期刊
COLD SPRING HARBOR PERSPECTIVES IN MEDICINE
卷 6, 期 8, 页码 -出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/cshperspect.a024083
关键词
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资金
- Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases
Amyloid-beta (A beta) peptides aggregate to form polymorphic amyloid fibrils and a variety of intermediate assemblies, including oligomers and protofibrils, both in vitro and in human brain tissue. Since the beginning of the 21st century, considerable progress has been made to characterize the molecular structures of A beta aggregates. Full molecular structural models based primarily on data from measurements using solid-state nuclear magnetic resonance (ssNMR) have been developed for several in vitro A beta fibrils and one metastable protofibril. Partial structural characterization of other aggregation intermediates has been achieved. One full structural model for fibrils derived frombrain tissue has also been reported. Future work is likely to focus on additional structures from brain tissue and on further clarification of non-fibrillar A beta aggregates.
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