...Lauren Rice; Nicholas Marzano; Dezerae Cox; Bailey Skewes; Antoine M. van Oijen; Heath Ecroyd Small heat shock proteins (sHsps) are molecular chaperones that act to prevent the aberrant aggregation of misfolded proteins. Whilst it is suggested that sHsps prevent aggregation by binding to misfolded...

... 2023 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2023 endoplasmic reticulum molecular chaperones proteasomes transmembrane proteins The assembly of multi-spanning or multimeric transmembrane domain (TMD) containing proteins is complex, one...

... The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2021 cellular targeting endoplasmic reticulum ERAD molecular chaperones protein conformation ubiquitin proteasome system The regulation of salt and fluid balance across membranes is an essential...

... that sHSPs may be universally conserved effectors of longevity. aging mitochondria molecular chaperones Saccharomyces cerevisiae Analysis and visualisation of genetic and protein interactions within the proteomic data was performed with the open-source software Cytoscape (https...

... Alzheimer's and Parkinson's diseases. Molecular chaperones are intimately involved in maintaining proteostasis, and their mechanisms of action are in part dependent on the morphology of aggregation-prone proteins. This study utilised native ion mobility–mass spectrometry to provide molecular insights...

... 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...

... cilia heat shock proteins molecular chaperones molecular dynamics NMR spectroscopy Cilia are essential elements of motile and sensitive cells. In human, cilia are crucial for the function of specific tissues, including testis, kidney or lung and their dysfunction is responsible for various...

... ) 3 4 2018 16 8 2018 28 8 2018 © 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2018 cytoskeleton molecular chaperones protein conformation Chaperonin proteins are ATPases which assemble into single- and double-ring...

... ]. 31 5 2017 11 7 2017 17 7 2017 18 7 2017 © 2017 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2017 formate hydrogenlyase HycE HycH hydrogen molecular chaperones [NiFe]-hydrogenase Mixed acid fermentation enables...

... (ERAD). We previously established that a conserved, ER lumenal, molecular chaperone, Lhs1/GRP170, selects αENaC, but not β- or γ-ENaC, for degradation when the ENaC subunits were individually expressed. We now find that when all three subunits are co-expressed, Lhs1-facilitated ERAD was blocked...

... 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...

... BiP and CHOP. autism ER stress molecular chaperones neuroligin protein misfolding unfolded protein response Genetic studies of monogenic forms of ASDs (autism spectrum disorders) have identified synaptic function as one of the molecular pathways underlying neurodevelopmental...

... To whom correspondence should be addressed (e-mail [email protected] ). 14 3 2001 3 7 2001 15 8 2001 The Biochemical Society, London ©2001 2001 heat-shock proteins luciferase refolding molecular chaperones protein–protein interaction tetratricopeptide repeats...

...Elena GANEA; John J. HARDING α-Crystallin, a major lens protein, has many of the properties of a molecular chaperone, but its ability to assist refolding of proteins has been less certain. In the present work it was shown that α-crystallin specifically increased the reactivation of guanidine...

... chains, nor did it traffic to the lysosome to undergo normal endosomal-lysosomal proteolytic processing. Instead, C91T remained in an early biosynthetic compartment and was degraded. The molecular chaperone, immunoglobulin binding protein (BiP), was associated with newly-synthesized wild-type and mutant...