Glycosylation-directed quality control of protein folding
C Xu, DTW Ng - Nature reviews Molecular cell biology, 2015 - nature.com
Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated
in the endoplasmic reticulum. These adducts have many biological functions, including …
in the endoplasmic reticulum. These adducts have many biological functions, including …
Folding and misfolding of human membrane proteins in health and disease: from single molecules to cellular proteostasis
Advances over the past 25 years have revealed much about how the structural properties of
membranes and associated proteins are linked to the thermodynamics and kinetics of …
membranes and associated proteins are linked to the thermodynamics and kinetics of …
Calnexin cycle–structural features of the ER chaperone system
G Kozlov, K Gehring - The FEBS journal, 2020 - Wiley Online Library
The endoplasmic reticulum (ER) is the major folding compartment for secreted and
membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for …
membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for …
Roles of N-linked glycans in the endoplasmic reticulum
A Helenius, M Aebi - Annual review of biochemistry, 2004 - annualreviews.org
▪ Abstract From a process involved in cell wall synthesis in archaea and some bacteria, N-
linked glycosylation has evolved into the most common covalent protein modification in …
linked glycosylation has evolved into the most common covalent protein modification in …
Quality control in the endoplasmic reticulum
L Ellgaard, A Helenius - Nature reviews Molecular cell biology, 2003 - nature.com
The endoplasmic reticulum (ER) has a quality-control system for'proof-reading'newly
synthesized proteins, so that only native conformers reach their final destinations. Non …
synthesized proteins, so that only native conformers reach their final destinations. Non …
Mechanisms of pre‐apoptotic calreticulin exposure in immunogenic cell death
Dying tumour cells can elicit a potent anticancer immune response by exposing the
calreticulin (CRT)/ERp57 complex on the cell surface before the cells manifest any signs of …
calreticulin (CRT)/ERp57 complex on the cell surface before the cells manifest any signs of …
Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system
J Verghese, J Abrams, Y Wang… - … and molecular biology …, 2012 - Am Soc Microbiol
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 …
program that results in the immediate synthesis of a battery of cytoprotective genes in the …
A review of the mammalian unfolded protein response
A Chakrabarti, AW Chen… - Biotechnology and …, 2011 - Wiley Online Library
Proteins requiring post‐translational modifications such as N‐linked glycosylation are
processed in the endoplasmic reticulum (ER). A diverse array of cellular stresses can lead to …
processed in the endoplasmic reticulum (ER). A diverse array of cellular stresses can lead to …
Structure of the human MHC-I peptide-loading complex
A Blees, D Januliene, T Hofmann, N Koller, C Schmidt… - Nature, 2017 - nature.com
The peptide-loading complex (PLC) is a transient, multisubunit membrane complex in the
endoplasmic reticulum that is essential for establishing a hierarchical immune response …
endoplasmic reticulum that is essential for establishing a hierarchical immune response …
Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
M Michalak, J Groenendyk, E Szabo, LI Gold… - Biochemical …, 2009 - portlandpress.com
Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The
protein is involved in regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity …
protein is involved in regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity …