---
_id: '13237'
abstract:
- lang: eng
  text: The formation of amyloid fibrils is a general class of protein self-assembly
    behaviour, which is associated with both functional biology and the development
    of a number of disorders, such as Alzheimer and Parkinson diseases. In this Review,
    we discuss how general physical concepts from the study of phase transitions can
    be used to illuminate the fundamental mechanisms of amyloid self-assembly. We
    summarize progress in the efforts to describe the essential biophysical features
    of amyloid self-assembly as a nucleation-and-growth process and discuss how master
    equation approaches can reveal the key molecular pathways underlying this process,
    including the role of secondary nucleation. Additionally, we outline how non-classical
    aspects of aggregate formation involving oligomers or biomolecular condensates
    have emerged, inspiring developments in understanding, modelling and modulating
    complex protein assembly pathways. Finally, we consider how these concepts can
    be applied to kinetics-based drug discovery and therapeutic design to develop
    treatments for protein aggregation diseases.
acknowledgement: The authors acknowledge support from the Institute for the Physics
  of Living Systems, University College London (T.C.T.M.), the Swedish Research Council
  (2015-00143) (S.L.), the European Research Council under the European Union’s Seventh
  Framework Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no.
  337969) (T.P.J.K.), the BBSRC (T.P.J.K.), the Newman Foundation (T.P.J.K.) and the
  Wellcome Trust Collaborative Award 203249/Z/16/Z (T.P.J.K.). The authors thank C.
  Flandoli for help with illustrations.
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C.T.
  full_name: Michaels, Thomas C.T.
  last_name: Michaels
- first_name: Daoyuan
  full_name: Qian, Daoyuan
  last_name: Qian
- first_name: Anđela
  full_name: Šarić, Anđela
  id: bf63d406-f056-11eb-b41d-f263a6566d8b
  last_name: Šarić
  orcid: 0000-0002-7854-2139
- first_name: Michele
  full_name: Vendruscolo, Michele
  last_name: Vendruscolo
- first_name: Sara
  full_name: Linse, Sara
  last_name: Linse
- first_name: Tuomas P.J.
  full_name: Knowles, Tuomas P.J.
  last_name: Knowles
citation:
  ama: Michaels TCT, Qian D, Šarić A, Vendruscolo M, Linse S, Knowles TPJ. Amyloid
    formation as a protein phase transition. <i>Nature Reviews Physics</i>. 2023;5:379–397.
    doi:<a href="https://doi.org/10.1038/s42254-023-00598-9">10.1038/s42254-023-00598-9</a>
  apa: Michaels, T. C. T., Qian, D., Šarić, A., Vendruscolo, M., Linse, S., &#38;
    Knowles, T. P. J. (2023). Amyloid formation as a protein phase transition. <i>Nature
    Reviews Physics</i>. Springer Nature. <a href="https://doi.org/10.1038/s42254-023-00598-9">https://doi.org/10.1038/s42254-023-00598-9</a>
  chicago: Michaels, Thomas C.T., Daoyuan Qian, Anđela Šarić, Michele Vendruscolo,
    Sara Linse, and Tuomas P.J. Knowles. “Amyloid Formation as a Protein Phase Transition.”
    <i>Nature Reviews Physics</i>. Springer Nature, 2023. <a href="https://doi.org/10.1038/s42254-023-00598-9">https://doi.org/10.1038/s42254-023-00598-9</a>.
  ieee: T. C. T. Michaels, D. Qian, A. Šarić, M. Vendruscolo, S. Linse, and T. P.
    J. Knowles, “Amyloid formation as a protein phase transition,” <i>Nature Reviews
    Physics</i>, vol. 5. Springer Nature, pp. 379–397, 2023.
  ista: Michaels TCT, Qian D, Šarić A, Vendruscolo M, Linse S, Knowles TPJ. 2023.
    Amyloid formation as a protein phase transition. Nature Reviews Physics. 5, 379–397.
  mla: Michaels, Thomas C. T., et al. “Amyloid Formation as a Protein Phase Transition.”
    <i>Nature Reviews Physics</i>, vol. 5, Springer Nature, 2023, pp. 379–397, doi:<a
    href="https://doi.org/10.1038/s42254-023-00598-9">10.1038/s42254-023-00598-9</a>.
  short: T.C.T. Michaels, D. Qian, A. Šarić, M. Vendruscolo, S. Linse, T.P.J. Knowles,
    Nature Reviews Physics 5 (2023) 379–397.
date_created: 2023-07-16T22:01:12Z
date_published: 2023-07-01T00:00:00Z
date_updated: 2023-08-02T06:28:38Z
day: '01'
department:
- _id: AnSa
doi: 10.1038/s42254-023-00598-9
external_id:
  isi:
  - '001017539800001'
intvolume: '         5'
isi: 1
language:
- iso: eng
month: '07'
oa_version: None
page: 379–397
publication: Nature Reviews Physics
publication_identifier:
  eissn:
  - 2522-5820
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Amyloid formation as a protein phase transition
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2023'
...
---
_id: '12165'
abstract:
- lang: eng
  text: It may come as a surprise that a phenomenon as ubiquitous and prominent as
    the transition from laminar to turbulent flow has resisted combined efforts by
    physicists, engineers and mathematicians, and remained unresolved for almost one
    and a half centuries. In recent years, various studies have proposed analogies
    to directed percolation, a well-known universality class in statistical mechanics,
    which describes a non-equilibrium phase transition from a fluctuating active phase
    into an absorbing state. It is this unlikely relation between the multiscale,
    high-dimensional dynamics that signify the transition process in virtually all
    flows of practical relevance, and the arguably most basic non-equilibrium phase
    transition, that so far has mainly been the subject of model studies, which I
    review in this Perspective.
article_processing_charge: No
article_type: original
author:
- first_name: Björn
  full_name: Hof, Björn
  id: 3A374330-F248-11E8-B48F-1D18A9856A87
  last_name: Hof
  orcid: 0000-0003-2057-2754
citation:
  ama: Hof B. Directed percolation and the transition to turbulence. <i>Nature Reviews
    Physics</i>. 2023;5:62-72. doi:<a href="https://doi.org/10.1038/s42254-022-00539-y">10.1038/s42254-022-00539-y</a>
  apa: Hof, B. (2023). Directed percolation and the transition to turbulence. <i>Nature
    Reviews Physics</i>. Springer Nature. <a href="https://doi.org/10.1038/s42254-022-00539-y">https://doi.org/10.1038/s42254-022-00539-y</a>
  chicago: Hof, Björn. “Directed Percolation and the Transition to Turbulence.” <i>Nature
    Reviews Physics</i>. Springer Nature, 2023. <a href="https://doi.org/10.1038/s42254-022-00539-y">https://doi.org/10.1038/s42254-022-00539-y</a>.
  ieee: B. Hof, “Directed percolation and the transition to turbulence,” <i>Nature
    Reviews Physics</i>, vol. 5. Springer Nature, pp. 62–72, 2023.
  ista: Hof B. 2023. Directed percolation and the transition to turbulence. Nature
    Reviews Physics. 5, 62–72.
  mla: Hof, Björn. “Directed Percolation and the Transition to Turbulence.” <i>Nature
    Reviews Physics</i>, vol. 5, Springer Nature, 2023, pp. 62–72, doi:<a href="https://doi.org/10.1038/s42254-022-00539-y">10.1038/s42254-022-00539-y</a>.
  short: B. Hof, Nature Reviews Physics 5 (2023) 62–72.
date_created: 2023-01-12T12:10:18Z
date_published: 2023-01-01T00:00:00Z
date_updated: 2023-08-01T12:50:48Z
day: '01'
department:
- _id: BjHo
doi: 10.1038/s42254-022-00539-y
external_id:
  isi:
  - '000890148700002'
intvolume: '         5'
isi: 1
keyword:
- General Physics and Astronomy
language:
- iso: eng
month: '01'
oa_version: None
page: 62-72
publication: Nature Reviews Physics
publication_identifier:
  eissn:
  - 2522-5820
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Directed percolation and the transition to turbulence
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2023'
...