The heat shock response: life on the verge of death

K Richter, M Haslbeck, J Buchner - Molecular cell, 2010 - cell.com
Organisms must survive a variety of stressful conditions, including sudden temperature
increases that damage important cellular structures and interfere with essential functions. In …

Molecular chaperone functions in protein folding and proteostasis

YE Kim, MS Hipp, A Bracher… - Annual review of …, 2013 - annualreviews.org
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

CCT2 is an aggrephagy receptor for clearance of solid protein aggregates

X Ma, C Lu, Y Chen, S Li, N Ma, X Tao, Y Li, J Wang… - Cell, 2022 - cell.com
Protein aggregation is a hallmark of multiple human pathologies. Autophagy selectively
degrades protein aggregates via aggrephagy. How selectivity is achieved has been elusive …

[HTML][HTML] A human interactome in three quantitative dimensions organized by stoichiometries and abundances

MY Hein, NC Hubner, I Poser, J Cox, N Nagaraj… - Cell, 2015 - cell.com
The organization of a cell emerges from the interactions in protein networks. The
interactome is critically dependent on the strengths of interactions and the cellular …

[HTML][HTML] Widespread macromolecular interaction perturbations in human genetic disorders

N Sahni, S Yi, M Taipale, JIF Bass… - Cell, 2015 - cell.com
How disease-associated mutations impair protein activities in the context of biological
networks remains mostly undetermined. Although a few renowned alleles are well …

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

M Taipale, DF Jarosz, S Lindquist - Nature reviews Molecular cell …, 2010 - nature.com
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 quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways

M Taipale, G Tucker, J Peng, I Krykbaeva, ZY Lin… - Cell, 2014 - cell.com
Chaperones are abundant cellular proteins that promote the folding and function of their
substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set …

Functional modules of the proteostasis network

GG Jayaraj, MS Hipp, FU Hartl - Cold Spring Harbor …, 2020 - cshperspectives.cshlp.org
Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis)
and prevent the accumulation of potentially toxic protein aggregates. This proteostasis …

Converging concepts of protein folding in vitro and in vivo

FU Hartl, M Hayer-Hartl - Nature structural & molecular biology, 2009 - nature.com
Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

Effects of in vivo conditions on amyloid aggregation

MC Owen, D Gnutt, M Gao, SKTS Wärmländer… - Chemical Society …, 2019 - pubs.rsc.org
One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …