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Daniel Herschlag grad student 2008 Stanford
 (Structural and functional comparisons in the alkaline phosphatase superfamily : implications for mechanism and evolution)
Wendell A. Lim post-doc 2008-2014 UCSF
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Zalatan JG, Lee ME, Almeida R, et al. (2015) Engineering complex synthetic transcriptional programs with CRISPR RNA scaffolds. Cell. 160: 339-50
Andrews LD, Zalatan JG, Herschlag D. (2014) Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: comparative analysis of alkaline phosphatase and protein tyrosine phosphatases. Biochemistry. 53: 6811-9
Zalatan JG, Coyle SM, Rajan S, et al. (2012) Conformational control of the Ste5 scaffold protein insulates against MAP kinase misactivation. Science (New York, N.Y.). 337: 1218-22
Good MC, Zalatan JG, Lim WA. (2011) Scaffold proteins: hubs for controlling the flow of cellular information. Science (New York, N.Y.). 332: 680-6
Lassila JK, Zalatan JG, Herschlag D. (2011) Biological phosphoryl-transfer reactions: understanding mechanism and catalysis. Annual Review of Biochemistry. 80: 669-702
Zalatan JG, Herschlag D. (2009) The far reaches of enzymology. Nature Chemical Biology. 5: 516-20
Zalatan JG, Fenn TD, Herschlag D. (2008) Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion. Journal of Molecular Biology. 384: 1174-89
O'Brien PJ, Lassila JK, Fenn TD, et al. (2008) Arginine coordination in enzymatic phosphoryl transfer: evaluation of the effect of Arg166 mutations in Escherichia coli alkaline phosphatase. Biochemistry. 47: 7663-72
Zalatan JG, Catrina I, Mitchell R, et al. (2007) Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis. Journal of the American Chemical Society. 129: 9789-98
Catrina I, O'Brien PJ, Purcell J, et al. (2007) Probing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction. Journal of the American Chemical Society. 129: 5760-5
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