. Understanding the misfolding, aggregation, trafficking and pathogenicity of affected proteins thus could reveal universal principles and common therapeutic targets for some of the most devastating and intractable human brain disorders.