Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
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| 001 | 528786202 | ||
| 005 | 20190713030956.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 180924s2016 xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.3929/ethz-b-000116640 |2 doi |
| 024 | 7 | 0 | |a 10.1038/ncomms10948 |2 doi |
| 035 | |a (ETHRESEARCH)oai:www.research-collecti.ethz.ch:20.500.11850/116640 | ||
| 245 | 0 | 0 | |a Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation |h [Elektronische Daten] |c [Paolo Arosio, Thomas C.T. Michaels, Sara Linse, Cecilia Månsson, Cecilia Emanuelsson, Jenny Presto, Jan Johansson, Michele Vendruscolo, Christopher M. Dobson, Tuomas P.J. Knowles] |
| 246 | 0 | |a Nat Commun | |
| 506 | |a Open access |2 ethresearch | ||
| 520 | 3 | |a It is increasingly recognized that molecular chaperones play a key role in modulating the formation of amyloid fibrils, a process associated with a wide range of human disorders. Understanding the detailed mechanisms by which they perform this function, however, has been challenging because of the great complexity of the protein aggregation process itself. In this work, we build on a previous kinetic approach and develop a model that considers pairwise interactions between molecular chaperones and different protein species to identify the protein components targeted by the chaperones and the corresponding microscopic reaction steps that are inhibited. We show that these interactions conserve the topology of the unperturbed reaction network but modify the connectivity weights between the different microscopic steps. Moreover, by analysing several protein-molecular chaperone systems, we reveal the striking diversity in the microscopic mechanisms by which molecular chaperones act to suppress amyloid formation. | |
| 540 | |a Creative Commons Attribution 4.0 International |u http://creativecommons.org/licenses/by/4.0 |2 ethresearch | ||
| 700 | 1 | |a Arosio |D Paolo |e joint author | |
| 700 | 1 | |a Michaels |D Thomas C.T. |e joint author | |
| 700 | 1 | |a Linse |D Sara |e joint author | |
| 700 | 1 | |a Månsson |D Cecilia |e joint author | |
| 700 | 1 | |a Emanuelsson |D Cecilia |e joint author | |
| 700 | 1 | |a Presto |D Jenny |e joint author | |
| 700 | 1 | |a Johansson |D Jan |e joint author | |
| 700 | 1 | |a Vendruscolo |D Michele |e joint author | |
| 700 | 1 | |a Dobson |D Christopher M. |e joint author | |
| 700 | 1 | |a Knowles |D Tuomas P.J. |e joint author | |
| 773 | 0 | |t Nature Communications |d London : Nature Publishing Group |g 7, p. 10948 |x 2041-1723 | |
| 856 | 4 | 0 | |u http://hdl.handle.net/20.500.11850/116640 |q text/html |z WWW-Backlink auf das Repository (Open access) |
| 908 | |D 1 |a Journal Article |2 ethresearch | ||
| 950 | |B ETHRESEARCH |P 856 |E 40 |u http://hdl.handle.net/20.500.11850/116640 |q text/html |z WWW-Backlink auf das Repository (Open access) | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Arosio |D Paolo |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Michaels |D Thomas C.T. |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Linse |D Sara |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Månsson |D Cecilia |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Emanuelsson |D Cecilia |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Presto |D Jenny |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Johansson |D Jan |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Vendruscolo |D Michele |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Dobson |D Christopher M. |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Knowles |D Tuomas P.J. |e joint author | ||
| 950 | |B ETHRESEARCH |P 773 |E 0- |t Nature Communications |d London : Nature Publishing Group |g 7, p. 10948 |x 2041-1723 | ||
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B ETHRESEARCH |F ETHRESEARCH |b ETHRESEARCH |j Journal Article |c Open access | ||