... the importance of efficient import machinery in maintaining the crucial function of mitochondria beyond protein transport [ 69 ]. mitochondrial dysfunction oxidative stress protein import protein misfolding translation As a eukaryotic cell is made up of a complex network of membrane-bound...

... of misfolded proteins in order to resolve the protein overload [ 12 ]. Therefore, they are referred to as proteostasis regulators (PRs). Many of these have been proposed as potential candidate drugs in protein misfolding and aggregation diseases (e.g. Cystic Fibrosis, Alzheimer's disease, retinitis pigmentosa...

... ) * These authors contributed equally to this work. 13 6 2019 5 11 2019 18 11 2019 18 11 2019 © 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2019 heat shock molecular chaperones protein misfolding protein quality control...

... (Supplementary Figures S1–S27). amyloid bispidine cytotoxicity oligomer prion protein misfolding Self-assembly of biological macromolecules into ordered structures regulates several biological processes and is a critical determinant of normal or diseased states [ 1 ]. Amyloid aggregation...

... disease amyloid-β model organisms molecular chaperones protein misfolding ProSP-C BRICHOS protein, corresponding to residues 59–197 in proSP-C, was expressed and purified as described previously [ 29 ]. Briefly, the construct was expressed in E. coli strain Origami B (DE3) pLysS (Novagen...

... there is activation of the UPR (unfolded protein response) as a result of misfolded protein retention. As a positive control for protein misfolding, we also expressed the mutant G221R neuroligin3, which is known to be completely retained within the ER. Our data show that overexpression of either R451C or G221R mutant...

...–SEL1L–HRD1 complex. cell biology endoplasmic reticulum endoplasmic-reticulum-associated degradation (ERAD) glycobiology glycoprotein glycosylation protein degradation protein misfolding The endoplasmic reticulum (ER) is the major site for protein folding and maturation...

... disease amyloid Aβ42 (amyloid-β 42) Aβ43 (amyloid-β 43) foldamer protein misfolding 1 To whom correspondence should be addressed (email jshorter@mail.med.upenn.edu ). 6 12 2013 20 8 2014 21 8 2014 21 8 2014 © 2014 The Authors 2014 This is an Open Access...

... by protein misfolding if the proteasome is down-regulated as recently reported in humans with Type 2 diabetes. It remains unknown, however, whether the glucose sensor enzyme glucokinase is involved in this process. A direct interaction between glucokinase and ubiquitin could be shown in vivo by FRET...

... genetic prion disease prion protein (PrP) protein aggregation protein misfolding Genetic prion diseases have a pattern of autosomal dominant inheritance and are linked to point mutations or insertions in the PRNP gene encoding the cellular prion protein (PrP C ) on chromosome 20 [ 1 ]. More...

... before its insertion in a helical conformation (blue) into the membrane [ 26 ]. BRICHOS domain HET-S prion hydrophobin melanin synthesis proinsulin C-peptide protein misfolding self-chaperoning spider silk For every polypeptide chain, a specific conformation or ensemble...

... 6 2011 24 6 2011 24 6 2011 © The Authors Journal compilation © 2011 Biochemical Society 2011 Alzheimer's disease amyloid-β peptide atomic force microscopy GM1 ganglioside membrane bilayer protein misfolding surface plasmon field-enhanced fluorescence spectroscopy...

... amyloidotic polyneuropathy and senile systemic amyloidosis. Although it has been widely accepted that protein misfolding of the monomeric form of TTR is a rate-limiting step for amyloid formation, no effective therapy targeting this misfolding step is available. In the present study, we focused on CyDs...

... aggregation protein misfolding Prion diseases are invariably fatal neurodegenerative disorders of humans and animals that arise because of misfolding of the PrP C [cellular isoform of PrP (prion protein)], a GPI (glycosylphosphatidylinositol)-anchored glycoprotein whose function is not clear [ 1...

... lipoyl domain 2-oxoglutarate dehydrogenase post-translational modification protein misfolding protein–protein interaction substrate channelling The 2-oxo acid dehydrogenase multienzyme complexes play pivotal roles in metabolism. They catalyse the oxidative decarboxylation of 2-oxo acids...

... Society 2007 cellular chaperone conformational disease cystic fibrosis cystic fibrosis transmembrane conductance regulator (CFTR) endoplasmic-reticulum-associated degradation (ERAD) protein folding protein misfolding pharmacological chaperone Biological organisms provide a unique...

...-specific chaperone (ASSC) 1-deoxygalactonojirimycin (DGJ) endoplasmic reticulum-associated degradation (ERAD) Fabry disease α-galactosidase A protein misfolding 1 To whom correspondence should be addressed (email jian-qiang.fan@mssm.edu ). 5 4 2007 24 5 2007 8 6 2007...