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Christopher M Dobson

Showing results (31-40 of 516) with videos related to

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Biological & Pharmaceutical Bulletin|October 2, 2015
Conformational Effects of the A21G Flemish Mutation on the Aggregation of Amyloid β PeptideMaho Yagi-Utsumi, Christopher M Dobson
FEBS Letters|June 24, 2009
Bridging the gap: from protein misfolding to protein misfolding diseasesLeila M Luheshi, Christopher M Dobson
Methods in Molecular Biology (Clifton, N.J.)|August 14, 2012
Nanobodies as structural probes of protein misfolding and fibril formationErwin De Genst, Christopher M Dobson
Protein Science : a Publication of the Protein Society|October 24, 2003
Chemical modification of insulin in amyloid fibrilsMelanie R Nilsson, Christopher M Dobson
Biochemistry|January 15, 2003
In vitro characterization of lactoferrin aggregation and amyloid formationMelanie R Nilsson, Christopher M Dobson
HFSP Journal|May 1, 2009
Characterization of the nucleation barriers for protein aggregation and amyloid formationStefan Auer, Christopher M Dobson, Michele Vendruscolo
Journal of Molecular Biology|July 5, 2005
A toy model for predicting the rate of amyloid formation from unfolded proteinDamien Hall, Nami Hirota, Christopher M Dobson
Journal of Cellular and Molecular Medicine|August 2, 2008
Immunological features of alpha-synuclein in Parkinson's diseaseCintia Roodveldt, John Christodoulou, Christopher M Dobson
Journal of Molecular Biology|February 12, 2008
Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analysesPéter Várnai, Christopher M Dobson, Michele Vendruscolo
Biophysical Journal|September 20, 2005
Amyloid fibril formation can proceed from different conformations of a partially unfolded proteinMartino Calamai, Fabrizio Chiti, Christopher M Dobson
Pageof 52

Showing results (31-40 of 516) with videos related to

Sort By:
Pageof 52
Biological & Pharmaceutical Bulletin|October 2, 2015
Conformational Effects of the A21G Flemish Mutation on the Aggregation of Amyloid β PeptideMaho Yagi-Utsumi, Christopher M Dobson
FEBS Letters|June 24, 2009
Bridging the gap: from protein misfolding to protein misfolding diseasesLeila M Luheshi, Christopher M Dobson
Methods in Molecular Biology (Clifton, N.J.)|August 14, 2012
Nanobodies as structural probes of protein misfolding and fibril formationErwin De Genst, Christopher M Dobson
Protein Science : a Publication of the Protein Society|October 24, 2003
Chemical modification of insulin in amyloid fibrilsMelanie R Nilsson, Christopher M Dobson
Biochemistry|January 15, 2003
In vitro characterization of lactoferrin aggregation and amyloid formationMelanie R Nilsson, Christopher M Dobson
HFSP Journal|May 1, 2009
Characterization of the nucleation barriers for protein aggregation and amyloid formationStefan Auer, Christopher M Dobson, Michele Vendruscolo
Journal of Molecular Biology|July 5, 2005
A toy model for predicting the rate of amyloid formation from unfolded proteinDamien Hall, Nami Hirota, Christopher M Dobson
Journal of Cellular and Molecular Medicine|August 2, 2008
Immunological features of alpha-synuclein in Parkinson's diseaseCintia Roodveldt, John Christodoulou, Christopher M Dobson
Journal of Molecular Biology|February 12, 2008
Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analysesPéter Várnai, Christopher M Dobson, Michele Vendruscolo
Biophysical Journal|September 20, 2005
Amyloid fibril formation can proceed from different conformations of a partially unfolded proteinMartino Calamai, Fabrizio Chiti, Christopher M Dobson
Pageof 52