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David Teplow on Shaping Up Amyloid Toxicity: Does It Compute?

COMMENT On Computers, Flies, and Alzheimer Disease Two recently published papers address the fundamental question of how amyloid proteins form neurotoxic assemblies (see Luheshi et al., 2007 and Cheon et al., 2007). Pat McCaffrey has written an informative and ...

David Teplow on See How They Grow: Structure of Amyloid-β Fibrils

COMMENT The work by Luhrs et al. truly is a tour de force that integrates hydrogen exchange/NMR studies, electron microscopy, thioflavin T-binding, MTT assays, and molecular modeling into studies of the structure of fibrils formed by wild-type Aβ42 and a variety ...

David Teplow on New Insights into Fibril Formation

COMMENT An increasing number of neurodegenerative diseases are associated with the formation of amyloid fibrils. Understanding the mechanism of fibril formation thus has obvious clinical value. In addition, knowledge gained in the study of amyloid fibril assembly ...

David Teplow on Heads or Tails—What Makes an Amyloid Fibril?

COMMENT Serag et al. report the results of site-directed spin labeling (SDSL) studies of inter-residue distances in native and amyloid-associated forms of transthyretin (TTR). TTR is associated with a number of amyloidoses, including senile systemic amyloidosis ...

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