Year |
Citation |
Score |
2020 |
Hiller DA, Dunican BF, Nallur S, Li NS, Piccirilli JA, Strobel SA. The positively charged active site of the bacterial toxin RelE causes a large shift in the general base pKa. Biochemistry. PMID 32320214 DOI: 10.1021/Acs.Biochem.9B01047 |
0.397 |
|
2018 |
Torgerson CD, Hiller DA, Stav S, Strobel SA. Gene regulation by a glycine riboswitch singlet uses a finely tuned energetic landscape for helical switching. Rna (New York, N.Y.). PMID 30237163 DOI: 10.1261/Rna.067884.118 |
0.347 |
|
2017 |
Hutchings ML, Alpha-Cobb CJ, Hiller DA, Berro J, Strobel SA. Mycofumigation Through Production of the Volatile DNA Methylating Agent N-methyl-N-nitrosoisobutyramide by Fungi in the Genus Muscodor. The Journal of Biological Chemistry. PMID 28283571 DOI: 10.1074/Jbc.M117.779009 |
0.357 |
|
2015 |
Dunican BF, Hiller DA, Strobel SA. Transition State Charge Stabilization and Acid-Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE. Biochemistry. PMID 26535789 DOI: 10.1021/Acs.Biochem.5B00866 |
0.383 |
|
2011 |
Carrasco N, Hiller DA, Strobel SA. Minimal transition state charge stabilization of the oxyanion during peptide bond formation by the ribosome. Biochemistry. 50: 10491-8. PMID 22035282 DOI: 10.1021/Bi201290S |
0.337 |
|
2011 |
Hiller DA, Strobel SA. The chemical versatility of RNA. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 366: 2929-35. PMID 21930584 DOI: 10.1098/Rstb.2011.0143 |
0.319 |
|
2011 |
Hiller DA, Singh V, Zhong M, Strobel SA. A two-step chemical mechanism for ribosome-catalysed peptide bond formation. Nature. 476: 236-9. PMID 21765427 DOI: 10.1038/Nature10248 |
0.365 |
|
2011 |
Hancock SP, Hiller DA, Perona JJ, Jen-Jacobson L. The energetic contribution of induced electrostatic asymmetry to DNA bending by a site-specific protein. Journal of Molecular Biology. 406: 285-312. PMID 21167173 DOI: 10.1016/J.Jmb.2010.12.012 |
0.624 |
|
2010 |
Hiller DA, Zhong M, Singh V, Strobel SA. Transition states of uncatalyzed hydrolysis and aminolysis reactions of a ribosomal P-site substrate determined by kinetic isotope effects. Biochemistry. 49: 3868-78. PMID 20359191 DOI: 10.1021/Bi901458X |
0.308 |
|
2006 |
Hiller DA, Perona JJ. Positively charged C-terminal subdomains of EcoRV endonuclease: contributions to DNA binding, bending, and cleavage. Biochemistry. 45: 11453-63. PMID 16981705 DOI: 10.1021/Bi0606400 |
0.644 |
|
2005 |
Hiller DA, Rodriguez AM, Perona JJ. Non-cognate enzyme-DNA complex: structural and kinetic analysis of EcoRV endonuclease bound to the EcoRI recognition site GAATTC. Journal of Molecular Biology. 354: 121-36. PMID 16236314 DOI: 10.1016/J.Jmb.2005.09.046 |
0.636 |
|
2003 |
Hiller DA, Fogg JM, Martin AM, Beechem JM, Reich NO, Perona JJ. Simultaneous DNA binding and bending by EcoRV endonuclease observed by real-time fluorescence. Biochemistry. 42: 14375-85. PMID 14661948 DOI: 10.1021/Bi035520W |
0.614 |
|
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