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2015 ; 86
(3
): 632-45
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Amyloid polymorphism: structural basis and neurobiological relevance
#MMPMID25950632
Tycko R
Neuron
2015[May]; 86
(3
): 632-45
PMID25950632
show ga
Our understanding of the molecular structures of amyloid fibrils that are
associated with neurodegenerative diseases, of mechanisms by which
disease-associated peptides and proteins aggregate into fibrils, and of
structural properties of aggregation intermediates has advanced considerably in
recent years. Detailed molecular structural models for certain fibrils and
aggregation intermediates are now available. It is now well established that
amyloid fibrils are generally polymorphic at the molecular level, with a given
peptide or protein being capable of forming a variety of distinct,
self-propagating fibril structures. Recent results from structural studies and
from studies involving cell cultures, transgenic animals, and human tissue
provide initial evidence that molecular structural variations in amyloid fibrils
and related aggregates may correlate with or even produce variations in disease
development. This article reviews our current knowledge of the structural and
mechanistic aspects of amyloid formation, as well as current evidence for the
biological relevance of structural variations.
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