The biology of proteostasis in aging and disease
J Labbadia, RI Morimoto - Annual review of biochemistry, 2015 - annualreviews.org
Loss of protein homeostasis (proteostasis) is a common feature of aging and disease that is
characterized by the appearance of nonnative protein aggregates in various tissues. Protein …
characterized by the appearance of nonnative protein aggregates in various tissues. Protein …
Molecular and cellular basis of genetically inherited skeletal muscle disorders
JJ Dowling, CC Weihl, MJ Spencer - Nature Reviews Molecular Cell …, 2021 - nature.com
Neuromuscular disorders comprise a diverse group of human inborn diseases that arise
from defects in the structure and/or function of the muscle tissue—encompassing the muscle …
from defects in the structure and/or function of the muscle tissue—encompassing the muscle …
Proteostasis impairment in protein-misfolding and-aggregation diseases
Cells possess an extensive network of components to safeguard proteome integrity and
maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines …
maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines …
Translation deregulation in human disease
S Tahmasebi, A Khoutorsky, MB Mathews… - … reviews Molecular cell …, 2018 - nature.com
Advances in sequencing and high-throughput techniques have provided an unprecedented
opportunity to interrogate human diseases on a genome-wide scale. The list of disease …
opportunity to interrogate human diseases on a genome-wide scale. The list of disease …
Molecular chaperone functions in protein folding and proteostasis
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
The unfolded protein response: integrating stress signals through the stress sensor IRE1α
Stress induced by accumulation of unfolded proteins at the endoplasmic reticulum (ER) is a
classic feature of secretory cells and is observed in many tissues in human diseases …
classic feature of secretory cells and is observed in many tissues in human diseases …
Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders
M Wang, S Wey, Y Zhang, R Ye… - Antioxidants & redox …, 2009 - liebertpub.com
GRP78/BiP is a major endoplasmic reticulum (ER) chaperone protein critical for protein
quality control of the ER, as well as controlling the activation of the ER-transmembrane …
quality control of the ER, as well as controlling the activation of the ER-transmembrane …
Protein folding in the endoplasmic reticulum
I Braakman, DN Hebert - Cold Spring Harbor …, 2013 - cshperspectives.cshlp.org
In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum
(ER), including the role of three types of covalent modifications: signal peptide removal, N …
(ER), including the role of three types of covalent modifications: signal peptide removal, N …
In and out of the ER: protein folding, quality control, degradation, and related human diseases
DN Hebert, M Molinari - Physiological reviews, 2007 - journals.physiology.org
A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …
[HTML][HTML] ER chaperones in mammalian development and human diseases
M Ni, AS Lee - FEBS letters, 2007 - Elsevier
The field of endoplasmic reticulum (ER) stress in mammalian cells has expanded rapidly
during the past decade, contributing to understanding of the molecular pathways that allow …
during the past decade, contributing to understanding of the molecular pathways that allow …