...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...

...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...

... and Environmental Microbiology, College of Life Sciences, University of Dundee DD1 5EH, Scotland, U. K. (email fsargent@dundee.ac.uk ). 14 6 2007 © The Authors Journal compilation © 2007 Biochemical Society 2007 membrane protein membrane transport molecular chaperone protein–protein...

... The Biochemical Society 2005 amyotrophic lateral sclerosis 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...

... in the light of recent work with E. coli hydrogenase-2. 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...

... molybdopterin guanine dinucleotide Tat twin-arginine transport TMAO trimethylamine N -oxide 1 To whom correspondence should be addressed (email f.sargent@uea.ac.uk ). 15 9 2004 © 2005 The Biochemical Society 2005 molecular chaperone molybdopterin cofactor...

... be addressed (email j.spuy@ucl.ac.uk ). 16 4 2004 © 2004 The Biochemical Society 2004 heat-shock protein immunophilin molecular chaperone proteasome retinal degeneration tetratricopeptide repeat LCA (Leber's congenital amaurosis) is inherited in an autosomal recessive manner...