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Cecilia Blikstad, PhD
Postdoctoral Researcher UC Berkeley, Department of Plant and Microbial Biology Kerfeld Lab West PhD, Biochemistry, Uppsala University, Sweden, 2013 MSc, Chemistry, Uppsala University, Sweden, 2008 Lawrence Berkeley National Laboratory Building 64/Room 243 1 Cyclotron Road, Berkeley, California 94720 Phone 510-486-6846 cblikstad@lbl.gov |
Publications:
- Blikstad C and Ivarsson I (2015) High-throughput methods for identification of protein-protein interactions involving short linear motifs, Cell Communication and Signaling, 13, 38
- Blikstad C, Dahlström K, Salminen T and Widersten M (2014) Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution, FEBS Journal, 281, 2387-2398
- Hamnevik E, Blikstad C, Norrehed S and Widersten M (2014) Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A, Journal of Molecular Catalysis B, 99, 68-78
- Blikstad C, Dahlström K, Salminen T and Widersten M (2013) Stereoselective oxidation of aryl-substituted vicinal diols into chiral α-hydroxy aldehydes by re-engineered propanediol oxidoreductase, ACS Catalysis, 3, 3016-3025
- Valegård K, Iqbal A, Kershaw N, Ivison D, Genereux C, Dubus A, Blikstad C, Demetriades M, Hopkinson J, Lloyd A, Roper D, McDonough M, Andersson I and Schofield C (2013) Structural and mechanistic studies on the orf12 gene product from the clavulanic acid biosynthesis pathway, Acta Crystallographica Section D, 69, 1567–1579
- Lopes Pinto F, Erasmie S, Blikstad C, Lindblad P and Oliveira P (2011) FtsZ degradation in the cyanobacterium Anabaena sp. strain PCC 7120, Journal of Plant Physiology, 168, 1934-1942
- Blikstad C and Widersten M (2010) Functional characterization of a stereospecific diol dehydrogenase, FucO, from Escherichia coli: substrate specificity, pH dependence, kinetic isotope effects and influence of solvent viscosity, Journal of Molecular Catalysis B, 66, 148-155
- Blikstad C, Shokeer A, Kurtovic S and Mannervik B (2008) Emergence of a novel highly specific and catalytically efficient enzyme from a naturally promiscuous glutathione transferase, Biochimica et Biophysica Acta, 1780, 1458-1463
