Publication Date:
2009-12-17
Description:
We present an analytical treatment of a set of coupled kinetic equations that governs the self-assembly of filamentous molecular structures. Application to the case of protein aggregation demonstrates that the kinetics of amyloid growth can often be dominated by secondary rather than by primary nucleation events. Our results further reveal a range of general features of the growth kinetics of fragmenting filamentous structures, including the existence of generic scaling laws that provide mechanistic information in contexts ranging from in vitro amyloid growth to the in vivo development of mammalian prion diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Tuomas P J -- Waudby, Christopher A -- Devlin, Glyn L -- Cohen, Samuel I A -- Aguzzi, Adriano -- Vendruscolo, Michele -- Terentjev, Eugene M -- Welland, Mark E -- Dobson, Christopher M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Dec 11;326(5959):1533-7. doi: 10.1126/science.1178250.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cavendish Laboratory, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0HE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20007899" target="_blank"〉PubMed〈/a〉
Keywords:
Amyloid/*chemistry
;
Biochemical Processes
;
Glutathione Peroxidase/chemistry
;
Insulin/chemistry
;
Kinetics
;
Lactoglobulins/chemistry
;
Mathematical Concepts
;
Multiprotein Complexes/*chemistry
;
Peptide Termination Factors/chemistry
;
Peptides/chemistry
;
Prions/chemistry
;
*Protein Multimerization
;
Saccharomyces cerevisiae Proteins/chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
