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- 15Chemistry, Department of/Journal Articles (Chemistry)
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- 5Biological Sciences, Department of/Journal Articles (Biological Sciences)
- 2Graduate and Postdoctoral Studies (GPS), Faculty of
- 2Graduate and Postdoctoral Studies (GPS), Faculty of/Theses and Dissertations
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Protein-glycolipid interactions studied in vitro using ESI-MS and nanodiscs: Insights into the mechanisms and energetics of binding
Download2015
Han, Ling Han, Kitova, Elena N., Klassen, John S., Pluvinage, Benjamin, Lin, Hong, Nikjah, Sanaz, Li, Jun, Boraston, Alisdair B.
Electrospray ionization-mass spectrometry (ESI-MS) analysis combined with the use of nanodiscs (NDs) to solubilize glycolipids (GLs) has recently emerged as a promising analytical method for detecting protein–GL interactions in vitro and, when applied to libraries of GLs, ranking their...
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Protein-glycolipid interactions studied in vitro using ESI-MS and nanodiscs: Insights into the mechanisms and energetics of binding
Download2015
Nikjah, Sanaz, Boraston, Alisdair B., Lin, Hong, Kitova, Elena N., Li, Jun, Pluvinage, Benjamin, Han, Ling Han, Klassen, John S.
Electrospray ionization-mass spectrometry (ESI-MS) analysis combined with the use of nanodiscs (NDs) to solubilize glycolipids (GLs) has recently emerged as a promising analytical method for detecting protein–GL interactions in vitro and, when applied to libraries of GLs, ranking their...
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Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
Download2010
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Liu, Lan
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...
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Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
Download2010
El-Hawiet, Amr, Liu, Lan, Klassen, John S., Kitova, Elena N.
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...
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Spring 2011
Molecular transition metal catalysts offer unique potential for the production of fine chemicals. Chemical processes carried out in the presence of well defined molecular catalysts often only require mild, easily accessible conditions, fewer sacrificial reagents, and can selectively produce a...
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Screening anti-cancer drugs against tubulin using catch-and-release electrospray ionization mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Winter, Philip, Tuszynski, Jack A., Darestani, Reza R.
Tubulin, which is the building block of microtubules, plays an important role in cell division. This critical role makes tubulin an attractive target for the development of chemotherapeutic drugs to treat cancer. Currently, there is no general binding assay for tubulin–drug interactions. The...
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Screening anti-cancer drugs against tubulin using catch-and-release electrospray ionization mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Winter, Philip, Tuszynski, Jack A., Darestani, Reza R.
Tubulin, which is the building block of microtubules, plays an important role in cell division. This critical role makes tubulin an attractive target for the development of chemotherapeutic drugs to treat cancer. Currently, there is no general binding assay for tubulin–drug interactions. The...
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Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
Download2016
Kitova, Elena N., Klassen, John S., Fan, Xuxin, Privé, Gilbert G., Cairo, Christopher W., Xiong, Zi Jian, Ng, Kenneth K. S., Zou, Chunxia, Eugenio, Luiz, Li, Jun
An electrospray ionization mass spectrometry (ESI-MS) assay for screening carbohydrate libraries against lectins is described. The assay is based on the proxy protein ESI-MS method, which combines direct ESI-MS protein–ligand binding measurements and competitive protein binding, to simultaneously...
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Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
Download2016
Privé, Gilbert G., Ng, Kenneth K. S., Xiong, Zi Jian, Klassen, John S., Kitova, Elena N., Fan, Xuxin, Li, Jun, Zou, Chunxia, Eugenio, Luiz, Cairo, Christopher W.
An electrospray ionization mass spectrometry (ESI-MS) assay for screening carbohydrate libraries against lectins is described. The assay is based on the proxy protein ESI-MS method, which combines direct ESI-MS protein–ligand binding measurements and competitive protein binding, to simultaneously...
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2004
Okon, Mark, Schulman, Brenda A., Macauley, Matthew S., McIntosh, Lawrence P., Mackereth, Cameron D., Schärpf, Manuela, Errington, Wesley J.
Although sumoylation regulates a diverse and growing number of recognized biological processes, the molecular mechanisms by which the covalent attachment of the ubiquitin-like protein SUMO can alter the properties of a target protein remain to be established. To address this question, we have...