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Keywords: molecular chaperone
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Biochem Soc Trans (2014) 42 (6): 1744–1751.
Published: 17 November 2014
...A. Graham Pockley; Brian Henderson; Gabriele Multhoff Although heat-shock (cell stress) proteins are commonly considered as being intracellular molecular chaperones that undertake a number of cytoprotective and cellular housekeeping functions, there is now a wealth of evidence to indicate...
Biochem Soc Trans (2011) 39 (1): 94–98.
Published: 19 January 2011
...Peter Lund It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding...
Biochem Soc Trans (2007) 35 (5): 835–847.
Published: 25 October 2007
... years ago, and, since then, research in this area has expanded on a global scale. In this review, the key discoveries in this field are summarized, and recent studies of bacterial twin-arginine signal-peptide-binding proteins are discussed. membrane protein membrane transport molecular chaperone...
Biochem Soc Trans (2005) 33 (4): 551–552.
Published: 01 August 2005
... apoptosis hsp molecular chaperone motoneuron therapeutic target Neurodegenerative diseases are characterized by changes in protein structure, which result in misfolding and aggregation. Molecular chaperones such as hsps (heat-shock proteins) are thought to play a critical role in preventing...
Biochem Soc Trans (2005) 33 (1): 124–126.
Published: 01 February 2005
... processes governing assembly and export of Tat-dependent enzymes. molecular chaperone molybdopterin cofactor protein–protein interactions Tat protein transport system trimethylamine N -oxide (TMAO) reductase twin-arginine signal peptide TMAO (trimethylamine N -oxide) is a nitrogen...
Biochem Soc Trans (2005) 33 (1): 105–107.
Published: 01 February 2005
... molecular chaperone [NiFe] hydrogenase protein–protein interaction Tat protein transport system N -oxide reductase twin-arginine signal peptide Escherichia coli displays a remarkable flexibility in its respiratory electron transport processes. As an obligate anaerobe, E. coli can utilize...
Biochem Soc Trans (2004) 32 (4): 643–645.
Published: 01 August 2004
... 2004 heat-shock protein immunophilin molecular chaperone proteasome retinal degeneration tetratricopeptide repeat LCA (Leber's congenital amaurosis) is inherited in an autosomal recessive manner and is characterized by severely impaired vision or blindness at birth. Mutations in AIPL1...