Christopher J. Wilds, Ph.D.
Affiliations: | 2000 | McGill University, Montreal, QC, Canada |
Area:
Organic ChemistryGoogle:
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Parents
Sign in to add mentorMasad J. Damha | grad student | 2000 | McGill | |
(Synthesis, physicochemical and biological properties of oligonucleotides containing 2-fluoro-2-deoxy-beta-D-arabinose.) |
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Publications
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Pontarelli A, Wilds CJ. (2023) C5-Propynyl modified 2'-fluoroarabinonucleic acids form stable duplexes with RNA that are RNase H competent. Organic & Biomolecular Chemistry. 21: 7437-7446 |
Pontarelli A, Wilds CJ. (2023) Oligonucleotides Containing C5-Propynyl Modified Arabinonucleic Acids: Synthesis, Biophysical and Antisense Properties. Chembiochem : a European Journal of Chemical Biology. e202300068 |
Kozlov G, Mattijssen S, Jiang J, et al. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Research |
Pontarelli A, Liu JT, Movasat H, et al. (2022) Synthesis of a Convertible Linker Containing a Disulfide Group for Oligonucleotide Functionalization. Organic Letters |
Pontarelli A, Wilds CJ. (2022) Arabinonucleic acids containing C5-propynyl modifications form stable hybrid duplexes with RNA that are efficiently degraded by E. coli RNase H. Bioorganic & Medicinal Chemistry Letters. 67: 128744 |
Copp W, Wilds CJ. (2020) O -Alkylguanine DNA Alkyltransferase Mediated Disassembly of a DNA Tetrahedron. Chemistry (Weinheim An Der Bergstrasse, Germany) |
Behmand B, Noronha AM, Wilds CJ, et al. (2020) Hydrated electrons induce the formation of interstrand cross-links in DNA modified by cisplatin adducts. Journal of Radiation Research |
Copp W, Wilds CJ. (2020) Frontispiece: O 6 ‐Alkylguanine DNA Alkyltransferase Mediated Disassembly of a DNA Tetrahedron Chemistry – a European Journal. 26 |
Sacre L, O'Flaherty DK, Archambault P, et al. (2017) O⁴-Alkylated-2'-deoxyuridine repair by O⁶-alkylguanine DNA alkyltransferase is augmented by a C5-fluorine modification. Chembiochem : a European Journal of Chemical Biology |
Schoonhoven NM, O'Flaherty DK, McManus FP, et al. (2017) Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein. Molecules (Basel, Switzerland). 22 |