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2016
Richards, Michele R., Campuzano, Iain D. G., Kitova, Elena N., Klassen, John S., Li, Jun, Privé, Gilbert G., Xiong, Zi Jian, Bagal, Dhanashri
Saposin A (SapA) lipoprotein discs, also known as picodiscs (PDs), represent an attractive method to solubilize glycolipids for protein interaction studies in aqueous solution. Recent electrospray ionization mass spectrometry (ESI-MS) data suggest that the size and composition of...
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2016
Klassen, John S., Campuzano, Iain D. G., Bagal, Dhanashri, Privé, Gilbert G., Kitova, Elena N., Xiong, Zi Jian, Richards, Michele R., Li, Jun
Saposin A (SapA) lipoprotein discs, also known as picodiscs (PDs), represent an attractive method to solubilize glycolipids for protein interaction studies in aqueous solution. Recent electrospray ionization mass spectrometry (ESI-MS) data suggest that the size and composition of...
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Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
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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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Structural basis for antibody recognition in the receptor-binding domains of toxins A and B from Clostridium difficile
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Ng, Kenneth K. S., Tanha, Jamshid, Kitova, Elena N., Eugenio, Luiz, Murase, Tomohiko, Klassen, John S., Hussack, Greg, Schorr, Melissa
Clostridium difficile infection is a serious and highly prevalent nosocomial disease in which the two large, Rho-glucosylating toxins TcdA and TcdB are the main virulence factors. We report for the first time crystal structures revealing how neutralizing and non-neutralizing single-domain...