Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding
The pervasive weak electromagnetic fields (EMF) inundate the industrialized society, but the biological effects of EMF as weak as 10 µT have been scarcely analyzed. Heat shock proteins (HSPs) are molecular chaperones that mediate a sequential stress response. HSP70 and HSP90 provide cells under unde...
Main Authors: | Zhizhou Huang, Mikako Ito, Shaochuan Zhang, Takuro Toda, Jun-ichi Takeda, Tomoo Ogi, Kinji Ohno |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2023-10-01
|
Series: | Ecotoxicology and Environmental Safety |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S0147651323009867 |
Similar Items
-
Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones
by: Huafeng Xu
Published: (2022-06-01) -
Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection
by: Anna Lubkowska, et al.
Published: (2021-08-01) -
Evidence of a Cell Surface Role for Hsp90 Complex Proteins Mediating Neuroblast Migration in the Subventricular Zone
by: Leo M. Miyakoshi, et al.
Published: (2017-05-01) -
Hypoglycemia Impairs the Heat Shock Protein Response: A Risk for Heat Shock in Cattle?
by: Samuel A. Atkin, et al.
Published: (2022-02-01) -
HOP, a Co-chaperone Involved in Response to Stress in Plants
by: René Toribio, et al.
Published: (2020-10-01)