Norbert O. Reich
Affiliations: | Chemistry | University of California, Santa Barbara, Santa Barbara, CA, United States |
Area:
Materials Chemistry, Biochemistry & Biophysics, Biomedical Sciences, Biology-Inspired Chemistry & Physics, Deivces, Assembly & Nanochemistry, Structural Chemistry, Spectroscopy & Advanced AnalysisWebsite:
http://www.chem.ucsb.edu/reichgroup/norbert-reichGoogle:
"Norbert Reich"Mean distance: 8.34 | S | N | B | C | P |
Parents
Sign in to add mentorPaul R. Ortiz de Montellano | grad student | 1984 | UCSF | |
(Isozyme specific mechanism-based inactivators of cytochrome P-450 : fatty acid w- and w-1-hydroxylases) |
Children
Sign in to add traineeKevin M. Cheung | research assistant | 2012-2014 | UC Santa Barbara |
William M. Lindstrom | grad student | 2000 | UC Santa Barbara |
Amy M. Martin | grad student | 2001 | UC Santa Barbara |
R. A. Estabrook | grad student | 2007 | UC Santa Barbara |
Stacey N. Peterson | grad student | 2007 | UC Santa Barbara |
Fa-Kuen Shieh | grad student | 2007 | UC Santa Barbara |
Benjamin A. Youngblood | grad student | 2007 | UC Santa Barbara |
Alexey Y. Koyfman | grad student | 2008 | UC Santa Barbara |
Stephanie R. Coffin | grad student | 2009 | UC Santa Barbara |
Gary B. Braun | grad student | 2010 | UC Santa Barbara |
Andrew J. Bonham | grad student | 2004-2010 | UC Santa Barbara |
Douglas M. Matje | grad student | 2011 | UC Santa Barbara |
Celeste T. Holz-Schietinger | grad student | 2012 | UC Santa Barbara |
Adam J. Pollak | grad student | 2014 | UC Santa Barbara |
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Publications
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Konttinen O, Carmody J, Kurnik M, et al. (2023) High fidelity DNA strand-separation is the major specificity determinant in DNA methyltransferase CcrM's catalytic mechanism. Nucleic Acids Research |
Stillson NJ, Anderson KE, Reich NO. (2022) In silico study of selective inhibition mechanism of S-adenosyl-L-methionine analogs for human DNA methyltransferase 3A. Computational Biology and Chemistry. 102: 107796 |
Huang S, Stillson NJ, Sandoval JE, et al. (2021) A Novel Class of Selective Non-Nucleoside Inhibitors of Human DNA Methyltransferase 3A. Bioorganic & Medicinal Chemistry Letters. 127908 |
Sandoval JE, Reich NO. (2020) p53 and TDG are dominant in regulating the activity of the human de novo DNA methyltransferase DNMT3A on nucleosomes. The Journal of Biological Chemistry |
Konttinen O, Carmody J, Pathuri S, et al. (2020) Cell cycle regulated DNA methyltransferase: fluorescent tracking of a DNA strand-separation mechanism and identification of the responsible protein motif. Nucleic Acids Research |
Konttinen OR, Reich NO, Carmody J, et al. (2020) Investigation of the DNA strand separation step by DNA methyltransferase Caulobacter Crescentus The Faseb Journal. 34: 1-1 |
Sandoval JE, Reich NO. (2019) The R882H substitution in the human de novo DNA methyltransferase DNMT3A disrupts allosteric regulation by the tumor supressor p53. The Journal of Biological Chemistry |
Horton JR, Woodcock CB, Opot SB, et al. (2019) The cell cycle-regulated DNA adenine methyltransferase CcrM opens a bubble at its DNA recognition site. Nature Communications. 10: 4600 |
Barel I, Reich NO, Brown FLH. (2019) Integrated rate laws for processive and distributive enzymatic turnover. The Journal of Chemical Physics. 150: 244120 |
Sandoval JE, Huang YH, Muise A, et al. (2019) Mutations in the DNMT3A DNA methyltransferase in AML patients cause both loss and gain of function and differential regulation by protein partners. The Journal of Biological Chemistry |