Fauvet, B., Rebeaud, M.E., Tiwari, S., De Los Rios, P. and Goloubinoff, P. (2021) Repair or Degrade: The Thermodynamic Dilemma of Cellular Protein Quality-Control. Frontiers in Molecular Biosciences, 27, Article ID: 768888.
https://doi.org/10.3389/fmolb.2021.768888

has been cited by the following article:

• TITLE: The Sigma-1 Receptor as a Pharmacologic Chaperone: Energetics

  AUTHORS: Robert B. Raffa, Joseph V. Pergolizzi Jr.

  KEYWORDS: Chaperone, Sigma-1 Receptor, Energetics, Thermodynamics, Isothermal Titration Microcalorimetry

  JOURNAL NAME: Journal of Biosciences and Medicines, Vol.12 No.8, August 27, 2024

  ABSTRACT: Initially thought to be an opioid receptor subtype, Sigma-1 receptors (S1R) are now known to be unique proteins that have chaperone-like properties. As such, they play critical roles in cellular signaling, homeostasis, and cell survival. These roles offer significant insight for understanding homeostasis of normal physiologic processes, and the pathophysiologic consequences of disruption of normal function. Because of the broad nature of chaperone action, S1R agonists and antagonists represent potential drug discovery goals for the pharmacotherapeutic treatment of a variety of disorders that result from dysfunctional proteins. The present study summarizes the S1R as a pharmacologic chaperone crucial for protein folding and cellular homeostasis. Through literature review and thermodynamic analysis, it explores how S1R stabilizes target proteins, influencing neuroprotection and potential drug therapies. The binding of chaperones to target proteins is thermodynamically favorable, offering insights into treating diseases linked to protein misfolding.