Abstract
Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Adult
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Aged
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Aged, 80 and over
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Alzheimer Disease / metabolism
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Amyloid / chemistry*
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Amyloid / metabolism
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Amyloid Neuropathies / genetics
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Amyloid Neuropathies / metabolism
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Amyloid beta-Peptides / chemistry
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Amyloid beta-Peptides / metabolism
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Amyloidosis / metabolism
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Animals
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Humans
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Immunoglobulin Light Chains / chemistry
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Models, Molecular
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Muramidase / genetics
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Muramidase / metabolism
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Prealbumin / chemistry
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Prealbumin / metabolism
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Protein Conformation*
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Protein Folding
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Structure-Activity Relationship
Substances
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Amyloid
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Amyloid beta-Peptides
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Immunoglobulin Light Chains
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Prealbumin
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Muramidase