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Keywords: chaperone
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Articles
Daniel Fonseca, Samuel Gilberto, Cristina Ribeiro-Silva, Raquel Ribeiro, Inês Batista Guinote, Susana Saraiva, Ricardo A. Gomes, Élia Mateus, Ana Viana, Eduardo Barroso, Ana Ponces Freire, Patrick Freire, Carlos Cordeiro, Gonçalo da Costa
Journal:
Biochemical Journal
Biochem J (2016) 473 (14): 2225–2237.
Published: 12 July 2016
... deposits in Alzheimer's disease, dialysis-related amyloidosis and Parkinson's diseases. Human fibrinogen, an extracellular chaperone, was reported to specifically interact with a wide spectrum of stressed proteins and suppress their aggregation, being an interacting protein with TTR. Fibrinogen...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2016) 473 (1): 55–66.
Published: 09 December 2015
...Hyo Jung Kim; Ae-Ran Kwon; Bong-Jin Lee The DJ-1/ThiJ/ Pf pI superfamily is a group of proteins found in diverse organisms. This superfamily includes versatile proteins, such as proteases, chaperones, heat-shock proteins and human Parkinson's disease protein. Most members of the DJ-1/ThiJ/ Pf pI...
Includes: Supplementary data
Articles
Isabelle Petit-Härtlein, Kevin Rome, Eve de Rosny, Florian Molton, Carole Duboc, Erwan Gueguen, Agnès Rodrigue, Jacques Covès
Journal:
Biochemical Journal
Biochem J (2015) 472 (2): 205–216.
Published: 13 November 2015
... as a zinc-dependent chaperone activity was demonstrated for ZraP in Salmonella . We have purified ZraP from E. coli and shown that it is an octamer containing four interfacial metal-binding sites contributing to dimer stability. These sites are located close to the N-terminus, whereas the C-terminus...
Includes: Supplementary data
Articles
Ashish K. Mishra, Timur Mavlyutov, Deo R. Singh, Gabriel Biener, Jay Yang, Julie A. Oliver, Arnold Ruoho, Valerică Raicu
Journal:
Biochemical Journal
Biochem J (2015) 466 (2): 263–271.
Published: 20 February 2015
... by various synthetic molecules including (+)-pentazocine, cocaine and haloperidol and endogenous molecules such as sphingosine, dimethyltryptamine and dehydroepiandrosterone. Ligand-regulated protein chaperone functions linked to oxidative stress and neurodegenerative disorders such as amyotrophic lateral...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2015) 465 (1): 115–125.
Published: 12 December 2014
...Rooban B. Nahomi; Michael A. DiMauro; Benlian Wang; Ram H. Nagaraj Previous studies have identified peptides in the ‘crystallin-domain’ of the small heat-shock protein (sHSP) α-crystallin with chaperone and anti-apoptotic activities. We found that peptides in heat-shock protein Hsp20 (G 71...
Articles
Journal:
Biochemical Journal
Biochem J (2014) 462 (1): e1–e3.
Published: 24 July 2014
...Darius J. R. Lane; Des R. Richardson How is cellular iron (Fe) uptake and efflux regulated in mammalian cells? In this issue of the Biochemical Journal , Yanatori et al. report for the first time that a member of the emerging PCBP [poly(rC)-binding protein] Fe-chaperone family, PCBP2, physically...
Articles
Journal:
Biochemical Journal
Biochem J (2014) 461 (2): 189–203.
Published: 26 June 2014
... -neutralization activity by ~90% and significantly decreased chaperone and protease activities, indicating that these activities are intrinsic to plasmoDJ1. The plasmoDJ1 gene knockout in Plasmodium berghei ANKA attenuated virulence and reduced oocyst production, suggesting a major role for plasmoDJ1 in parasite...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2014) 458 (3): 459–467.
Published: 28 February 2014
...Joseph R. Tran; Jeffrey L. Brodsky The 26S proteasome is responsible for most regulated protein turnover and for the degradation of aberrant proteins in eukaryotes. The assembly of this ~2.5 MDa multicatalytic protease requires several dedicated chaperones and, once assembled, substrate selectivity...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2014) 457 (1): 99–105.
Published: 10 December 2013
.... WT-ED-LDLR promoted autocatalytic cleavage of pro-PCSK9. The findings of the present study indicate that the binding of WT-ED-LDLR to pro-PCSK9 in the ER promotes autocatalytic cleavage of PCSK9, and autocatalytically cleaved PCSK9 acts as a chaperone to promote the exit of WT-ED-LDLR from the ER...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2013) 454 (2): 217–225.
Published: 09 August 2013
...Kuljit Singh; Aliabbas A. Saleh; Ankan K. Bhadra; Ipsita Roy Maintenance of cellular redox homoeostasis forms an important part of the cellular defence mechanism and continued cell viability. Despite extensive studies, the role of the chaperone Hsp104 (heat-shock protein of 102 kDa) in propagation...
Articles
Paola Pietroni, Nishi Vasisht, Jonathan P. Cook, David M. Roberts, J. Michael Lord, Rasmus Hartmann-Petersen, Lynne M. Roberts, Robert A. Spooner
Journal:
Biochemical Journal
Biochem J (2013) 453 (3): 435–445.
Published: 12 July 2013
... compete for a binding site on the regulatory particle of the 26S proteasome, but their fates differ. Casein is degraded, but the mammalian 26S proteasome AAA (ATPase associated with various cellular activities)-ATPase subunit RPT5 acts as a chaperone that prevents aggregation of denatured RTA...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2013) 449 (1): 25–37.
Published: 07 December 2012
... inject them directly into hosts. Of these, the Sec system is ubiquitous, essential and by far the best understood. Secretory polypeptides are sorted from cytoplasmic ones initially due to characteristic signal peptides. Then they are targeted to the plasma membrane by chaperones/pilots. The translocase...
Articles
Journal:
Biochemical Journal
Biochem J (2012) 448 (3): 343–352.
Published: 21 November 2012
... fibril aggregates. The sHsp (small heat-shock protein) αB-crystallin acts as a molecular chaperone to prevent both amorphous and fibrillar protein aggregation; however, the precise molecular mechanisms behind its chaperone action are incompletely understood. To investigate whether the chaperone activity...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2012) 442 (2): 335–343.
Published: 13 February 2012
... of CPDH activity, both, in vivo and in vitro . HemW could bind haem covalently and could transfer haem to a membrane component in vitro , suggesting a function of HemW as a haem chaperone. HemW (10 μM) was loaded with haem by overnight incubation with an equimolar concentration of haem at room...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2012) 442 (1): 85–93.
Published: 27 January 2012
... (envelope stress response) pathways of enteric bacteria are critical for maintenance of the envelope against these antimicrobial agents. In the present study, we demonstrate that the periplasmic protein ZraP contributes to envelope homoeostasis and assign both chaperone and regulatory function to ZraP from...
Articles
Journal:
Biochemical Journal
Biochem J (2012) 441 (2): 685–696.
Published: 21 December 2011
... and pharmacological chaperones {TUDCA (tauroursodeoxycholate sodium salt), 4-PBA (sodium 4-phenylbutyrate) and the cGMP analogue CPT-cGMP [8-(4-chlorophenylthio)-cGMP]} differentially reduced degradation and/or promoted plasma-membrane localization of defective subunits. Improved subunit maturation was concordant...
Articles
Journal:
Biochemical Journal
Biochem J (2012) 441 (1): 387–397.
Published: 14 December 2011
...Xiaofeng Wang; Xin-an Lu; Xiaomin Song; Wei Zhuo; Lin Jia; Yushan Jiang; Yongzhang Luo Hsp90 (heat-shock protein 90) is one of the most important molecular chaperones in eukaryotes. Hsp90 facilitates the maturation, activation or degradation of its client proteins. It is now well accepted that both...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2011) 439 (2): 321–332.
Published: 28 September 2011
... 2011 chaperone immunosuppressant infection membrane biogenesis periplasmic peptidylprolyl cis – trans isomerase (periplasmic PPIase) protein folding survival PPIases (peptidylprolyl cis – trans isomerases) catalyse the cis – trans isomerization of peptidyl-prolyl bonds...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2011) 435 (1): 127–142.
Published: 15 March 2011
... and/or substrate specificity, we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase and on the suppression of aggregation of a non-foldable polyQ (polyglutamine)-expanded Huntingtin fragment. Overexpressed chaperones that suppressed polyQ aggregation were found...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2010) 432 (2): 275–282.
Published: 12 November 2010
... of classical and dynamic light scattering and NMR spectroscopy to demonstrate that AHSP forms a heterodimeric complex with α o that inhibits α o aggregation and promotes α o folding in the absence of haem. These findings indicate that AHSP may function as an α o -specific chaperone, and suggest an important...
Includes: Supplementary data
Articles
Vita Chien, Jacqueline F. Aitken, Shaoping Zhang, Christina M. Buchanan, Anthony Hickey, Thomas Brittain, Garth J. S. Cooper, Kerry M. Loomes
Journal:
Biochemical Journal
Biochem J (2010) 432 (1): 113–121.
Published: 25 October 2010
... diabetes mellitus). In the present study, we have investigated the possible effects on hA misfolding of the chaperones HSP (heat-shock protein) 70, GRP78/BiP (glucose-regulated protein of 78 kDa/immunoglobulin heavy-chain-binding protein) and HSP40/DnaJ. We demonstrate that hA underwent spontaneous time...
Articles
Journal:
Biochemical Journal
Biochem J (2010) 429 (3): 553–563.
Published: 14 July 2010
...Anna C. Y. Fan; Lisandra M. Gava; Carlos H. I. Ramos; Jason C. Young The mitochondrial import receptor Tom70 (translocase of the mitochondrial outer membrane 70) interacts with chaperone–preprotein complexes through two domains: one that binds Hsp70 (heat-shock protein 70)/Hsc70 (heat-shock cognate...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2010) 429 (1): 157–169.
Published: 14 June 2010
...Xin-Miao Fu; Bao Ting Zhu Members of the PDI (protein disulfide-isomerase) family are critical for the correct folding of secretory proteins by catalysing disulfide bond formation as well as by serving as molecular chaperones to prevent protein aggregation. In the present paper, we report...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2009) 421 (2): 273–282.
Published: 26 June 2009
...Jan K. Jensen; Klavs Dolmer; Christine Schar; Peter G. W. Gettins RAP (receptor-associated protein) is a three domain 38 kDa ER (endoplasmic reticulum)-resident protein that is a chaperone for the LRP (low-density lipoprotein receptor-related protein). Whereas RAP is known to compete for binding...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2009) 421 (1): 71–77.
Published: 12 June 2009
...Yo-hei Watanabe; Yosuke Nakazaki; Ryoji Suno; Masasuke Yoshida The ClpB chaperone forms a hexamer ring and rescues aggregated proteins in co-operation with the DnaK system. Each subunit of ClpB has two nucleotide-binding modules, AAA (ATPase associated with various cellular activities)-1 and AAA-2...
Articles
Vincenzo Zara, Alessandra Ferramosca, Philippe Robitaille-Foucher, Ferdinando Palmieri, Jason C. Young
Journal:
Biochemical Journal
Biochem J (2009) 419 (2): 369–375.
Published: 27 March 2009
... cleavable presequences which are not essential for targeting, but have some other function before import. The cytosolic chaperones Hsc70 (heat-shock cognate 70) and Hsp90 (heat-shock protein 90) complex with carrier precursors and interact specifically with the Tom (translocase of the mitochondrial outer...
Includes: Supplementary data
Articles
Charlotte Nerelius, Emily Martin, Siwei Peng, Magnus Gustafsson, Kerstin Nordling, Timothy Weaver, Jan Johansson
Journal:
Biochemical Journal
Biochem J (2008) 416 (2): 201–209.
Published: 12 November 2008
... to non-helical conformations. Mutations in the Brichos domain of proSP-C may lead to ILD via loss of CTC chaperone function. 1 To whom correspondence should be addressed (email [email protected] ). 15 5 2008 9 7 2008 22 7 2008 22 7 2008 © The Authors Journal...
Articles
Journal:
Biochemical Journal
Biochem J (2008) 413 (3): 447–457.
Published: 15 July 2008
... of this position. The function of the distant U-box protein, AtPUB49, representing a large family of eukaryotic proteins containing a U-box linked to a cyclophilin-like peptidyl-prolyl cis – trans isomerase domain, was characterized biochemically. AtPUB49 functioned both as a prolyl isomerase and a chaperone...
Includes: Supplementary data
Articles
Journal:
Biochemical Journal
Biochem J (2008) 413 (1): 1–13.
Published: 12 June 2008
... PARK1 and PARK4 Unknown Cytoplasm/membranes Aggregation/reduced proteasomal activity Parkin PARK2 E3 Cytoplasm Loss of E3 activity* UCH-L1 PARK5 DUB/E3† Cytoplasm Reduced DUB/E3 activity DJ-1 PARK7 Chaperone Mitochondrial Loss of chaperone/antioxidant activity PINK1...
Articles
Journal:
Biochemical Journal
Biochem J (2008) 413 (1): 15–28.
Published: 12 June 2008
... of chloroplasts, to form an uninterrupted passageway for preproteins from the cytoplasm into the stroma. The TIC translocon also consists of a membrane channel and a set of components that mediate the interaction of preproteins with molecular chaperones as they emerge into the stroma from the TIC channel [ 7 – 10...
Articles
Journal:
Biochemical Journal
Biochem J (2008) 412 (2): 389–397.
Published: 14 May 2008
... was found to be crucial for the survival of these enteric bacteria under extremely low pH conditions. We recently demonstrated that HdeA is able to exhibit chaperone-like activity exclusively within the stomach pH range by transforming from a well-folded conformation at higher pH values (above pH 3...
Articles
Journal:
Biochemical Journal
Biochem J (2008) 412 (1): 73–80.
Published: 25 April 2008
...Eleanor W. Trotter; Jonathan D. Rand; Jill Vickerstaff; Chris M. Grant The yeast Tsa1 peroxiredoxin, like other 2-Cys peroxiredoxins, has dual activities as a peroxidase and as a molecular chaperone. Its peroxidase function predominates in lower-molecular-mass forms, whereas a super-chaperone form...
Articles
Journal:
Biochemical Journal
Biochem J (2008) 409 (3): 691–699.
Published: 15 January 2008
..., increasing the probability of unfolding and aggregation events occurring. It is hypothesized that the α-crystallin molecular chaperone system recognizes and binds these proteins before they can form the light-scattering centres that result in cataract, thus maintaining the long-term transparency of the lens...
Articles
Journal:
Biochemical Journal
Biochem J (2008) 409 (3): 771–777.
Published: 15 January 2008
...Ashis Biswas; Benlian Wang; Masaru Miyagi; Ram H. Nagaraj α-Crystallin prevents protein aggregation under various stress conditions through its chaperone-like properties. Previously, we demonstrated that MGO (methylglyoxal) modification of αA-crystallin enhances its chaperone function and thus may...
Articles
Chhanda Biswas, Olga Ostrovsky, Catherine A. Makarewich, Sherry Wanderling, Tali Gidalevitz, Yair Argon
Journal:
Biochemical Journal
Biochem J (2007) 405 (2): 233–241.
Published: 27 June 2007
... containing 0.1 mM CaCl 2 (buffer A). calcium store chaperone endoplasmic reticulum (ER) glucose-regulated protein of 94 kDa (GRP94) heat-shock protein (HSP) GRP94 (glucose-regulated protein of 94 kDa), also known as gp96 (glycoprotein 96), is an ER (endoplasmic reticulum) molecular...
Articles
Heath Ecroyd, Sarah Meehan, Joseph Horwitz, J. Andrew Aquilina, Justin L. P. Benesch, Carol V. Robinson, Cait E. Macphee, John A. Carver
Journal:
Biochemical Journal
Biochem J (2007) 401 (1): 129–141.
Published: 11 December 2006
... these mimics to undertake a mechanistic and structural invest-igation of the effect of phosphorylation on the chaperone activity of αB-crystallin to protect against two types of protein misfolding, i.e. amorphous aggregation and amyloid fibril assembly. We show that mimicking phosphorylation of αB-crystallin...
Articles
Journal:
Biochemical Journal
Biochem J (2006) 397 (2): 355–367.
Published: 28 June 2006
... and 1×PIM. chaperone murine double minute clone 2 oncoprotein (MDM2) p53 protein folding ubiquitin The p53 protein is a tumour suppressor that functions as a transcription factor at a key nodal point in the response of cells to environmental change. p53 protein is active...
Articles
Journal:
Biochemical Journal
Biochem J (2006) 396 (1): 31–39.
Published: 26 April 2006
...Fang-Chun Sun; Shou Wei; Chia-Wei Li; Yuo-Sheng Chang; Chih-Chung Chao; Yiu-Kay Lai The ubiquitously expressed molecular chaperone GRP78 (78 kDa glucose-regulated protein) generally localizes to the ER (endoplasmic reticulum). GRP78 is specifically induced in cells under the UPR (unfolded protein...
Articles
Journal:
Biochemical Journal
Biochem J (2005) 392 (1): 145–152.
Published: 08 November 2005
... 2005 29 7 2005 29 7 2005 The Biochemical Society, London 2005 chaperone heat-shock cognate 70 (Hsc70) heat-shock factor 1 (HSF1) heat-shock protein 70 (Hsp70) stress response Various physiological and cellular stresses can disrupt essential cellular signalling pathways...
Articles
Anton V. Zavialov, Vladimir M. Tischenko, Laura J. Fooks, Bjørn O. Brandsdal, Johan Åqvist, Vladimir P. Zav'yalov, Sheila Macintyre, Stefan D. Knight
Journal:
Biochemical Journal
Biochem J (2005) 389 (3): 685–694.
Published: 26 July 2005
...Anton V. Zavialov; Vladimir M. Tischenko; Laura J. Fooks; Bjørn O. Brandsdal; Johan Åqvist; Vladimir P. Zav'yalov; Sheila Macintyre; Stefan D. Knight Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 384 (3): 461–467.
Published: 07 December 2004
... unclear. In the present study, we demonstrate that in human melanoma cells CDK11 p110 and CDK11 p46 interact with Hsp90 (heat-shock protein 90) and its co-chaperone cdc37. Furthermore, we show that the treatment of cells with the Hsp90-specific inhibitor geldanamycin leads to ubiquitination and enhanced...
Articles
Ingrid BOURGES, Claire RAMUS, Bénédicte MOUSSON de CAMARET, Réjane BEUGNOT, Claire REMACLE, Pierre CARDOL, Götz HOFHAUS, Jean-Paul ISSARTEL
Journal:
Biochemical Journal
Biochem J (2004) 383 (3): 491–499.
Published: 26 October 2004
... several subcomplexes. One of these, containing the 23, 30 and 49 kDa subunits, also contained prohibitin. This is the first description of prohibitin interaction with complex I subunits and suggests that this protein might play a role in the assembly or degradation of mitochondrial complex I. chaperone...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 383 (3): 589–597.
Published: 26 October 2004
... to be a general folding assistant for secretory proteins and to probably function as a PDI (protein disulphide isomerase)-like molecular chaperone. In the present paper, we report the first purification to homogeneity and direct functional analysis of native ERp29, which has led to the unexpected finding...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 383 (1): 165–170.
Published: 24 September 2004
... functions have been ascribed, such as translation inhibition, regulation of purine repressor or calpain activation. Owing to a limited sequence similarity to Hsp90 (heat-shock protein 90), they have also been proposed to be molecular chaperones; however, this has never been tested. In the present paper, we...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 381 (3): 803–811.
Published: 27 July 2004
... correspondence should be addressed (e-mail [email protected] ). 2 3 2004 19 4 2004 5 5 2004 5 5 2004 The Biochemical Society, London 2004 chaperone chelator copper neocuproine P-ATPase transporter Plasmodium falciparum Malaria infects hundreds of millions...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 381 (1): 249–255.
Published: 22 June 2004
...Annamaria GUAGLIARDI; Lucia MANCUSI; Mosè ROSSI In eukaryotic cells and in Escherichia coli , reversion of protein aggregation is mediated by the network of chaperones belonging to Hsp70 and Hsp100 families [Weibezahn, Bukau and Mogk (2004) Microb. Cell Fact. 3 , 1–12]. The thermophilic prokaryotes...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 379 (1): e1–e2.
Published: 01 April 2004
... affinity chromatography chaperone 14-3-3 protein phosphoprotein proteomic analysis serine/threonine phosphorylation Biochem. J. (2004) 379, e1 e2 (Printed in Great Britain) e1 COMMENTARY Master of all things phosphorylated Michael B. YAFFE1 Center for Cancer Research, Massachusetts Institute...
Articles
Journal:
Biochemical Journal
Biochem J (2004) 378 (3): 793–799.
Published: 15 March 2004
...Xueji WU; Mihiro YANO; Hiroyo WASHIDA; Hiroshi KIDO The chaperone activity of Hsp70 (70 kDa heat-shock protein) in protein folding and its conformational switch, including oligomeric and monomeric interconversion, are regulated by the hydrolysis of ATP and the ATP–ADP exchange cycle. The crystal...
Articles
Journal:
Biochemical Journal
Biochem J (2003) 374 (2): 433–441.
Published: 01 September 2003
... target Hsp90. Both drugs were found to bind directly wild-type Hsp90 via the N- and C-terminal domains. Both drugs strongly suppressed the in vitro chaperone activity of native Hsp90 towards citrate synthase at 1.5–3.0 μM. Amlexanox suppressed C-terminal chaperone activity in vitro , but not N-terminal...
Articles
Journal:
Biochemical Journal
Biochem J (2003) 370 (3): 849–857.
Published: 15 March 2003
... regarding the detailed mechanism by which LKB1 regulates cell growth. In this study we have purified LKB1 from cells and establish that it is associated with the heat-shock protein 90 (Hsp90) chaperone and the Cdc37 kinase-specific targetting subunit for Hsp90. We demonstrate that Cdc37 and Hsp90 bind...
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