Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

Protein folding is a spontaneous process. However, under physiological conditions, proteins are inherently unstable, and the protein concentrations in living cells favor unspecific interactions between partially folded proteins. Thus, the cellular proteome requires the assistance of helper factors, the molecular chaperones, for quality control and the maintenance of protein homeostasis. This series of reviews delves into how these molecular machines work in the eukaryotic cell, how they convey resilience to life, how these functions have allowed expansion of the protein universe, and how we can target them for therapeutic purposes. Together, they present the progress made in recent years in our understanding of one of the most fundamental aspects of life. © 2019 Buchner.

Citation

Johannes Buchner. Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic series. The Journal of biological chemistry. 2019 Feb 08;294(6):2074-2075

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 30626733

View Full Text