The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here:

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Portrait of Sara Snogerup Linse

Sara Linse


Portrait of Sara Snogerup Linse

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation


  • 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

Summary, in English

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.


  • Biochemistry and Structural Biology
  • MultiPark: Multidisciplinary research focused on Parkinson´s disease

Publishing year





Nature Communications



Document type

Journal article


Nature Publishing Group


  • Biochemistry and Molecular Biology




  • ISSN: 2041-1723