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Updated: Jul 17, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
Chaperones as parts of cellular networks
Peter Csermely1, Csaba Söti, Gregory L Blatch
1Department of Medical Chemistry, Semmelweis University, Puskin Street 9, H-1 088 Budapest, Hungary. csermely@puskin.sote.hu
Abstract:
The most important interactions between cellular molecules have a high affinity, are unique and specific, and require a network approach for a detailed description. Molecular chaperones usually have many first and second neighbors in protein-protein interaction networks and they play a prominent role in signaling and transcriptional regulatory networks of the cell. Chaperones may uncouple protein, signaling, membranous, organellar and transcriptional networks during stress, which gives an additional protection for the cell at the network-level. Recent advances uncovered that chaperones act as genetic buffers stabilizing the phenotype of various cells and organisms. This chaperone effect on the emergent properties of cellular networks may be generalized to proteins having a specific, central position and low affinity, weak links in protein networks. Cellular networks are preferentially remodeled in various diseases and aging, which may help us to design novel therapeutic and anti-aging strategies.
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