David A. Hiller, Ph.D.

Affiliations: 
2005 University of California, Santa Barbara, Santa Barbara, CA, United States 
Area:
Biochemistry
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John J. Perona grad student 2005 UC Santa Barbara
 (Mechanism of DNA bending and its role in the specificity of EcoRV restriction endonuclease.)
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Publications

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Hiller DA, Dunican BF, Nallur S, et al. (2020) The positively charged active site of the bacterial toxin RelE causes a large shift in the general base pKa. Biochemistry
Torgerson CD, Hiller DA, Stav S, et al. (2018) Gene regulation by a glycine riboswitch singlet uses a finely tuned energetic landscape for helical switching. Rna (New York, N.Y.)
Hutchings ML, Alpha-Cobb CJ, Hiller DA, et al. (2017) Mycofumigation Through Production of the Volatile DNA Methylating Agent N-methyl-N-nitrosoisobutyramide by Fungi in the Genus Muscodor. The Journal of Biological Chemistry
Dunican BF, Hiller DA, Strobel SA. (2015) Transition State Charge Stabilization and Acid-Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE. Biochemistry
Carrasco N, Hiller DA, Strobel SA. (2011) Minimal transition state charge stabilization of the oxyanion during peptide bond formation by the ribosome. Biochemistry. 50: 10491-8
Hiller DA, Strobel SA. (2011) The chemical versatility of RNA. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 366: 2929-35
Hiller DA, Singh V, Zhong M, et al. (2011) A two-step chemical mechanism for ribosome-catalysed peptide bond formation. Nature. 476: 236-9
Hancock SP, Hiller DA, Perona JJ, et al. (2011) The energetic contribution of induced electrostatic asymmetry to DNA bending by a site-specific protein. Journal of Molecular Biology. 406: 285-312
Hiller DA, Zhong M, Singh V, et al. (2010) Transition states of uncatalyzed hydrolysis and aminolysis reactions of a ribosomal P-site substrate determined by kinetic isotope effects. Biochemistry. 49: 3868-78
Hiller DA, Perona JJ. (2006) Positively charged C-terminal subdomains of EcoRV endonuclease: contributions to DNA binding, bending, and cleavage. Biochemistry. 45: 11453-63
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