The assembly of ribosomal subunits is a highly orchestrated process that involves a huge
cohort of accessory factors. Most eukaryotic ribosome biogenesis factors were first identified …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Biological processes are regulated by intermolecular interactions and chemical
modifications that do not affect protein levels, thus esca** detection in classical proteomic …

Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

A common need for microbial cells is the ability to respond to potentially toxic environmental
insults. Here we review the progress in understanding the response of the yeast …

Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis)
and prevent the accumulation of potentially toxic protein aggregates. This proteostasis …

The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

The protein folding problem was first articulated as question of how order arose from
disorder in proteins: How did the various native structures of proteins arise from interatomic …

Heat shock protein 90α (Hsp90α), encoded by the HSP90AA1 gene, is the stress inducible
isoform of the molecular chaperone Hsp90. Hsp90α is regulated differently and has different …

How can species remain unaltered for long periods yet also undergo rapid diversification?
By linking genetic variation to phenotypic variation via environmental stress, the Hsp90 …