Repository logo

Infoscience

  • English
  • French
Log In
Logo EPFL, École polytechnique fédérale de Lausanne

Infoscience

  • English
  • French
Log In
  1. Home
  2. Academic and Research Output
  3. Journal articles
  4. Allostery in Its Many Disguises: From Theory to Applications
 
review article

Allostery in Its Many Disguises: From Theory to Applications

Wodak, Shoshana J.
•
Paci, Emanuele
•
Dokholyan, Nikolay V.
Show more
April 2, 2019
Structure

Allosteric regulation plays an important role in many biological processes, such as signal transduction, transcriptional regulation, andmetabolism. Allostery is rooted in the fundamental physical properties of macromolecular systems, but its underlying mechanisms are still poorly understood. A collection of contributions to a recent interdisciplinary CECAM(Center Europeen de Calcul Atomique et Moleculaire) workshop is used here to provide an overview of the progress and remaining limitations in the understanding of the mechanistic foundations of allostery gained from computational and experimental analyses of real protein systems and model systems. The main conceptual frameworks instrumental in driving the field are discussed. We illustrate the role of these frameworks in illuminating molecular mechanisms and explaining cellular processes, and describe some of their promising practical applications in engineering molecular sensors and informing drug design efforts.

  • Details
  • Metrics
Type
review article
DOI
10.1016/j.str.2019.01.003
Web of Science ID

WOS:000463163300003

Author(s)
Wodak, Shoshana J.
Paci, Emanuele
Dokholyan, Nikolay V.
Berezovsky, Igor N.
Horovitz, Amnon
Li, Jing  
Hilser, Vincent J.
Behar, Ivet
Karanicolas, John
Stock, Gerhard
Show more
Date Issued

2019-04-02

Publisher

CELL PRESS

Published in
Structure
Volume

27

Issue

4

Start page

566

End page

578

Subjects

Biochemistry & Molecular Biology

•

Biophysics

•

Cell Biology

•

conformational-changes

•

dynamic allostery

•

nuclear receptors

•

chemical rescue

•

ligand-binding

•

protein

•

modulation

•

mechanisms

•

network

•

pathway

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
PCSL  
LCBC  
Available on Infoscience
June 18, 2019
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/158138
Logo EPFL, École polytechnique fédérale de Lausanne
  • Contact
  • infoscience@epfl.ch

  • Follow us on Facebook
  • Follow us on Instagram
  • Follow us on LinkedIn
  • Follow us on X
  • Follow us on Youtube
AccessibilityLegal noticePrivacy policyCookie settingsEnd User AgreementGet helpFeedback

Infoscience is a service managed and provided by the Library and IT Services of EPFL. © EPFL, tous droits réservés