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Keywords: protein folding
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Articles
Biochem J (2019) 476 (23): 3631–3647.
Published: 10 December 2019
... obtained from the fits. These values are collected in Supplementary Table S4 , where additional details of the fitting process are provided. Unlike unfolding, which often occurs in a single kinetic phase, protein folding is typically a complex process involving several parallel kinetic channels...
Includes: Supplementary data
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Biochem J (2019) 476 (11): 1653–1677.
Published: 14 June 2019
... protein folding Molecular chaperones play key roles in maintaining cellular protein health, facilitating protein targeting, and ensuring high-fidelity protein biosynthesis. Central players among molecular chaperones are the 70-kDa heat-shock proteins, or Hsp70s, which occur in virtually all...
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Biochem J (2016) 473 (20): 3705–3724.
Published: 11 October 2016
...Beata Adamczak; Miłosz Wieczór; Mateusz Kogut; Janusz Stangret; Jacek Czub Osmolytes are a class of small organic molecules that shift the protein folding equilibrium. For this reason, they are accumulated by organisms under environmental stress and find applications in biotechnology where proteins...
Includes: Supplementary data
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Biochem J (2016) 473 (15): 2273–2293.
Published: 28 July 2016
... on behalf of the Biochemical Society 2016 allosteric regulation heparin metastability polymerization proteinase inhibition protein folding receptor binding serpin The initial identification of a relationship that would grow into the serpin superfamily of proteins was made in 1980...
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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 (2014) 461 (2): 213–222.
Published: 26 June 2014
... temperature. Next the cells were washed again twice with PBS before being submitted to FACS analysis. biophysics HIV HIV entry inhibitor membrane fusion membrane protein protein folding HIV-1 entry into the cells is blocked by alteration in the levels of Chol (cholesterol) and sphingolipids...
Includes: Supplementary data
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Biochem J (2014) 461 (1): 107–113.
Published: 13 June 2014
... formation is negatively regulated by the product of its catalytic activity. disulfide formation endoplasmic reticulum endoplasmic reticulum oxidase 1 (Ero1) protein disulfide isomerase (PDI) protein folding The formation of disulfides within proteins entering the secretory pathway...
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Biochem J (2011) 439 (2): 321–332.
Published: 28 September 2011
...Ikenna R. Obi; Roland Nordfelth; Matthew S. Francis Periplasmic PPIases (peptidylprolyl cis – trans isomerases) catalyse the cis – trans isomerization of peptidyl-prolyl bonds, which is a rate-limiting step during protein folding. We demonstrate that the surA , ppiA , ppiD , fkpA and fklB alleles...
Includes: Supplementary data
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Biochem J (2011) 435 (2): 391–399.
Published: 29 March 2011
... calsequestrin catecholaminergic polymorphic ventricular tachycardia (CPVT) metal ion molecular dynamics protein folding proteolysis The interaction between metal ions and proteins plays an essential role in cellular physiology and is vital for the co-ordinated functioning of many organs, including...
Includes: Supplementary data
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Biochem J (2011) 434 (1): 143–151.
Published: 27 January 2011
... and Allergy, Brigham and Women's Hospital, Boston, MA 02115, U.S.A. 4 To whom correspondence should be addressed (email sarah.perrett@cantab.net ). 16 11 2010 23 11 2010 23 11 2010 © The Authors Journal compilation © 2011 Biochemical Society 2011 amyloid mutant protein...
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Biochem J (2010) 426 (2): 197–203.
Published: 09 February 2010
... be addressed (email gomes@itqb.unl.pt ). 19 10 2009 24 11 2009 14 12 2009 14 12 2009 © The Authors Journal compilation © 2010 Biochemical Society 2010 frataxin iron–sulfur cluster Isu metallochaperone protein folding Yfh1 Reduced expression of frataxin...
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Biochem J (2009) 419 (3): 595–602.
Published: 14 April 2009
... of the TSP C-terminus in isolation. 16 7 2008 15 1 2009 5 2 2009 5 2 2009 © The Authors Journal compilation © 2009 Biochemical Society 2009 P22 tailspike protein assembly protein folding viral adhesion protein TSP (P22 tailspike protein) is the adhesion protein...
Includes: Supplementary data
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Biochem J (2009) 417 (3): 651–666.
Published: 16 January 2009
...@ualberta.ca ). 12 9 2008 6 10 2008 8 10 2008 © The Authors Journal compilation © 2009 Biochemical Society 2009 calcium homoeostasis calreticulin endoplasmic reticulum (ER) protein folding quality control The ER (endoplasmic reticulum) plays a vital role in many...
Includes: Multimedia, Supplementary data
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Biochem J (2008) 416 (2): 201–209.
Published: 12 November 2008
... and the transmembrane domain, were associated with altered intracellular trafficking, but not aggregation [ 18 , 19 ]. amyloid Brichos domain chaperone interstitial lung disease prosurfactant protein C (proSP-C) protein folding Human lung surfactant protein C (SP-C), a hydrophobic 35-residue acylated...
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Biochem J (2008) 413 (1): 29–36.
Published: 12 June 2008
... folding of CFTR in the ER, we constructed double-cysteine CFTR mutants that would be retained in the ER and only undergo cross-linking when the protein folds into a native structure. The mature form, but not the immature forms, of M348C(TM6)/T1142C(TM12) (where TM is transmembrane segment), T351C(TM6...
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Biochem J (2008) 411 (1): 115–122.
Published: 13 March 2008
... but not to the oxidized protein, at a molar ratio of 1:1 in vitro , with a sub-nanomolar dissociation constant, suggesting a potential role for zinc in protecting the reduced protein from oxidation [ 10 , 11 ]. cysteine redox potential disulfide bond formation glutathione mitochondrial import protein folding...
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Biochem J (2007) 406 (2): e1.
Published: 13 August 2007
...William R. Skach Protein folding disorders comprise a rapidly growing group of diseases that involve virtually every organ system and affect individuals of all ages. Their principal pathology is the inability of a protein to acquire or maintain its physiological three-dimensional structure...
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Biochem J (2005) 389 (3): 685–694.
Published: 26 July 2005
... chaperone/usher pathway protein stability protein folding Most Gram-negative pathogens express adhesive surface organelles that allow them to specifically target and bind to host tissues and cause infection. A periplasmic chaperone/usher machinery is used for the controlled assembly of many...
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Biochem J (2005) 387 (2): 479–488.
Published: 05 April 2005
... for at least 1 h. affinity tag choline-binding module C-LytA partly folded state protein folding β-solenoid LytA amidase, the major murein hydrolase from Streptococcus pneumoniae , catalyses the cleavage of the N -acetylmuramoyl- L -alanine bond of the peptidoglycan backbone [ 1...
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Biochem J (2004) 380 (2): 441–448.
Published: 01 June 2004
... or in the retention of misfolded proteins. These observations suggest the existence of a highly stringent quality control mechanism in the ER of S. pombe that might reduce the secretion efficiency of endogenous proteins. Key words: calnexin, endoplasmic reticulum, molecular chaper- one, protein folding, secretion...
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Biochem J (2003) 374 (3): 785–792.
Published: 15 September 2003
... with Arrhenius formalism estimates a kinetic barrier to irreversible denaturation for Klentaq that is significantly higher than that for Klenow. Key words: CD, differential scanning calorimetry, protein folding, Taq polymerase, thermophilic. INTRODUCTION Full-length DNA polymerase 1 from Thermus aquaticus (Taq...
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Biochem J (2003) 371 (3): 965–972.
Published: 01 May 2003
... and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/or thioredoxin reductase promote the functional folding of citrate synthase and α-glucosidase after urea denaturation. They also promote...
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Biochem J (2003) 370 (3): 805–815.
Published: 15 March 2003
... to several important proteins in this compartment. Key words: autophosphorylation, protein folding, protein protein interaction, targeting, Tom40p. found associated with different cellular compartments, including cytosol [1,15], plasma membrane [15], nucleus [16] and mito- chondria [17 22]. With regard...
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Biochem J (2002) 365 (2): 505–511.
Published: 15 July 2002
... synthesis to elucidate their physiological functions and pathological effects. inflammation PLA 2 protein folding solid phase peptide synthesis SPPS Abbreviations used: PLA 2 , phospholipase A 2 ; cPLA 2 , cytosolic phospholipase A 2 ; iPLA 2 , calcium-independent PLA 2 ; sPLA 2 , secretory...
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Biochem J (2001) 358 (1): 269–274.
Published: 08 August 2001
... correspondence should be addressed (e-mail jrw@crc.dk ). 29 3 2001 31 5 2001 15 6 2001 The Biochemical Society, London ©2001 2001 carboxypeptidase Y protein folding Saccharomyces cerevisiae thiol oxidation Abbreviations used: proCPY, procarboxypeptidase Y; ER...
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Biochem J (2001) 356 (3): 685–704.
Published: 08 June 2001
... protein, protein folding, P-type ATPases. of about 100 kDa with usually ten predicted transmembrane spans and four intracellular loops that differ greatly in length. A large fraction of the mass of the protein is found in the L4 5 intracellular loop, which has long been known to be the location of the ATP...
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Biochem J (2001) 354 (3): 553–559.
Published: 08 March 2001
... binding protein folding xenoestrogen Biochem. J. (2001) 354, 553 559 (Printed in Great Britain) 553 The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands Peter KLAPPA*1, Robert B. FREEDMAN*, Martina LANGENBUCH*, Michael S. LAN‹, Gary K. ROBINSON...
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Biochem J (2000) 350 (3): 873–881.
Published: 08 September 2000
... of surrounding modules or other molecular partners. 1 To whom correspondence should be addressed (e-mail andre.zapun@ibs.fr ). 28 2 2000 23 6 2000 13 7 2000 The Biochemical Society, London © 2000 2000 amyloidosis disulphide bond protein folding Biochem. J. (2000) 350...
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Biochem J (2000) 347 (3): 771–779.
Published: 25 April 2000
... ectodomain expressed in Lec8 cells was produced in quantity in a bioreactor for subsequent structural analysis. Key words: autophosphorylation, biosynthesis, insulin binding, mutagenesis, protein folding. glycosylated and proteolytically processed to a and b chains during transport to the cell surface [7 10...
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Biochem J (2000) 345 (3): 467–472.
Published: 25 January 2000
... with sHsps [2] ; however, its mechanism of action is still poorly understood. It was thought to be incapable of protecting enzyme activity against thermal inactivation [6] but such protection was provided for catalase [11]. There are contradictory results for the role of a- crystallin in protein folding...
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Biochem J (1999) 344 (3): 659–665.
Published: 08 December 1999
... N-glycan processing, in terms of maturation and catalytical activity. dopa-oxidase activity endomannosidase protein folding melanogenesis N-butyldeoxynojirimicin TRP-1 Biochem. J. (1999) 344, 659 665 (Printed in Great Britain) 659 Protein specific N-glycosylation of tyrosinase...