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Keith R Willison

Showing results (1-10 of 52) with videos related to

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Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|May 9, 2018
The substrate specificity of eukaryotic cytosolic chaperonin CCTKeith R Willison
Structure (London, England : 1993)|June 8, 2011
Structural changes underlying allostery in group II chaperoninsKeith R Willison
Current Opinion in Structural Biology|October 27, 2005
Allosteric regulation of chaperoninsAmnon Horovitz, Keith R Willison
Journal of the Royal Society, Interface|August 19, 2008
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actinGabriel M Altschuler, Keith R Willison
Current Opinion in Biotechnology|July 2, 2013
Quantitative single cell and single molecule proteomics for clinical studiesKeith R Willison, David R Klug
Experimental Cell Research|June 13, 2006
Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cellsJulie Grantham, Karen I Brackley, Keith R Willison
Proteins|February 16, 2011
On the evolutionary origin of the chaperoninsCarien Dekker, Keith R Willison, William R Taylor
Journal of Molecular Biology|June 10, 2006
Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunitGünter Pappenberger, Elizabeth A McCormack, Keith R Willison
The Journal of Biological Chemistry|November 9, 2010
A two-step mechanism for the folding of actin by the yeast cytosolic chaperoninSarah F Stuart, Robin J Leatherbarrow, Keith R Willison
Journal of Molecular Biology|September 21, 2005
Unfolding energetics of G-alpha-actin: a discrete intermediate can be re-folded to the native state by CCTGabriel M Altschuler, David R Klug, Keith R Willison
Pageof 6

Showing results (1-10 of 52) with videos related to

Sort By:
Pageof 6
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|May 9, 2018
The substrate specificity of eukaryotic cytosolic chaperonin CCTKeith R Willison
Structure (London, England : 1993)|June 8, 2011
Structural changes underlying allostery in group II chaperoninsKeith R Willison
Current Opinion in Structural Biology|October 27, 2005
Allosteric regulation of chaperoninsAmnon Horovitz, Keith R Willison
Journal of the Royal Society, Interface|August 19, 2008
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actinGabriel M Altschuler, Keith R Willison
Current Opinion in Biotechnology|July 2, 2013
Quantitative single cell and single molecule proteomics for clinical studiesKeith R Willison, David R Klug
Experimental Cell Research|June 13, 2006
Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cellsJulie Grantham, Karen I Brackley, Keith R Willison
Proteins|February 16, 2011
On the evolutionary origin of the chaperoninsCarien Dekker, Keith R Willison, William R Taylor
Journal of Molecular Biology|June 10, 2006
Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunitGünter Pappenberger, Elizabeth A McCormack, Keith R Willison
The Journal of Biological Chemistry|November 9, 2010
A two-step mechanism for the folding of actin by the yeast cytosolic chaperoninSarah F Stuart, Robin J Leatherbarrow, Keith R Willison
Journal of Molecular Biology|September 21, 2005
Unfolding energetics of G-alpha-actin: a discrete intermediate can be re-folded to the native state by CCTGabriel M Altschuler, David R Klug, Keith R Willison
Pageof 6