2'-deoxyadenosine and 2'-fluoro-2'-deoxyadenosine

2'-deoxyadenosine has been researched along with 2'-fluoro-2'-deoxyadenosine in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's1 (33.33)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
An, SH; Au, A; Garza, G; Land, KM; Shokar, A; Tong, E; Wnuk, SF; Zayas, J1
Chepanoske, CL; David, SS; Fujiwara, T; Porello, SL; Sugiyama, H1
David, SS; Williams, SD1

Other Studies

3 other study(ies) available for 2'-deoxyadenosine and 2'-fluoro-2'-deoxyadenosine

ArticleYear
S-Adenosylhomocysteine hydrolase of the protozoan parasite Trichomonas vaginalis: potent inhibitory activity of 9-(2-deoxy-2-fluoro-β,D-arabinofuranosyl)adenine.
    Bioorganic & medicinal chemistry letters, 2012, Jun-15, Volume: 22, Issue:12

    Topics: Adenosine; Adenosylhomocysteinase; Animals; Antiprotozoal Agents; Cell Culture Techniques; Cell Survival; CHO Cells; Cricetinae; Enzyme Inhibitors; Humans; Inhibitory Concentration 50; Metronidazole; Protozoan Proteins; Structure-Activity Relationship; Trichomonas vaginalis; Uridine

2012
Substrate recognition by Escherichia coli MutY using substrate analogs.
    Nucleic acids research, 1999, Aug-01, Volume: 27, Issue:15

    Topics: Apurinic Acid; Base Pair Mismatch; Base Sequence; Binding Sites; Deoxyadenosines; DNA; DNA Footprinting; DNA Glycosylases; DNA-Binding Proteins; Edetic Acid; Escherichia coli; Formycins; N-Glycosyl Hydrolases; Substrate Specificity; Sulfuric Acid Esters; Thermodynamics

1999
A single engineered point mutation in the adenine glycosylase MutY confers bifunctional glycosylase/AP lyase activity.
    Biochemistry, 2000, Aug-22, Volume: 39, Issue:33

    Topics: Amino Acid Sequence; Borohydrides; Carbon-Oxygen Lyases; Deoxyadenosines; Deoxyribonuclease IV (Phage T4-Induced); DNA Glycosylases; DNA Repair; DNA-(Apurinic or Apyrimidinic Site) Lyase; Escherichia coli; Escherichia coli Proteins; Formycins; Glycoside Hydrolases; Kinetics; Models, Chemical; Molecular Sequence Data; Multienzyme Complexes; N-Glycosyl Hydrolases; Point Mutation; Protein Engineering; Sequence Homology, Amino Acid; Substrate Specificity

2000