Activation of 2-5A-dependent RNase by analogs of 2-5A (5'-O-triphosphoryladenylyl(2'—-5')adenylyl(2'—-5')adenosine ) using 2',5'-tetraadenylate (core)-cellulose.
نویسندگان
چکیده
منابع مشابه
A bipartite model of 2-5A-dependent RNase L.
The 2-5A-dependent RNase (RNase L) is a tightly regulated endoribonuclease of higher vertebrates that is catalytically active only after engaging unusual effector molecules consisting of the 2',5'-linked oligoadenylates, p1-3A(2'p5'A)>/=2 (2-5A). Progressive truncations from either terminus have provided insight into the structure, function, and regulation of RNase L. We determined that deletio...
متن کاملA dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferon.
2-5A-dependent RNase is the terminal factor in the interferon-regulated 2-5A system thought to function in both the molecular mechanism of interferon action and in the general control of RNA stability. However, direct evidence for specific functions of 2-5A-dependent RNase has been generally lacking. Therefore, we developed a strategy to block the 2-5A system using a truncated form of 2-5A-depe...
متن کامل5A.2 Large Out-of-Core Tetrahedral Meshing
We present an effective strongly uncoupled method, which, given a closed and watertight surface mesh, generates its Delaunay constrained tetrahedrisation into sub-domains. Uncoupled means here that once chosen, a sub-domain interface will not be changed anymore. This method aims at preserving in the final tetrahedral mesh the properties of the mesh which would have been produced by the original...
متن کاملDoxifluridine-conjugated 2-5A analog shows strong RNase L activation ability and tumor suppressive effect.
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 doxiflu...
متن کاملOnly one 3'-hydroxyl group of ppp5' A2'p5'A2'p5' A (2-5A) is required for activation of the 2-5A-dependent endonuclease.
To investigate the relative importance of each of the ribose 3'-hydroxyl groups of 2-5A (ppp5' A2'p5'A2'-p5' A) in determining binding to and activation of the 2-5A-dependent endonuclease (RNase L), the 3'-hydroxyl functionality of each adenosine moiety of 2-5A trimer triphosphate was sequentially replaced by hydrogen. The analog in which the 5'-terminal adenosine was replaced by 3'-deoxyadenos...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)62691-8