David A. Hiller, Ph.D.
Affiliations: | 2005 | University of California, Santa Barbara, Santa Barbara, CA, United States |
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BiochemistryGoogle:
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Parents
Sign in to add mentorJohn 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 |