The proteostasis network and its decline in ageing

MS Hipp, P Kasturi, FU Hartl - Nature reviews Molecular cell biology, 2019 - nature.com
Ageing is a major risk factor for the development of many diseases, prominently including
neurodegenerative disorders such as Alzheimer disease and Parkinson disease. A hallmark …

Pathways of cellular proteostasis in aging and disease

CL Klaips, GG Jayaraj, FU Hartl - Journal of Cell Biology, 2018 - rupress.org
Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?

A Marcelo, R Koppenol, LP de Almeida, CA Matos… - Cell death & …, 2021 - nature.com
Stress granules (SGs) are membraneless cell compartments formed in response to different
stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other …

Targeting protein aggregation for the treatment of degenerative diseases

YS Eisele, C Monteiro, C Fearns… - Nature reviews Drug …, 2015 - nature.com
The aggregation of specific proteins is hypothesized to underlie several degenerative
diseases, which are collectively known as amyloid disorders. However, the mechanistic …

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 …

Protein folding and misfolding

CM Dobson - Nature, 2003 - nature.com
The manner in which a newly synthesized chain of amino acids transforms itself into a
perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence …

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 …

HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum

J Wang, J Lee, D Liem, P Ping - Gene, 2017 - Elsevier
The HSPA5 gene encodes the binding immunoglobulin protein (BiP), an Hsp70 family
chaperone localized in the ER lumen. As a highly conserved molecular chaperone, BiP …

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

DE Ehrnhoefer, J Bieschke, A Boeddrich… - Nature structural & …, 2008 - nature.com
The accumulation of β-sheet–rich amyloid fibrils or aggregates is a complex, multistep
process that is associated with cellular toxicity in a number of human protein misfolding …

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 …