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Keywords: chaperone
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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
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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
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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...
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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
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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
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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
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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...
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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
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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...
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Biochem J (2012) 442 (2): 335–343.
Published: 13 February 2012
... 2012 chaperone coproporphyrinogen III dehydrogenase (CPDH) cytochrome haem HemN trafficking HemW (10 μM) was loaded with haem by overnight incubation with an equimolar concentration of haem at room temperature in 50 mM Tris/HCl and 150 mM NaCl, pH 8. For haem discharge, 250 pmol...
Includes: Supplementary data
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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...
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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
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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
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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
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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
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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
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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
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Biochem J (2008) 413 (1): 1–13.
Published: 12 June 2008
...@leeds.ac.uk . 4 2 2008 22 4 2008 22 4 2008 © The Authors Journal compilation © 2008 Biochemical Society 2008 chaperone mitochondrion Parkinson's disease reactive oxygen species (ROS) ubiquitin Parkinson's disease (PD) is the second most common neurodegenerative disease...
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Biochem J (2008) 413 (1): 15–28.
Published: 12 June 2008
... these pathways and highlight the regulatory mechanisms that integrate the plastid protein-trafficking pathways with the developmental and metabolic state of the plant. © The Authors Journal compilation © 2008 Biochemical Society 2008 chaperone chloroplast plastid protein import protein targeting...
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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...
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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...
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Biochem J (2007) 405 (2): 233–241.
Published: 27 June 2007
... (buffer A). 14 12 2006 15 3 2007 5 4 2007 5 4 2007 © The Authors Journal compilation © 2007 Biochemical Society 2007 calcium store chaperone endoplasmic reticulum (ER) glucose-regulated protein of 94 kDa (GRP94) heat-shock protein (HSP) GRP94 (glucose...
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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...
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Biochem J (2006) 397 (2): 355–367.
Published: 28 June 2006
... defined. However, this second binding site of MDM2 is within a conformationally flexible motif known to be misfolded in human cancers [ 24 ], suggesting a link between p53 conformation and MDM2 binding. A chaperoning role for MDM2 in altering the folding of p53 might be required to assist in ubiquitin...
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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...
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Biochem J (2005) 392 (1): 145–152.
Published: 08 November 2005
... ). 11 3 2005 12 7 2005 29 7 2005 29 7 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 and inhibit...
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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...
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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...
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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...
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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...
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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...
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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...
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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...
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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...
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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...