{"scopus_import":"1","_id":"10361","publication_status":"published","publication":"Annual Review of Physical Chemistry","language":[{"iso":"eng"}],"date_created":"2021-11-26T12:52:12Z","abstract":[{"text":"Understanding how normally soluble peptides and proteins aggregate to form amyloid fibrils is central to many areas of modern biomolecular science, ranging from the development of functional biomaterials to the design of rational therapeutic strategies against increasingly prevalent medical conditions such as Alzheimer's and Parkinson's diseases. As such, there is a great need to develop models to mechanistically describe how amyloid fibrils are formed from precursor peptides and proteins. Here we review and discuss how ideas and concepts from chemical reaction kinetics can help to achieve this objective. In particular, we show how a combination of theory, experiments, and computer simulations, based on chemical kinetics, provides a general formalism for uncovering, at the molecular level, the mechanistic steps that underlie the phenomenon of amyloid fibril formation.","lang":"eng"}],"volume":69,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No","day":"28","publisher":"Annual Reviews","pmid":1,"doi":"10.1146/annurev-physchem-050317-021322","article_type":"original","page":"273-298","type":"journal_article","issue":"1","acknowledgement":"We acknowledge support from the Swiss National Science Foundation (T.C.T.M.); Peterhouse,\r\nCambridge (T.C.T.M.); the Royal Society (A.S.); the Academy of Medical Sciences (A.S.); the\r\nWellcome Trust (A.S., M.V., C.M.D., T.P.J.K.); the Cambridge Centre for Misfolding Diseases\r\n(M.V., C.M.D., T.P.J.K.); the Biotechnology and Biological Sciences Research Council (C.M.D.,\r\nT.P.J.K.); and the Frances and Augustus Newman Foundation (T.P.J.K.). The research leading\r\nto these results has received funding from the European Research Council (ERC) under the\r\nEuropean Union’s Seventh Framework Programme (FP7/2007-2013) through the ERC grant\r\nPhysProt (337969).","status":"public","external_id":{"pmid":["29490200"]},"author":[{"first_name":"Thomas C.T.","last_name":"Michaels","full_name":"Michaels, Thomas C.T."},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","last_name":"Šarić","orcid":"0000-0002-7854-2139","first_name":"Anđela"},{"full_name":"Habchi, Johnny","last_name":"Habchi","first_name":"Johnny"},{"first_name":"Sean","last_name":"Chia","full_name":"Chia, Sean"},{"full_name":"Meisl, Georg","last_name":"Meisl","first_name":"Georg"},{"full_name":"Vendruscolo, Michele","first_name":"Michele","last_name":"Vendruscolo"},{"first_name":"Christopher M.","last_name":"Dobson","full_name":"Dobson, Christopher M."},{"full_name":"Knowles, Tuomas P.J.","last_name":"Knowles","first_name":"Tuomas P.J."}],"oa_version":"None","date_updated":"2021-11-26T15:58:19Z","month":"02","year":"2018","publication_identifier":{"issn":["0066-426X"],"eissn":["1545-1593"]},"keyword":["physical and theoretical chemistry"],"quality_controlled":"1","title":"Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation","intvolume":"        69","extern":"1","date_published":"2018-02-28T00:00:00Z","citation":{"short":"T.C.T. Michaels, A. Šarić, J. Habchi, S. Chia, G. Meisl, M. Vendruscolo, C.M. Dobson, T.P.J. Knowles, Annual Review of Physical Chemistry 69 (2018) 273–298.","mla":"Michaels, Thomas C. T., et al. “Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.” <i>Annual Review of Physical Chemistry</i>, vol. 69, no. 1, Annual Reviews, 2018, pp. 273–98, doi:<a href=\"https://doi.org/10.1146/annurev-physchem-050317-021322\">10.1146/annurev-physchem-050317-021322</a>.","ama":"Michaels TCT, Šarić A, Habchi J, et al. Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation. <i>Annual Review of Physical Chemistry</i>. 2018;69(1):273-298. doi:<a href=\"https://doi.org/10.1146/annurev-physchem-050317-021322\">10.1146/annurev-physchem-050317-021322</a>","ieee":"T. C. T. Michaels <i>et al.</i>, “Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation,” <i>Annual Review of Physical Chemistry</i>, vol. 69, no. 1. Annual Reviews, pp. 273–298, 2018.","chicago":"Michaels, Thomas C.T., Anđela Šarić, Johnny Habchi, Sean Chia, Georg Meisl, Michele Vendruscolo, Christopher M. Dobson, and Tuomas P.J. Knowles. “Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.” <i>Annual Review of Physical Chemistry</i>. Annual Reviews, 2018. <a href=\"https://doi.org/10.1146/annurev-physchem-050317-021322\">https://doi.org/10.1146/annurev-physchem-050317-021322</a>.","apa":"Michaels, T. C. T., Šarić, A., Habchi, J., Chia, S., Meisl, G., Vendruscolo, M., … Knowles, T. P. J. (2018). Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation. <i>Annual Review of Physical Chemistry</i>. Annual Reviews. <a href=\"https://doi.org/10.1146/annurev-physchem-050317-021322\">https://doi.org/10.1146/annurev-physchem-050317-021322</a>","ista":"Michaels TCT, Šarić A, Habchi J, Chia S, Meisl G, Vendruscolo M, Dobson CM, Knowles TPJ. 2018. Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation. Annual Review of Physical Chemistry. 69(1), 273–298."}}