R. Qian

Two Naturally Occurring α2,6-Sialyltransferase Forms with a Single Amino Acid Change in the Catalytic Domain Differ in Their Catalytic Activity and Proteolytic Processing*

K. Colley, J. Ma, R. Qian, 1997, The Journal of Biological Chemistry.

Sialyltransferase Isoforms Are Phosphorylated in the Cis-medial Golgi on Serine and Threonine Residues in Their Luminal Sequences*

K. Colley, J. Ma, R. Qian, 1999, The Journal of Biological Chemistry.

Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing.

C. Chen, K. Colley, R. Qian, 2001, The Journal of biological chemistry.

Two soluble glycosyltransferases glycosylate less efficiently in vivo than their membrane bound counterparts.

K. Colley, D. Darling, R. Qian, 1998, Glycobiology.

Identification of IgE and IgG1 specific antigens in Echinococcus granulosus cyst fluid

R. Qian, J. Ye, S. Wang, 2017, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas.