期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 18, 期 6, 页码 771-779出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2008.10.001
关键词
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资金
- Fondazione Cariplo (Progetto Nobel)
- Italian Ministry of Instruction
- University and Research [PRIN 2006058958, FIRB RBNE03PX83]
- Italian Ministry of Health
- EMBO Young Investigator Programme
- European Union [EYRAMY]
The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the origin of an increasing number of human diseases. The misfolding of a protein is often associated with its assembly into extracellular fibrillar aggregates, commonly termed amyloid fibrils. Despite the many efforts expended to characterise amyloid formation in vitro, it is increasingly evident that the biological environment in which aggregation occurs naturally influences the mechanism and rate of the process, as well as the structure and stability of the resulting fibrils. This problem is not trivial because of the inherent complexity of biology and difficulty to design proper experiments able to address the molecular level of the phenomenon in vivo. We will show successful approaches that have been used recently and will illustrate some of the results that have contributed to elucidate important structural aspects of amyloid formation in vivo.
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