期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 421, 期 2-3, 页码 160-171出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2012.02.031
关键词
amyloid; kinetics; mechanism; aggregation; nucleation
资金
- Schiff Foundation
- Kennedy Memorial Trust
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
- BBSRC [BB/H003843/1] Funding Source: UKRI
- MRC [MC_G1000734] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H003843/1] Funding Source: researchfish
- Medical Research Council [MC_G1000734] Funding Source: researchfish
The ability to relate bulk experimental measurements of amyloid formation to the microscopic assembly processes that underlie protein aggregation is critical in order to achieve a quantitative understanding of this complex phenomenon. In this review, we focus on the insights from classical and modern theories of linear growth phenomena and discuss how theory allows the roles of growth and nucleation processes to be defined through the analysis of experimental in vitro time courses of amyloid formation. Moreover, we discuss the specific signatures in the time course of the reactions that correspond to the actions of primary and secondary nucleation processes, and outline strategies for identifying and characterising the nature of the dominant process responsible in each case for the generation of new aggregates. We highlight the power of a global analysis of experimental time courses acquired under different conditions, and discuss how such an analysis allows a rigorous connection to be established between the macroscopic measurements and the rates of the individual microscopic processes that underlie the phenomenon of amyloid formation. (C) 2012 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据