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Protein Refolding

Known as: Refolding, Protein 
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones… Expand
National Institutes of Health

Papers overview

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Review
2005
Review
2005
Inclusion bodies produced in Escherichia coli are composed of densely packed denatured protein molecules in the form of particles… Expand
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Highly Cited
2004
Highly Cited
2004
Spidroins, the major silk proteins making up the spider's dragline silk, originate in two distinct tissue layers (A and B) in the… Expand
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Highly Cited
2003
Highly Cited
2003
Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that bind denatured proteins in vitro, thereby facilitating… Expand
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Review
2002
Review
2002
The rapid provision of purified native protein underpins both structural biology and the development of new biopharmaceuticals… Expand
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Review
2001
Review
2001
Diverse human disorders, including several neurodegenerative diseases and systemic amyloidosis, are thought to arise from the… Expand
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Highly Cited
2000
Highly Cited
2000
The in vitro refolding of hen egg-white lysozyme is studied in the presence of various osmolytes. Proline is found to prevent… Expand
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Highly Cited
2000
Highly Cited
2000
We have studied the effects of macromolecular crowding on protein folding kinetics by studying the oxidative refolding of hen… Expand
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Highly Cited
1999
Highly Cited
1999
High hydrostatic pressures (1-2 kbar), combined with low, nondenaturing concentrations of guanidine hydrochloride (GdmHCl) foster… Expand
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Highly Cited
1996
Highly Cited
1996
The role of the abundant stress protein Hsp90 in protecting cells against stress-induced damage is not well understood. The… Expand
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Highly Cited
1996
Highly Cited
1996
The properties of molecular chaperones in protein-assisted refolding were examined in vitro using recombinant human cytosolic… Expand
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