... are degraded by Lon and ClpXP proteases, whereas matrix AAA (m-AAA) and intermembrane AAA (i-AAA) guard opposite faces of the mitochondrial IM [ 83 ]. mitochondrial dysfunction oxidative stress protein import protein misfolding translation As a eukaryotic cell is made up of a complex network...

... BY) . globotriaosylsphingosine lysosomal enzyme proteasome inhibitor protein misfolding transcriptomics New therapeutic approaches include the use of small molecules, which have the capacity to modify proteostasis, including protein synthesis, folding and degradation. They either increase the folding capacity of the ER...

... mutant proteins (1 µM) were evaluated by incubating with β-casein (10 µM) in 20 mM phosphate sodium buffer (pH 8.0) at 37°C or 25°C for varying length of time before SDS–PAGE analysis. heat shock molecular chaperones protein misfolding protein quality control serine proteases β-barrel...

[email protected] ) or Bishwajit Kundu ( [email protected] ) 6 8 2016 25 10 2016 31 10 2016 1 11 2016 © 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society 2017 amyloid bispidine cytotoxicity oligomer prion protein misfolding...

... disease amyloid-β model organisms molecular chaperones protein misfolding Fibril formation kinetics was studied by recording the thioflavin T (ThT) fluorescence intensity as a function of time in a plate reader (FLUOStar Galaxy, BMG Labtech, Offenberg, Germany). The fluorescence...

... 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...

... degradation (ERAD) glycobiology glycoprotein glycosylation protein degradation protein misfolding The endoplasmic reticulum (ER) is the major site for protein folding and maturation in the secretory pathway of eukaryotic cells. Membrane-anchored and luminal proteins are folded and assembled...

... with Alzheimer's disease. One foldamer inhibits formation of toxic Aβ-species as well as the self-templating activity of Aβ fibrils, properties that could have therapeutic utility. Alzheimer’s disease amyloid Aβ42 (amyloid-β 42) Aβ43 (amyloid-β 43) foldamer protein misfolding Protein misfolding...

... 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...

... 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 than 20 point mutations have...

... be addressed (email [email protected] ). 6 6 2012 9 7 2012 23 7 2012 © The Authors Journal compilation © 2012 Biochemical Society 2012 BRICHOS domain HET-S prion hydrophobin melanin synthesis proinsulin C-peptide protein misfolding self-chaperoning spider silk...

... 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...

... 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 ]. Unique...

... correspondence should addressed (email [email protected] ). 15 8 2007 5 10 2007 11 10 2007 11 10 2007 © The Authors Journal compilation © 2008 Biochemical Society 2008 lipoyl domain 2-oxoglutarate dehydrogenase post-translational modification protein misfolding protein...

... with respect to conformational stability, but which retain full or partial catalytic activity. These findings apply to a relatively large set of missense mutations identified in both classic and variant Fabry disease patients, and suggest that protein misfolding may be more widespread than previously thought...

... cystic fibrosis transmembrane conductance regulator (CFTR) endoplasmic-reticulum-associated degradation (ERAD) protein folding protein misfolding pharmacological chaperone Biological organisms provide a unique environment for protein folding that is subject to a wide variety of physical...