التفاصيل البيبلوغرافية
العنوان: |
Doxifluridine-conjugated 2-5A analog shows strong RNase L activation ability and tumor suppressive effect. |
المؤلفون: |
Kitamura, Yoshiaki1,2, Kito, Seiya1, Nakashima, Remi1, Tanaka, Katsuki1, Nagaoka, Kumi3, Kitade, Yukio1,2,3,4 ykkitade@gifu-u.ac.jp |
المصدر: |
Bioorganic & Medicinal Chemistry. Aug2016, Vol. 24 Issue 16, p3870-3874. 5p. |
مصطلحات موضوعية: |
*RIBONUCLEASE L, *OLIGOADENYLATES, *TUMOR suppressor genes, *CERVICAL cancer, *BINDING sites |
مستخلص: |
RNase L is activated by 2′,5′-oligoadenylates (2-5A) at subnanomolar levels to cleave single-stranded RNA. We previously reported the hypothesis that the introduction of an 8-methyladenosine residue at the 2′-terminus of the 2-5A tetramer shifts the 2-5A binding site of RNase L. In this study, we synthesized various 5′-modified 2-5A analogs with 8-methyladenosine at the 2′-terminus. The doxifluridine-conjugated 8-methyladenosine-substituted 2-5A analog was significantly more effective as an activator of RNase L than the parent 5′-monophophorylated 2-5A tetramer and showed a tumor suppressive effect against human cervical cancer cells. [ABSTRACT FROM AUTHOR] |
قاعدة البيانات: |
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