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P Bottomley

Showing results (1-10 of 142) with videos related to

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Proceedings of the American Thoracic Society|October 30, 2010
The folding pathway of alpha1-antitrypsin: avoiding the unavoidableStephen P Bottomley
Journal of Molecular Biology|November 9, 2001
Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded stateD J Tew, S P Bottomley
Frontiers in Bioscience : a Journal and Virtual Library|December 3, 2004
A protein family under 'stress' - serpin stability, folding and misfoldingGlyn L Devlin, Stephen P Bottomley
Biochemical and Biophysical Research Communications|January 13, 1998
The effects of reactive centre loop length upon serpin polymerisationS P Bottomley, W S Chang
European Biophysics Journal : EBJ|September 25, 2003
How do proteins avoid becoming too stable? Biophysical studies into metastable proteinsLisa D Cabrita, Stephen P Bottomley
Protein Engineering|February 4, 1999
Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop lengthS P Bottomley, S R Stone
IUBMB Life|June 10, 2004
The role of protein misfolding in the pathogenesis of human diseasesAndrew M Ellisdon, Stephen P Bottomley
Current Medicinal Chemistry|July 16, 2010
Towards the treatment of polyglutamine diseases: the modulatory role of protein contextA L Robertson, S P Bottomley
Methods in Molecular Biology (Clifton, N.J.)|May 31, 2013
A method for the incremental expansion of polyglutamine repeats in recombinant proteinsAmy L Robertson, Stephen P Bottomley
Journal of Molecular Biology|September 28, 2011
Structural change in β-sheet A of Z α(1)-antitrypsin is responsible for accelerated polymerization and diseaseAnja S Knaupp, Stephen P Bottomley
Pageof 15

Showing results (1-10 of 142) with videos related to

Sort By:
Pageof 15
Proceedings of the American Thoracic Society|October 30, 2010
The folding pathway of alpha1-antitrypsin: avoiding the unavoidableStephen P Bottomley
Journal of Molecular Biology|November 9, 2001
Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded stateD J Tew, S P Bottomley
Frontiers in Bioscience : a Journal and Virtual Library|December 3, 2004
A protein family under 'stress' - serpin stability, folding and misfoldingGlyn L Devlin, Stephen P Bottomley
Biochemical and Biophysical Research Communications|January 13, 1998
The effects of reactive centre loop length upon serpin polymerisationS P Bottomley, W S Chang
European Biophysics Journal : EBJ|September 25, 2003
How do proteins avoid becoming too stable? Biophysical studies into metastable proteinsLisa D Cabrita, Stephen P Bottomley
Protein Engineering|February 4, 1999
Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop lengthS P Bottomley, S R Stone
IUBMB Life|June 10, 2004
The role of protein misfolding in the pathogenesis of human diseasesAndrew M Ellisdon, Stephen P Bottomley
Current Medicinal Chemistry|July 16, 2010
Towards the treatment of polyglutamine diseases: the modulatory role of protein contextA L Robertson, S P Bottomley
Methods in Molecular Biology (Clifton, N.J.)|May 31, 2013
A method for the incremental expansion of polyglutamine repeats in recombinant proteinsAmy L Robertson, Stephen P Bottomley
Journal of Molecular Biology|September 28, 2011
Structural change in β-sheet A of Z α(1)-antitrypsin is responsible for accelerated polymerization and diseaseAnja S Knaupp, Stephen P Bottomley
Pageof 15