Xavier Lee
Affiliations: | Cellular and Molecular Medicine | Cleveland Clinic Lerner Research Institute |
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Gogonea V, Gerstenecker GS, Wu Z, et al. (2013) The low-resolution structure of nHDL reconstituted with DMPC with and without cholesterol reveals a mechanism for particle expansion. Journal of Lipid Research. 54: 966-83 |
Granzin J, Huang Y, Topbas C, et al. (2012) Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain. Acta Crystallographica. Section D, Biological Crystallography. 68: 686-94 |
Wu Z, Gogonea V, Lee X, et al. (2011) The low resolution structure of ApoA1 in spherical high density lipoprotein revealed by small angle neutron scattering. The Journal of Biological Chemistry. 286: 12495-508 |
Huang J, Xu Z, Wang D, et al. (2010) Characterization of the secondary binding sites of Maclura pomifera agglutinin by glycan array and crystallographic analyses. Glycobiology. 20: 1643-53 |
Gogonea V, Wu Z, Lee X, et al. (2010) Congruency between biophysical data from multiple platforms and molecular dynamics simulation of the double-super helix model of nascent high-density lipoprotein. Biochemistry. 49: 7323-43 |
Wu Z, Gogonea V, Lee X, et al. (2009) Double superhelix model of high density lipoprotein. The Journal of Biological Chemistry. 284: 36605-19 |
Gabel F, Wang D, Madern D, et al. (2006) Dynamic flexibility of double-stranded RNA activated PKR in solution. Journal of Molecular Biology. 359: 610-23 |
Huang W, Haas TA, Biesterfeldt J, et al. (1999) Purification and crystallization of a novel membrane-anchored protein: the Schistosoma haematobium serpin. Acta Crystallographica. Section D, Biological Crystallography. 55: 350-2 |
Lee X, Thompson A, Zhang Z, et al. (1998) Structure of the complex of Maclura pomifera agglutinin and the T- antigen disaccharide, Galβ1,3GalNAc Journal of Biological Chemistry. 273: 6312-6318 |
Lee X, Dahms T, Ton-That H, et al. (1997) Primary sequence and refined tertiary structure of Pseudomonas fluorescens holo azurin at 2.05 A. Acta Crystallographica. Section D, Biological Crystallography. 53: 493-506 |