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Keywords: molecular chaperone
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Biochem J (2017) 474 (20): 3439–3454.
Published: 05 October 2017
.... This possibility emerged from the realisation that TorA has a significant level of amino acid sequence identity with ClpB [ 3 , 16 ], a member of the AAA+ superfamily that acts as a molecular chaperone in bacteria. Subsequently, studies have shown that TorA can reactivate heat-denatured luciferase in vitro [ 22...
Includes: Supplementary data
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Biochem J (2017) 474 (4): 445–469.
Published: 03 February 2017
... 2016 14 12 2016 © 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society 2017 molecular chaperone post-translational modification proteasome protein quality control ubiquitin ligases The mammalian E3, gp78 [ 164 ], is another major E3...
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Biochem J (2016) 473 (2): 167–178.
Published: 05 January 2016
... molecular chaperone protein conformation protein inclusions In the present study, we have investigated the effect of a BRICHOS domain on artificial proteins (β23 and β17), designed to form six β-strands with alternating polar/non-polar amino acid side chains. The model proteins form amyloid-like...
Includes: Supplementary data
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Biochem J (2015) 466 (3): 561–570.
Published: 06 March 2015
.... 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...
Includes: Supplementary data
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Biochem J (2008) 411 (3): 605–611.
Published: 14 April 2008
... 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...
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Biochem J (2008) 411 (1): 191–199.
Published: 13 March 2008
... 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...
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Biochem J (2007) 404 (1): 159–167.
Published: 26 April 2007
...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...
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Biochem J (2005) 387 (3): 797–805.
Published: 26 April 2005
... to 50% sensitivity at the wavelength of maximum emission (λ max ). Scans were background-subtracted by placing the same buffer in the reference cell. a disintegrin and metalloproteinase (ADAM) cysteine switch molecular chaperone TNFα-converting enzyme (TACE) tumour necrosis factor (TNF...
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Biochem J (2004) 381 (1): 59–69.
Published: 22 June 2004
... 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...
Includes: Supplementary data
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Biochem J (2002) 364 (3): 857–862.
Published: 15 June 2002
..., University of Gdańsk (e-mail wegrzyn@biotech.univ.gda.pl ). 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...
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Biochem J (2001) 360 (1): 167–172.
Published: 08 November 2001
... the disulphide linkage. We suggest that interconversion of these bc dimers is crucial for the replaceable and selective assembly of the a chain for abc trimer formation. Key words: basement membrane, disulphide linkage, double- stranded RNA, endoplasmic reticulum, molecular chaperone. that the b and c chains...
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Biochem J (2001) 354 (3): 663–670.
Published: 08 March 2001
..., precipitation INTRODUCTION The molecular chaperone activity of the 90 kDa heat shock protein (HSP90) was first characterized in terms of the function and regulation of steroid hormone receptors [1 3]. The cast of the target substrates or client proteins has since grown to include various types of kinase...