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The Amyloid State of Proteins in Human Diseases
Author(s) -
David Eisenberg,
Mathias Jucker
Publication year - 2012
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2012.02.022
Subject(s) - amyloid disease , amyloid (mycology) , biology , biochemistry of alzheimer's disease , protein folding , amyloid precursor protein , alzheimer's disease , disease , biochemistry , amyloid β , amyloid fibril , pathology , medicine , botany
Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.

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