Hsp90 chaperones protein folding in vitro.

Molecular chaperones. Unfolding protein folding.

The therapeutic potential of chemical chaperones in protein folding diseases.

Protein folding in vitro.

Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations.

Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies.

Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease.

Molecular chaperones in cellular protein folding: the birth of a field.

Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60.

Protein folding, misfolding and quality control: the role of molecular chaperones.

Pharmacological folding chaperones act as allosteric ligands of Frizzled4.

Chaperones rescue luciferase folding by separating its domains.

Small molecule diselenide additives for in vitro oxidative protein folding.

Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.

Protein folding. Translational tuning optimizes nascent protein folding in cells.

Protein-catalysed protein folding.

Concepts in protein folding.

Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression.

Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.

The Hsp90 Co-chaperones Sti1, Aha1, and P23 Regulate Adaptive Responses to Antifungal Azoles.

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.

Protein folding in the cell.

Dominant forces in protein folding.

Pathway of protein folding.

Fast protein folding kinetics.

Suggest Documents

Molecular chaperones. Unfolding protein folding.

The therapeutic potential of chemical chaperones in protein folding diseases.

Protein folding in vitro.

Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations.

Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies.

Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease.

Molecular chaperones in cellular protein folding: the birth of a field.

Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60.

Protein folding, misfolding and quality control: the role of molecular chaperones.

Pharmacological folding chaperones act as allosteric ligands of Frizzled4.

Chaperones rescue luciferase folding by separating its domains.

Small molecule diselenide additives for in vitro oxidative protein folding.

Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.

Protein folding. Translational tuning optimizes nascent protein folding in cells.

Protein-catalysed protein folding.

Concepts in protein folding.

Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression.

Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.

The Hsp90 Co-chaperones Sti1, Aha1, and P23 Regulate Adaptive Responses to Antifungal Azoles.

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.

Protein folding in the cell.

Dominant forces in protein folding.

Pathway of protein folding.

Fast protein folding kinetics.

Hsp90 chaperones protein folding in vitro.

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