Dr. Richard Pratt Cunningham DDS
Prosthodontist | Prosthodontics
55 Caren Avenue Suite 270 Columbus OH, 43085About
Dr. Richard Cunningham is a prosthodontist practicing in Columbus, OH. Dr. Cunningham specializes in the restoration and replacement of teeth. Prosthodontists maintain oral function, comfort and the appearance and health either with the natural teeth or the replacement of missing ones with maxillofacial tissues and artificial substances.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases.
- Targeted deletion of mNth1 reveals a novel DNA repair enzyme activity.
- Kinetics and binding of the thymine-DNA mismatch glycosylase, Mig-Mth, with mismatch-containing DNA substrates.
- Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity.
- Repair system for noncanonical purines in Escherichia coli.
- Solution structure of a DNA duplex containing an alpha-anomeric adenosine: insights into substrate recognition by endonuclease IV.
- Repair of thymine glycol by hNth1 and hNeil1 is modulated by base pairing and cis-trans epimerization.
- Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase.
- DNA apurinic-apyrimidinic site binding and excision by endonuclease IV.
- A molecular bar-coded DNA repair resource for pooled toxicogenomic screens.
- Systems based mapping demonstrates that recovery from alkylation damage requires DNA repair, RNA processing, and translation associated networks.
- Quantitative in vitro and in vivo characterization of the human P32T mutant ITPase.
- Cross-species Functionome analysis identifies proteins associated with DNA repair, translation and aerobic respiration as conserved modulators of UV-toxicity.
- DNA sequence context conceals α-anomeric lesions.
- Defects in purine nucleotide metabolism lead to substantial incorporation of xanthine and hypoxanthine into DNA and RNA.
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