Folding and misfolding of human membrane proteins in health and disease: from single molecules to cellular proteostasis

JT Marinko, H Huang, WD Penn, JA Capra… - Chemical …, 2019 - ACS Publications
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 …

[HTML][HTML] Hereditary spastic paraplegia: clinical-genetic characteristics and evolving molecular mechanisms

TL Giudice, F Lombardi, FM Santorelli, T Kawarai… - Experimental …, 2014 - Elsevier
Hereditary spastic paraplegia (HSP) is a group of clinically and genetically heterogeneous
neurological disorders characterized by pathophysiologic hallmark of length-dependent …

Protein‐misfolding diseases and chaperone‐based therapeutic approaches

TK Chaudhuri, S Paul - The FEBS journal, 2006 - Wiley Online Library
A large number of neurodegenerative diseases in humans result from protein misfolding and
aggregation. Protein misfolding is believed to be the primary cause of Alzheimer's disease …

Protein folding and quality control in the endoplasmic reticulum

B Kleizen, I Braakman - Current opinion in cell biology, 2004 - Elsevier
The endoplasmic reticulum (ER) is a highly versatile protein factory that is equipped with
chaperones and folding enzymes essential for protein folding. ER quality control guided by …

PLP1-related inherited dysmyelinating disorders: Pelizaeus-Merzbacher disease and spastic paraplegia type 2

K Inoue - Neurogenetics, 2005 - Springer
Pelizaeus-Merzbacher disease (PMD) and its allelic disorder, spastic paraplegia type 2
(SPG2), are among the best-characterized dysmyelinating leukodystrophies of the central …

Folding of heterologous proteins in bacterial cell factories: Cellular mechanisms and engineering strategies

Y Rong, SI Jensen, K Lindorff-Larsen… - Biotechnology Advances, 2023 - Elsevier
The expression of correctly folded and functional heterologous proteins is important in many
biotechnological production processes, whether it is enzymes, biopharmaceuticals or …

Versatility of the endoplasmic reticulum protein folding factory

E Anken, I Braakman - Critical reviews in biochemistry and …, 2005 - Taylor & Francis
The endoplasmic reticulum (ER) is dedicated to import, folding and assembly of all proteins
that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is …

Chaperoning G protein-coupled receptors: from cell biology to therapeutics

YX Tao, PM Conn - Endocrine reviews, 2014 - academic.oup.com
G protein-coupled receptors (GPCRs) are membrane proteins that traverse the plasma
membrane seven times (hence, are also called 7TM receptors). The polytopic structure of …

The essential functions of molecular chaperones and folding enzymes in maintaining endoplasmic reticulum homeostasis

LM Hendershot, TM Buck, JL Brodsky - Journal of Molecular Biology, 2023 - Elsevier
It has been estimated that up to one-third of the proteins encoded by the human genome
enter the endoplasmic reticulum (ER) as extended polypeptide chains where they undergo …

Calsperin is a testis-specific chaperone required for sperm fertility

M Ikawa, K Tokuhiro, R Yamaguchi, AM Benham… - Journal of Biological …, 2011 - ASBMB
Calnexin (CANX) and calreticulin (CALR) are homologous lectin chaperones located in the
endoplasmic reticulum and cooperate to mediate nascent glycoprotein folding. In the testis …