Alice Vrielink
Affiliations: | McGill University, Montreal, QC, Canada |
Area:
BiochemistryGoogle:
"Alice Vrielink"Mean distance: (not calculated yet)
Children
Sign in to add trainee| Paula I. Lario | grad student | 2003 | McGill |
| Babu Allampura Manjasetty | post-doc | (Physics Tree) |
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Publications
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| Anandan A, Dunstan NW, Ryan TM, et al. (2021) Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme-substrate recognition. Iucrj. 8: 732-746 |
| Samantha A, Damnjanović J, Iwasaki Y, et al. (2021) Structures of an engineered phospholipase D with specificity for secondary alcohol transphosphatidylation: insights into plasticity of substrate binding and activation. The Biochemical Journal. 478: 1749-1767 |
| Samantha A, Vrielink A. (2020) Lipid a Phosphoethanolamine Transferase Regulation, Structure and Immune Response. Journal of Molecular Biology |
| Kerber T, Vrielink A. (2020) The role of hydrogen atoms in redox catalysis by the flavoenzyme cholesterol oxidase. Methods in Enzymology. 634: 361-377 |
| Anandan A, Vrielink A. (2019) Structure and function of lipid A-modifying enzymes. Annals of the New York Academy of Sciences |
| Vrielink A, Holden HM. (2018) Editorial overview: Catalysis and regulation: Structural features guiding enzyme catalysed processes. Current Opinion in Structural Biology. 53: iii-v |
| Kahler CM, Sarkar-Tyson M, Kibble EA, et al. (2018) Enzyme targets for drug design of new anti-virulence therapeutics. Current Opinion in Structural Biology. 53: 140-150 |
| Kahler CM, Nawrocki KL, Anandan A, et al. (2018) Structure-Function Relationships of the Neisserial EptA Enzyme Responsible for Phosphoethanolamine Decoration of Lipid A: Rationale for Drug Targeting. Frontiers in Microbiology. 9: 1922 |
| Yu LJ, Golden E, Chen N, et al. (2017) Computational insights for the hydride transfer and distinctive roles of key residues in cholesterol oxidase. Scientific Reports. 7: 17265 |
| Harb LH, Arooj M, Vrielink A, et al. (2017) Computational site-directed mutagenesis studies of the role of the hydrophobic triad on substrate binding in cholesterol oxidase. Proteins |