R
Richard P. Cunningham
Researcher at University at Albany, SUNY
Publications - 78
Citations - 6293
Richard P. Cunningham is an academic researcher from University at Albany, SUNY. The author has contributed to research in topics: DNA & DNA glycosylase. The author has an hindex of 39, co-authored 78 publications receiving 6082 citations. Previous affiliations of Richard P. Cunningham include University of Vermont & State University of New York System.
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Endonuclease IV (nfo) mutant of Escherichia coli.
TL;DR: A cloned gene, designated nfo, caused overproduction of an EDTA-resistant endonuclease specific for apurinic-apyrimidinic sites in DNA, which resulted in mutants that had an increased sensitivity to the alkylating agents methyl methanesulfonate and mitomycin C and to the oxidants tert-butyl hydroperoxide and bleomycin.
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Structure and function of the multifunctional DNA-repair enzyme exonuclease III.
TL;DR: Residues conserved among AP endonucleases from bacteria to man cluster within this active site and appear to participate in phosphate-bond cleavage at AP sites through a nucleophilic attack facilitated by a single bound metal ion.
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The enzymology of apurinic/apyrimidinic endonucleases
TL;DR: Studies on the enzymology of apurinic/apyrimidinic (AP) endonucleases from procaryotic and eucaryotic organisms are reviewed and emphasis is placed on the enzymes from Escherichia coli from which a considerable portion of knowledge has been derived.
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Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments.
TL;DR: Homologous combinations of single-stranded fragments and superhelical DNA from phages phiX174 and fd reacted, whereas heterologous combination did not; the reaction required high concentrations of protein and MgCl2.
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New substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy- 2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase
TL;DR: Analysis of crude extracts obtained from wild type and endonuclease III deletion mutants of E. coli correlated well with data obtained with the purified enzymes, and uracil DNA N-glycosylase removes 5-OHdU more efficiently than the other two enzymes and has no activity on 5- OHdC even when present in great excess.