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 …

[HTML][HTML] The Hsp70 and Hsp60 chaperone machines

B Bukau, AL Horwich - Cell, 1998 - cell.com
An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

Protein folding in the cell

MJ Gething, J Sambrook - Nature, 1992 - nature.com
In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

[PDF][PDF] The roles of heat shock proteins in plants

E Vierling - Annual review of plant physiology and plant molecular …, 1991 - researchgate.net
Environmental conditions that change temperature, light environment, water status, or
hormone balance lead to altered gene expression in plants. At the molecular level, one of …

Molecular biology of prion diseases

SB Prusiner - Science, 1991 - science.org
Prions cause transmissible and genetic neurodegenerative diseases, including scrapie and
bovine spongiform encephalopathy of animals and Creutzfeldt-Jakob and Gerstmann …

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

Z Xu, AL Horwich, PB Sigler - Nature, 1997 - nature.com
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit
protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli …

A large-conductance mechanosensitive channel in E. coli encoded by mscL alone

SI Sukharev, P Blount, B Martinac, FR Blattner, C Kung - Nature, 1994 - nature.com
ALL cellular organisms respond to vibration, touch, gravity or changes in osmolarity,
although the molecules on which such mechanosensations depend are unknown …

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

K Braig, Z Otwinowski, R Hegde, DC Boisvert… - Nature, 1994 - nature.com
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made
of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry …

Biogenesis and metabolic maintenance of Rubisco

A Bracher, SM Whitney, FU Hartl… - Annual review of plant …, 2017 - annualreviews.org
Ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) mediates the fixation of
atmospheric CO2 in photosynthesis by catalyzing the carboxylation of the 5-carbon sugar …

Heat shock, stress proteins, chaperones, and proteotoxicity

LE Hightower - Cell, 1991 - cell.com
Cold Spring Harbor was the scene of the first international heat shock meeting, held in 1982
on the 20th anniversary year of Ferruccio Ritossa's discovery of the heat shock response …