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Skip to Search Results- 3Darestani, Reza Rezaei
- 3Zou, Chunxia
- 2Cairo, Christopher W.Xiong, Zi Jian
- 2Kitova, Elena N.
- 2Klassen, John S.
- 2Leney, Aneika C.
- 2Cholera-toxin binding
- 2GM1 ganglioside
- 2Ionization mass-spectrometry
- 2Ligands
- 2Mammalian sialidases
- 2Membrane-proteins
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Human neuraminidase isoenzymes show variable activities for 9-O-acetyl-sialoside substrates
Download2018-01-16
Hunter, Carmanah D, Khanna, Neha, Richards, Michele R, Darestani, Reza Rezaei, Zou, Chunxia, Klassen, John S, Cairo, Christopher W.
Recognition of terminal sialic acids is central to many cellular processes, and structural modification of sialic acid can disrupt these interactions. A prominent, naturally occuring, modification of sialic acid is 9-O-acetylation (9-O-Ac). Study of this modification through generation and...
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2015
Klassen, John S., Cairo, Christopher W.Xiong, Zi Jian, Li, Jun, Privé, Gilbert G., Leney, Aneika C., Kitova, Elena N., Darestani, Reza Rezaei, Zou, Chunxia, Nikjah, Sanaz
Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein–glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and...
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2015
Klassen, John S., Darestani, Reza Rezaei, Kitova, Elena N., Zou, Chunxia, Li, Jun, Leney, Aneika C., Cairo, Christopher W.Xiong, Zi Jian, Privé, Gilbert G., Nikjah, Sanaz
Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein–glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and...