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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 Analysis
Website:
http://www.chem.ucsb.edu/reichgroup/norbert-reich
Google:
"Norbert Reich"
Mean distance: 8.34
 
SNBCP

Parents

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Paul R. Ortiz de Montellano grad student 1984 UCSF
 (Isozyme specific mechanism-based inactivators of cytochrome P-450 : fatty acid w- and w-1-hydroxylases)
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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
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