VHL, the story of a tumour suppressor gene

L Gossage, T Eisen, ER Maher - Nature Reviews Cancer, 2015 - nature.com
Abstract Since the Von Hippel–Lindau (VHL) disease tumour suppressor gene VHL was
identified in 1993 as the genetic basis for a rare disorder, it has proved to be of wide medical …

Molecular chaperones in cellular protein folding

FU Hartl - Nature, 1996 - nature.com
The folding of many newly synthesized proteins in the cell depends on a set of conserved
proteins known as molecular chaperones. These prevent the formation of misfolded protein …

The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

DA Parsell, S Lindquist - Annual review of genetics, 1993 - go.gale.com
Complex processes are involved in the protection of cells and organisms by heat shock
proteins (hsps). Aberrant protein production due to high temperatures is prevented by the …

Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system

J Verghese, J Abrams, Y Wang… - … and molecular biology …, 2012 - Am Soc Microbiol
The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response

BJ Lang, ME Guerrero, TL Prince, Y Okusha… - Archives of …, 2021 - Springer
Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

Folding of newly translated proteins in vivo: the role of molecular chaperones

J Frydman - Annual review of biochemistry, 2001 - annualreviews.org
▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

Chaperone-mediated protein folding

AL Fink - Physiological reviews, 1999 - journals.physiology.org
The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

Molten globule and protein folding

OB Ptitsyn - Advances in protein chemistry, 1995 - Elsevier
Publisher Summary This chapter describes the present state of the studies of the molten
globule state and its role in protein folding and physiological processes. Recent data on the …

Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease

IJ Benjamin, DR McMillan - Circulation research, 1998 - Am Heart Assoc
How a cell responds to stress is a central problem in cardiovascular biology. Diverse
physiological stresses (eg, heat, hemodynamics, mutant proteins, and oxidative injury) …

Molecular chaperones and protein folding in plants

RS Boston, PV Viitanen, E Vierling - … control of gene expression in plants, 1996 - Springer
Protein folding in vivo is mediated by an array of proteins that act either as 'foldases' or
'molecular chaperones'. Foldases include protein disulfide isomerase and peptidyl prolyl …