Rodney A. Bednar, Ph.D. - Publications

Affiliations: 
Pennsylvania Drug Discovery Institute 
 Merck Research Laboratories, West Point, Pennsylvania, Lansdale, PA, United States 
 Stony Brook University, Stony Brook, NY, United States 
Area:
Drug Discovery, Enzymology
Website:
http://www.linkedin.com/in/rodneybednar

17 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
1993 Bednar RA, Jencks WP. Direct proton transfer between hydrocyanic acid and nitrogen and oxygen bases. [Erratum to document cited in CA103(25):214716g] Journal of the American Chemical Society. 115: 4947-4947. DOI: 10.1021/Ja00064A092  0.488
1991 Bednar RA, McCaffrey C, Shan K. Introduction of unnatural amino acids into chalcone isomerase. Bioconjugate Chemistry. 2: 211-6. PMID 1772902  0.423
1990 Bednar RA. Reactivity and pH dependence of thiol conjugation to N-ethylmaleimide: detection of a conformational change in chalcone isomerase. Biochemistry. 29: 3684-90. PMID 2340265  0.344
1990 Bednar RA, Adeniran AJ. Chemical modification of chalcone isomerase by diethyl pyrocarbonate: histidine residues are not essential for catalysis. Archives of Biochemistry and Biophysics. 282: 393-8. PMID 2241159 DOI: 10.1016/0003-9861(90)90134-K  0.397
1989 Bednar RA, Fried WB, Lock YW, Pramanik B. Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site. The Journal of Biological Chemistry. 264: 14272-6. PMID 2760066  0.573
1988 Bednar RA, Hadcock JR. Purification and characterization of chalcone isomerase from soybeans. The Journal of Biological Chemistry. 263: 9582-8. PMID 3384815  0.31
1985 Bednar RA, Jencks WP. Direct proton transfer between hydrocyanic acid and nitrogen and oxygen bases Journal of the American Chemical Society. 107: 7126-7134. DOI: 10.1021/Ja00310A061  0.466
1985 Bednar RA, Jencks WP. Is hydrocyanic acid a normal acid? Proton transfer from hydrocyanic acid to bases and small inhibition of proton exchange by acid Journal of the American Chemical Society. 107: 7117-7126. DOI: 10.1021/Ja00310A060  0.514
1985 Bednar RA, Jencks WP. Intramolecular proton transfer through water in diamine monocations Journal of the American Chemical Society. 107: 7135-7138. DOI: 10.1002/Chin.198612156  0.46
1985 Bednar RA, Jencks WP. Is HCN a normal acid? Proton transfer from HCN to bases and small inhibition of proton exchange by acid Journal of the American Chemical Society. 107: 7117-7126.  0.485
1985 Bednar RA, Jencks WP. Direct proton transfer between HCN and nitrogen and oxygen bases Journal of the American Chemical Society. 107: 7126-7134.  0.435
1982 Bednar RA, Colman RF. Chemical modification A probe of the structure and function of the subunits of DPN-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 257: 11734-9. PMID 7118908  0.533
1982 Bednar RA, Hartman FC, Colman RF. 3,4-Didehydro-2-ketoglutarate: an affinity label for diphosphopyridine nucleotide dependent isocitrate dehydrogenase. Biochemistry. 21: 3690-7. PMID 7115695 DOI: 10.1021/Bi00258A026  0.506
1982 Bednar RA, Hartman FC, Colman RF. 3-Bromo-2-ketoglutarate: a substrate and affinity label for diphosphopyridine nucleotide dependent isocitrate dehydrogenase. Biochemistry. 21: 3681-9. PMID 7115694 DOI: 10.1021/Bi00258A025  0.53
1982 Bednar RA, Colman RF. Synthesis, characterization, and reactions of 2′-, 3′-, and 5′-(2-bromoethyl)-AMP: Potential affinity labels for nucleotide binding sites in enzymes Journal of Protein Chemistry. 1: 203-224. DOI: 10.1007/Bf01025000  0.548
1981 Bacon CR, Bednar RA, Colman RF. The reaction of 4-iodoacetamidosalicylic acid with TPN-dependent isocitrate dehydrogenase from pig heart. The Journal of Biological Chemistry. 256: 6593-9. PMID 7240232  0.478
1981 Saradambal KV, Bednar RA, Colman RF. Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase. The Journal of Biological Chemistry. 256: 11866-72. PMID 6795194  0.48
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