... of the Biochemical Society 2019 Hsp70 J-protein molecular chaperone nucleotide exchange factor protein aggregation protein folding Molecular chaperones play key roles in maintaining cellular protein health, facilitating protein targeting, and ensuring high-fidelity protein biosynthesis. Central...

... and distributed under the Creative Commons Attribution License 4.0 (CC BY) . Hsp104 molecular chaperone prion Saccharomyces cerevisiae TorsinA A plasmid based on pBEVY-U and expressing the wild-type S. cerevisiae HSP104 gene (designated pUKC2751) was previously made in this laboratory...

... by Portland Press Limited on behalf of the Biochemical Society 2017 molecular chaperone post-translational modification proteasome protein quality control ubiquitin ligases Correspondence: Jeffrey L. Brodsky ( [email protected] ) Among these many ligases, three classes of E3s function...

... and increases solubility. Alzheimer's disease amyloid BRICHOS molecular chaperone protein conformation protein inclusions In neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease, amyloid formation is believed to be a main cause [ 1 – 3 ]. Although amyloid-forming...

... dissociation. Both processes are regulated by DnaK and substrates. ClpB DnaK protein aggregation molecular chaperone protein folding protein aggregate reactivation Molecular chaperones form an elaborate protein network that maintains cellular proteostasis [ 1 – 3 ]. The interactions between...

... structural and functional specificities. AtTrx-h3 acts as both a disulfide reductase and as a molecular chaperone. We prepared five representative AtTrx-hs and compared their protein structures and disulfide reductase and molecular chaperone activities. AtTrx-h2 with an N-terminal extension exhibited...

.... The 14-3-3ζ isoform is a molecular chaperone, preventing the stress-induced aggregation of target proteins in a manner comparable with that of the unrelated sHsps (small heat-shock proteins). 1 H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids...

... functioned as a molecular chaperone in vitro , preventing heat-induced aggregation of citrate synthase and reduction-driven denaturation of insulin. Sequence characteristics, synthesis patterns and functional properties demonstrate clearly that ArHsp21 is an sHSP able to chaperone other proteins...

... and as molecular chaperones, functions that are influenced by their oligomeric state. Of the human peroxiredoxins, Prx IV (peroxiredoxin IV) is unique in possessing an N-terminal signal peptide believed to allow secretion from the cell. Here, we present a characterization of Prx IV in human cells demonstrating...

... 2007 12 11 2007 © The Authors Journal compilation © 2008 Biochemical Society 2008 Living organisms have evolved ways to protect themselves under stress conditions. Stress proteins, or molecular chaperones, have been identified and studied extensively as the type of protein that function...

... and that mediate ERAD substrate selection are molecular chaperones, some of which are heat- and/or stress-inducible and are thus known as Hsps (heat-shock proteins). But, regardless of whether they are constitutively expressed or are inducible, it has been assumed that all molecular chaperones function identically...

...Gary Flom; Robert H. Behal; Luke Rosen; Douglas G. Cole; Jill L. Johnson The molecular chaperone Hsp (heat-shock protein) 90 is critical for the activity of diverse cellular client proteins. In a current model, client proteins are transferred from Hsp70 to Hsp90 in a process mediated by the co...

...Anja HARST; Hongying LIN; Wolfgang M. J. OBERMANN The ATP-dependent molecular chaperone Hsp90 (heat-shock protein 90) is essential for the maturation of hormone receptors and protein kinases. During the process of client protein activation, Hsp90 co-operates with cofactors/co-chaperones of unique...

... a disintegrin and metalloproteinase (ADAM) cysteine switch molecular chaperone TNFα-converting enzyme (TACE) tumour necrosis factor (TNF) zymogen TACE [TNFα (tumour necrosis factor α)-converting enzyme] is emerging as a centrepiece of mammalian cell signal transduction. Originally, it was described...

... by Hsp90 (heat-shock protein 90), a molecular chaperone that formed a tertiary complex with cPGES and CK-II. Treatment of cells with inhibitors of CK-II and Hsp90 and with a dominant-negative CK-II attenuated the formation of the cPGES–CK-II–Hsp90 complex and attendant cPGES phosphorylation and activation...

...Alexandre MARÉCHAL; Pierre-Luc TANGUAY; Mario CALLEJO; Renée GUÉRIN; Guy BOILEAU; Luis A. ROKEACH Folding of newly synthesized proteins within the ER (endoplasmic reticulum) is a rate-limiting step in protein secretion. Thus ER molecular chaperones and foldases have a major impact in determining...

...M. Satish KUMAR; P. Yadagiri REDDY; P. Anil KUMAR; Ira SUROLIA; G. Bhanuprakash REDDY α-Crystallin is a member of the small heat-shock protein family and functions like a molecular chaperone, and may thus help in maintaining the transparency of the eye lens by protecting the lens proteins from...

..., University of Gdańsk (e-mail [email protected] ). 12 10 2001 25 2 2002 4 4 2002 The Biochemical Society, London ©2002 2002 DNA helicase molecular chaperone replication complex inheritance replication-initiation protein Abbreviation used: ppGpp, guanosine 5...

... linkage, double- stranded RNA, endoplasmic reticulum, molecular chaperone. that the b and c chains form stable dimers before they are disulphide linked to each other. In contrast, the a chain (the Drosophila orthologue of the mammalian a5 chain) [14] did not associate with the monomeric b chain...

... the binding of multiple FKBP molecules to an unfolded INTRODUCTION Peptidyl-prolyl cis trans isomerase (PPIase), protein disulphide isomerase and various molecular chaperones have been identified as mediators of protein folding and assembly in ŠiŠo [1]. PPIases are classified into three distinct families...

... 2001 2001 domain structure molecular chaperone stress protein substrate binding Biochem. J. (2001) 354, 663 670 (Printed in Great Britain) 663 Substrate-binding characteristics of proteins in the 90 kDa heat shock protein family Takayuki K. NEMOTO1, Toshio ONO and Ki-ichiro TANAKA...