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2016

Klassen, John S., Han, Ling, Kitova, Elena N.

This study reports on the use of the catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) assay, combined with glycomicelles, as a method for detecting specific interactions between water-soluble proteins and glycolipids (GLs) in aqueous solution. The B subunit homopentamers...

2016

Han, Ling, Klassen, John S., Kitova, Elena N.

This study reports on the use of the catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) assay, combined with glycomicelles, as a method for detecting specific interactions between water-soluble proteins and glycolipids (GLs) in aqueous solution. The B subunit homopentamers...

2012

Klassen, John S., Lin, Hong, Kitova, Elena N., Ng, Kenneth K., Johnson, M. A., Eugenio, Luiz

Electrospray ionization mass spectrometry (ESI-MS) measurements were performed under a variety of solution conditions on a highly acidic sub-fragment (B3C) of the C-terminal carbohydrate-binding repeat region of Clostridium difficile toxin B, and two mutants (B4A and B4B) containing fewer acidic...

2012

Klassen, John S., Lin, Hong, Kitova, Elena N., Ng, Kenneth K., Johnson, M. A., Eugenio, Luiz

Electrospray ionization mass spectrometry (ESI-MS) measurements were performed under a variety of solution conditions on a highly acidic sub-fragment (B3C) of the C-terminal carbohydrate-binding repeat region of Clostridium difficile toxin B, and two mutants (B4A and B4B) containing fewer acidic...

2010

Soya, Naoto, Klassen, John S., Kitova, Elena N., Sun, Nian

An investigation of the nonspecific association of small charged biomolecules and proteins in electrospray ionization mass spectrometry (ES-MS) is described. Aqueous solutions containing pairs of proteins and a small acidic or basic biomolecule that does not interact specifically with either of...

2010

Kitova, Elena N., Sun, Nian, Klassen, John S., Soya, Naoto

An investigation of the nonspecific association of small charged biomolecules and proteins in electrospray ionization mass spectrometry (ES-MS) is described. Aqueous solutions containing pairs of proteins and a small acidic or basic biomolecule that does not interact specifically with either of...

2016

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...

2016

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...

2016

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...

2016

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...