Alice Vrielink

Add links
From Wikipedia, the free encyclopedia

Alice Vrielink
Alma materUniversity of London
Scientific career
ThesisThe crystal structure determination of cholesterol oxidase (1989)
Doctoral advisorDavid Mervyn Blow[1]

Alice Vrielink is a structural biologist and Professor of Structural Biology in the School of Molecular Sciences at the University of Western Australia. She is known for her work determining the structures of macromolecules such as enzymes and nucleic acids.

Education[edit]

Vrielink earned a Bachelor of Science in Chemistry and Masters of Science in Physical Chemistry at the University of Calgary in Canada.[2] For her master's research she worked on ligands of angiotensin, a hormone involved in regulating blood pressure.[3] She received a PhD in 1989 from the University of London where she worked on the structure of cholesterol oxidase.[4] She also has a Diploma in Crystallography from the Imperial College of Science and Technology.[2]

Career[edit]

Vrielink was an Assistant and Associate Professor at McGill University in Canada from 1994 to 2001.[2] From 2000 until 2007 she served as a Research Professor at the University of California, Santa Cruz and then joined the faculty at University of Western Australia as Professor of Structural Biology in 2007.[2]

Vrielink was a member of the 2014 National Committee on Crystallography[5] She is a past president of the Society of Crystallographers of Australia and New Zealand (SCANZ).[6]

Research[edit]

Vrielink conducts research in protein biochemistry and crystallography with a special focus on understanding the structural determinants governing enzyme chemistry.[7] Vrielink's early research centered on the three-dimensional structure of the enzyme cholesterol oxidase first in Brevibacterium[8][9] and then in Streptomyces.[10]

She has been involved in projects that have established the structure of compounds including L-amino-acid oxidase,[11] prions,[12] and snake venom.[13] In 2017, she mapped the molecular structure of EptA,[14] a protein that shields superbugs from antibiotics. This work has been covered by the BBC,[15] ABC,[16] Times Higher Education,[17] The West Australian,[18] and Particle.[19] Subsequent work on EptA has revealed why it may be a good target for drug development.[20][21]

Selected publications[edit]

  • Vrielink, A.; Rüger, W.; Driessen, H.P.; Freemont, P.S. (1 August 1994). "Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose". The EMBO Journal. 13 (15): 3413–3422. doi:10.1002/j.1460-2075.1994.tb06646.x. ISSN 0261-4189. PMC 395243. PMID 8062817.
  • Vrielink, Alice; Lloyd, Lesley F; Blow, David M (5 June 1991). "Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution". Journal of Molecular Biology. 219 (3): 533–554. doi:10.1016/0022-2836(91)90192-9. ISSN 0022-2836. PMID 2051487.
  • Pawelek, P. D.; Cheah, J.; Coulombe, R.; Macheroux, P.; Ghisla, S.; Vrielink, A. (15 August 2000). "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site". The EMBO Journal. 19 (16): 4204–4215. doi:10.1093/emboj/19.16.4204. ISSN 0261-4189. PMC 302035. PMID 10944103.
  • Burns, Colin S.; Aronoff-Spencer, Eliah; Dunham, Christine M.; Lario, Paula; Avdievich, Nikolai I.; Antholine, William E.; Olmstead, Marilyn M.; Vrielink, Alice; Gerfen, Gary J.; Peisach, Jack; Scott, William G. (1 March 2002). "Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein". Biochemistry. 41 (12): 3991–4001. doi:10.1021/bi011922x. ISSN 0006-2960. PMC 2905306. PMID 11900542.

References[edit]

  1. ^ Vrielink, Alice (3 July 2014). "David Blow (1931-2004) - A Remberance" (PDF). American Crystallographic Association. Archived (PDF) from the original on 3 July 2014. Retrieved 14 October 2021.
  2. ^ a b c d "Researcher Profile: Professor Alice Vrielink". UWA Research Repository.
  3. ^ Vrielink, Alice (1986). Structural and conformational energy studies of ligands of angiotensin converting enzyme and thermolysin (Thesis). Ottawa: National Library of Canada. OCLC 16710356.
  4. ^ Vrielink, Alice; University of London (1989). The crystal structure determination of cholesterol oxidase. hdl:10044/1/47699. OCLC 1063590654.
  5. ^ "Triennial Congress and General Assembly". Australian Academy of Science newsletter.
  6. ^ Vrielink, Alice (2016). "From the President" (PDF). Scanz Newsletter. Retrieved 7 February 2018.
  7. ^ Ducy, Liam. "UWA celebrates Australian link in scientific breakthrough". WAToday, August 20, 2014.
  8. ^ Li, Jiayao; Vrielink, Alice; Brick, Peter; Blow, David M. (26 January 1993). "Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases". Biochemistry. 32 (43): 11507–11515. doi:10.1021/bi00094a006. ISSN 0006-2960. PMID 8218217.
  9. ^ Vrielink, Alice; Lloyd, Lesley F; Blow, David M (5 June 1991). "Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution". Journal of Molecular Biology. 219 (3): 533–554. doi:10.1016/0022-2836(91)90192-9. ISSN 0022-2836. PMID 2051487.
  10. ^ Yue, Q. Kimberley; Kass, Ignatius J.; Sampson, Nicole S.; Vrielink, Alice (1 April 1999). "Crystal Structure Determination of Cholesterol Oxidase from Streptomyces and Structural Characterization of Key Active Site Mutants". Biochemistry. 38 (14): 4277–4286. doi:10.1021/bi982497j. ISSN 0006-2960. PMID 10194345.
  11. ^ Pawelek, P. D. (15 August 2000). "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site". The EMBO Journal. 19 (16): 4204–4215. doi:10.1093/emboj/19.16.4204. PMC 302035. PMID 10944103.
  12. ^ Burns, Colin S.; Aronoff-Spencer, Eliah; Dunham, Christine M.; Lario, Paula; Avdievich, Nikolai I.; Antholine, William E.; Olmstead, Marilyn M.; Vrielink, Alice; Gerfen, Gary J.; Peisach, Jack; Scott, William G. (1 March 2002). "Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein". Biochemistry. 41 (12): 3991–4001. doi:10.1021/bi011922x. ISSN 0006-2960. PMC 2905306. PMID 11900542.
  13. ^ Kang, Tse Siang; Georgieva, Dessislava; Genov, Nikolay; Murakami, Mário T.; Sinha, Mau; Kumar, Ramasamy P.; Kaur, Punit; Kumar, Sanjit; Dey, Sharmistha; Sharma, Sujata; Vrielink, Alice (2011). "Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis". The FEBS Journal. 278 (23): 4544–4576. doi:10.1111/j.1742-4658.2011.08115.x. ISSN 1742-4658. PMID 21470368. S2CID 40199362.
  14. ^ Anandan, Anandhi; Evans, Genevieve L.; Condic-Jurkic, Karmen; O’Mara, Megan L.; John, Constance M.; Phillips, Nancy J.; Jarvis, Gary A.; Wills, Siobhan S.; Stubbs, Keith A.; Moraes, Isabel; Kahler, Charlene M.; Vrielink, Alice (28 February 2017). "Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding". Proceedings of the National Academy of Sciences. 114 (9): 2218–2223. Bibcode:2017PNAS..114.2218A. doi:10.1073/pnas.1612927114. ISSN 0027-8424. PMC 5338521. PMID 28193899.
  15. ^ Dunlop, Greg (15 February 2017). "Antibiotic resistance: Scientists 'unmask' superbug-shielding protein". BBC News. Retrieved 7 February 2018.
  16. ^ Wildie, Tom (14 February 2017). "Australian scientists make breakthrough in fight against superbugs". ABC News. Retrieved 7 February 2018.
  17. ^ "Stopping the rise of the superbug". Times Higher Education. Archived from the original on 8 February 2018. Retrieved 7 February 2018.
  18. ^ O'Leary, Cathy (14 February 2017). "UWA breakthrough in superbug battle". The West Australian. Retrieved 7 February 2018.
  19. ^ Mitchell, Samille (14 March 2017). "WA Scientists Fight Deadly Superbugs". Particle.
  20. ^ Kahler, Charlene M.; Nawrocki, K. L.; Anandan, A.; Vrielink, Alice; Shafer, William M. (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. doi:10.3389/fmicb.2018.01922. ISSN 1664-302X. PMC 6111236. PMID 30186254.
  21. ^ Anandan, Anandhi; Dunstan, Nicholas W.; Ryan, Timothy M.; Mertens, Haydyn D. T.; Lim, Katherine Y. L.; Evans, Genevieve L.; Kahler, Charlene M.; Vrielink, Alice (1 September 2021). "Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme–substrate recognition". IUCrJ. 8 (5): 732–746. doi:10.1107/S2052252521005613. ISSN 2052-2525. PMC 8420757. PMID 34584735.

External links[edit]

Retrieved from "https://en.wikipedia.org/w/index.php?title=Alice_Vrielink&oldid=1158146572"