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Polyadenosine

In the first case, the reactions occurred with quite good yields of polymers, for example, polyadenosine [poly(A)], which was precipitated from the micelles. [Pg.267]

Minaga T, Kun E (1983b) Spectral analysis of the conformation of polyadenosine diphosphoribose. [Pg.67]

NAD glycohydrolases from rat liver nuclei, 66, 151 poly(ADP-ribose) synthetase from rat liver nuclei, 66, 154 poly(ADP-ribose) synthetase from calf thymus, 66, 159 extraction and quantitative determination of larger than tetrameric endogenous polyadenosine diphosphoribose from animal tissues, 66, 165 covalent modification of proteins by metabolites of NAD, 66, 168 coenzyme activity of NAD bound to polymer supports through the adenine moiety, 66, 176 use of differently immobilized nucleotides for binding NAD -dependent dehydrogenases, 66, 192. [Pg.503]

T. Shima, S. Hasegawa, S. Fujimura, H. Matsubara, and T. Sugimura, J. Biol Chem., 244 6632-6635 (1969). Studies on Polyadenosine Diphosphate-ribose. [Pg.168]

Fig. 3 The microRNA (miRNA) pathway. An miRNA is first transcribed as part of an imperfect hairpin in a longer Pol II transcript with 5 cap (open circle) and polyadenosine tail (AAAAAA). The hairpin (pre-miRNA) is removed from the transcript by the nuclear RNase III type enzyme Drosha and its partner, DGCR8. Exportin-5 (Xpo-5) transports the resulting by-product to the cytoplasm, where Dicer liberates a short-lived miRNA duplex. The duplex is unwound, and one strand enters RISC. If the miRNA is mismatched to its target (left), it does not induce cleavage, but may inhibit translation. With a perfect or near-perfect match (right), the target RNA is destroyed by RISC. Fig. 3 The microRNA (miRNA) pathway. An miRNA is first transcribed as part of an imperfect hairpin in a longer Pol II transcript with 5 cap (open circle) and polyadenosine tail (AAAAAA). The hairpin (pre-miRNA) is removed from the transcript by the nuclear RNase III type enzyme Drosha and its partner, DGCR8. Exportin-5 (Xpo-5) transports the resulting by-product to the cytoplasm, where Dicer liberates a short-lived miRNA duplex. The duplex is unwound, and one strand enters RISC. If the miRNA is mismatched to its target (left), it does not induce cleavage, but may inhibit translation. With a perfect or near-perfect match (right), the target RNA is destroyed by RISC.
I.U. Schraufstatter, D.B. Hinshaw, PA. Hyslop, R.G. Spragg, and C.G. Cochrane, Oxidant injury of cells. DNA strand-breaks activate polyadenosine diphosphate-ribose polymerase and lead to depletion of nicotinamide adenine dinucleotide, /. Clin. Invest. 77 1312 (1986). [Pg.286]

Junod AF, Jornot L, Petersen H. Differential effects of hyperoxia and hydn en peroxide on DNA damage, polyadenosine diphosphate-ribose polymerase activity, and nicotinamide adenine dinucl( -otide and adenosine triphosphate contents in cultured endothelial cells and fibroblasts. J Cell Physiol 1989 140 177-85. [Pg.196]

Adam GC, Parish CA, Wisniewski D, Meng J, Liu M, Calati K, Stein BD, Athanasopoulos J, Liberator P, Roemer T, Harris G, Chapman KT (2008) Application of Affinity Selection/ Mass Spectrometry to Determine the Structural Isomer of Pamafungins Responsible fra-Binding Polyadenosine Polymerase. J Am Chem Soc 130 16704... [Pg.266]

Doly J, Mandel P (1967) Mise en evidence de la biosynthese in vivo d un polymere compose, le polyadenosine diphosphoribose dans les noyaux de foie de poulet. C R Acad Sd 264 2687-2690... [Pg.8]

Okazaki H, Niedergang C, Mandel P (1976) Purification and properties of calf thymus polyadenosine diphosphate ribose polymerase. FEBS Lett 62 255-258... [Pg.8]

Minaga T, Kun E (1983) Spectral analysis of the conformation of polyadenosine diphospho-ribose - evidence indicating secondary structure. J Biol Chem 258 725-730... [Pg.46]

Minaga T, Romaschin AD, Kirsten E, Kun E (1979) The in vivo distribution of immunoreac-tive larger than tetrameric polyadenosine diphosphoribose in histone and nonhiston protein fraction of rat liver. J Biol Chem 254 9663-9668... [Pg.46]

Polyadenosine diphosphate ribose poIy(ADP-ribose) polymerase catalyzes the incorporation of the ADP-ribose moiety of NAD into a homopolymer of repeating ADP-ribose units covalently bound to histones and other nuclear protein acceptors [1,2]. This DNA-dependent enzyme, highly stimulated by nicks and DNA fragmentation [3,4], is thought to be involved in several basic functions of the chromatin, especially in DNA repair [5-7]. [Pg.190]

Cleaver JE (1985) Increased repair replication in human lymphoid cells by inhibition of polyadenosine diphosphoribose synthesis with no increase in patch sizes. Cancer Res 45 1163-1169... [Pg.250]

Romaschin AD, Kirsten E. Jackowski G, Kun E (1981) Quantitative isolation of oligo- and polyadenosine-diphosphoribosylated proteins by affinity chromatography from livers of normal and dimethylnitrosamine-treated Syrian hamsters. J Biol Chem 256 7800-7805... [Pg.488]

Pyran resembles the synthetic polynucleotides in regard to its action on the host immune response. The action of poly rI rC or the more potent polyadenosine uridine (poly rA rU) copolymers on immunologic response has been extensively reviewed elsewhere (Beers and Braun, 1971), and we have found similarities and differences between pyran and the polynucleotides. The action of poly rI rC in relation to immunologic and antiviral effects is only partly related to molecular weight (Morahan et al, 1972a, b), and these differences may relate to systemic biodegradabili-... [Pg.142]

Keith, G., Desgres, J., and De Murcia, G. (1990). Use of two-dimensional thin-layer chromatography for the components study of polyadenosine diphosphate ribose. Anal. Biochem. 191 309-313. [Pg.408]

See other pages where Polyadenosine is mentioned: [Pg.71]    [Pg.496]    [Pg.603]    [Pg.195]    [Pg.694]    [Pg.47]    [Pg.8]    [Pg.53]    [Pg.196]    [Pg.230]    [Pg.371]    [Pg.189]    [Pg.3]    [Pg.537]    [Pg.91]    [Pg.542]   
See also in sourсe #XX -- [ Pg.542 ]



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Polyadenosine diphosphate ribose polymerase

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