Molecular chaperones and protein quality control: An introduction to the JBC Reviews thematic series

Research output: Contribution to journalReview articlepeer-review

28 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)2074-2075
Number of pages2
JournalJournal of Biological Chemistry
Volume294
Issue number6
DOIs
StatePublished - 8 Feb 2019

Fingerprint

Dive into the research topics of 'Molecular chaperones and protein quality control: An introduction to the JBC Reviews thematic series'. Together they form a unique fingerprint.

Cite this