4.7 Review

From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation

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

  1. Schiff Foundation
  2. Kennedy Memorial Trust
  3. Wellcome Trust
  4. Biotechnology and Biological Sciences Research Council
  5. BBSRC [BB/H003843/1] Funding Source: UKRI
  6. MRC [MC_G1000734] Funding Source: UKRI
  7. Biotechnology and Biological Sciences Research Council [BB/H003843/1] Funding Source: researchfish
  8. Medical Research Council [MC_G1000734] Funding Source: researchfish

向作者/读者索取更多资源

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.

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