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Trent C Bjorndahl

Showing results (1-10 of 23) with videos related to

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Journal of Biomolecular NMR|May 27, 2003
Backbone 1H, 15N and 13C assignments for the human rhinovirus 3C protease (serotype 14)Trent C Bjorndahl, Hassan Monzavi, David S Wishart
BMC Bioinformatics|December 2, 2008
MetaboMiner--semi-automated identification of metabolites from 2D NMR spectra of complex biofluidsJianguo Xia, Trent C Bjorndahl, Peter Tang, et al.
Biochemistry|October 20, 2007
NMR solution structures of the apo and peptide-inhibited human rhinovirus 3C protease (Serotype 14): structural and dynamic comparisonTrent C Bjorndahl, Lena C Andrew, Valentyna Semenchenko, et al.
Journal of the American Chemical Society|February 14, 2002
Probing the structural determinants of type II' beta-turn formation in peptides and proteinsAlan C Gibbs, Trent C Bjorndahl, Robert S Hodges, et al.
Journal of Molecular Modeling|October 16, 2013
Molecular docking of thiamine reveals similarity in binding properties between the prion protein and other thiamine-binding proteinsNataraj S Pagadala, Trent C Bjorndahl, Nikolay Blinov, et al.
Bioorganic & Medicinal Chemistry|September 28, 2017
The compound (3-{5-[(2,5-dimethoxyphenyl)amino]-1,3,4-thiadiazolidin-2-yl}-5,8-methoxy-2H-chromen-2-one) inhibits the prion protein conversion from PrP<sup>C</sup> to PrP<sup>Sc</sup> with lower IC<sub>50</sub> in ScN2a cellsNataraj S Pagadala, Trent C Bjorndahl, Michael Joyce, et al.
Biochimica Et Biophysica Acta. Proteins and Proteomics|June 25, 2018
Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregationJohn Paul Glaves, Carol L Ladner-Keay, Trent C Bjorndahl, et al.
Biochimica Et Biophysica Acta. Proteins and Proteomics|August 5, 2018
Erratum to Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregation, BBAPAP (2018) 982-988John Paul Glaves, Carol L Ladner-Keay, Trent C Bjorndahl, et al.
Prion|May 14, 2014
Lipopolysaccharide induced conversion of recombinant prion proteinFozia Saleem, Trent C Bjorndahl, Carol L Ladner, et al.
Prion|September 19, 2018
A simple in vitro assay for assessing the efficacy, mechanisms and kinetics of anti-prion fibril compoundsCarol L Ladner-Keay, Li Ross, Rolando Perez-Pineiro, et al.
Pageof 3

Showing results (1-10 of 23) with videos related to

Sort By:
Pageof 3
Journal of Biomolecular NMR|May 27, 2003
Backbone 1H, 15N and 13C assignments for the human rhinovirus 3C protease (serotype 14)Trent C Bjorndahl, Hassan Monzavi, David S Wishart
BMC Bioinformatics|December 2, 2008
MetaboMiner--semi-automated identification of metabolites from 2D NMR spectra of complex biofluidsJianguo Xia, Trent C Bjorndahl, Peter Tang, et al.
Biochemistry|October 20, 2007
NMR solution structures of the apo and peptide-inhibited human rhinovirus 3C protease (Serotype 14): structural and dynamic comparisonTrent C Bjorndahl, Lena C Andrew, Valentyna Semenchenko, et al.
Journal of the American Chemical Society|February 14, 2002
Probing the structural determinants of type II' beta-turn formation in peptides and proteinsAlan C Gibbs, Trent C Bjorndahl, Robert S Hodges, et al.
Journal of Molecular Modeling|October 16, 2013
Molecular docking of thiamine reveals similarity in binding properties between the prion protein and other thiamine-binding proteinsNataraj S Pagadala, Trent C Bjorndahl, Nikolay Blinov, et al.
Bioorganic & Medicinal Chemistry|September 28, 2017
The compound (3-{5-[(2,5-dimethoxyphenyl)amino]-1,3,4-thiadiazolidin-2-yl}-5,8-methoxy-2H-chromen-2-one) inhibits the prion protein conversion from PrP<sup>C</sup> to PrP<sup>Sc</sup> with lower IC<sub>50</sub> in ScN2a cellsNataraj S Pagadala, Trent C Bjorndahl, Michael Joyce, et al.
Biochimica Et Biophysica Acta. Proteins and Proteomics|June 25, 2018
Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregationJohn Paul Glaves, Carol L Ladner-Keay, Trent C Bjorndahl, et al.
Biochimica Et Biophysica Acta. Proteins and Proteomics|August 5, 2018
Erratum to Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregation, BBAPAP (2018) 982-988John Paul Glaves, Carol L Ladner-Keay, Trent C Bjorndahl, et al.
Prion|May 14, 2014
Lipopolysaccharide induced conversion of recombinant prion proteinFozia Saleem, Trent C Bjorndahl, Carol L Ladner, et al.
Prion|September 19, 2018
A simple in vitro assay for assessing the efficacy, mechanisms and kinetics of anti-prion fibril compoundsCarol L Ladner-Keay, Li Ross, Rolando Perez-Pineiro, et al.
Pageof 3