期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 430, 期 20, 页码 3631-3641出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2018.07.007
关键词
functional amyloid; protein misfolding; microbial amyloids; nature-inspired therapeutics; toxic oligomer
资金
- National Institutes of Health [R01GM118651, R21 AI137535]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI137535] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM118651] Funding Source: NIH RePORTER
The term amyloid has historically been used to describe fibrillar aggregates formed as the result of protein misfolding and that are associated with a range of diseases broadly termed amyloidoses. The discovery of functional amyloids expanded the amyloid umbrella to encompass aggregates structurally similar to disease-associated amyloids but that engage in a variety of biologically useful tasks without incurring toxicity. The mechanisms by which functional amyloid systems ensure nontoxic assembly has provided insights into potential therapeutic strategies for treating amyloidoses. Some of the most-studied functional amyloids are ones produced by bacteria. Curli amyloids are extracellular fibers made by enteric bacteria that function to encase and protect bacterial communities during biofilm formation. Here we review recent studies highlighting microbial functional amyloid assembly systems that are tailored to enable the assembly of non-toxic amyloid aggregates. (C) 2018 Elsevier Ltd. All rights reserved.
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