Tiit Lukk, Ph.D.
Affiliations: | 2009 | University of Illinois, Urbana-Champaign, Urbana-Champaign, IL |
Area:
structure/function relationships for enzyme-catalyzed reactionsGoogle:
"Tiit Lukk"Mean distance: 8.78 | S | N | B | C | P |
Parents
Sign in to add mentorJohn A. Gerlt | grad student | 2009 | UIUC | |
(Discovery of function in the enolase superfamily.) | ||||
Satish K. Nair | post-doc | Tallinn University of Technology |
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Publications
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Fujinami D, Garcia de Gonzalo CV, Biswas S, et al. (2021) Structural and mechanistic investigations of protein S-glycosyltransferases. Cell Chemical Biology |
Ernits K, Eek P, Lukk T, et al. (2019) Author Correction: First crystal structure of an endo-levanase - the BT1760 from a human gut commensal Bacteroides thetaiotaomicron. Scientific Reports. 9: 17512 |
Ernits K, Eek P, Lukk T, et al. (2019) First crystal structure of an endo-levanase - the BT1760 from a human gut commensal Bacteroides thetaiotaomicron. Scientific Reports. 9: 8443 |
Schuller DJ, Huang Q, Lukk T. (2018) Crystallographic exploration of flexibility in an allosteric enzyme Acta Crystallographica Section A. 74 |
Dong SH, Tang W, Lukk T, et al. (2015) The enterrococcal cytolysin synthetase has an unanticipated lipid kinase fold. Elife. 4 |
Garg A, Lukk T, Kumar V, et al. (2015) Structure, function and inhibition of the phosphoethanolamine methyltransferases of the human malaria parasites Plasmodium vivax and Plasmodium knowlesi. Scientific Reports. 5: 9064 |
Organtini LJ, Allison AB, Lukk T, et al. (2015) Global displacement of canine parvovirus by a host-adapted variant: structural comparison between pandemic viruses with distinct host ranges. Journal of Virology. 89: 1909-12 |
Dong S, Tang W, Lukk T, et al. (2015) Author response: The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold Elife |
Majumdar S, Lukk T, Solbiati JO, et al. (2014) Roles of small laccases from Streptomyces in lignin degradation. Biochemistry. 53: 4047-58 |
Wichelecki DJ, Balthazor BM, Chau AC, et al. (2014) Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the d-mannonate dehydratase subgroup Biochemistry. 53: 2722-2731 |