606-02-0Relevant articles and documents
Mechanism of RNA cleavage by imidazole. Catalysis vs medium effects
Kirby,Marriott
, p. 833 - 834 (1995)
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Cleavage of short oligoribonucleotides by a Zn2+binding multi-nucleating azacrown conjugate
Laine, Maarit,L?nnberg, Tuomas,Helkearo, Mia,L?nnberg, Harri
, p. 111 - 117 (2016/10/04)
A multi-nucleating azacrown conjugate (5a) consisting of two 3,5-bis(1,5,9-triazacyclododecan-3-yloxymethyl)benzyl groups attached to 1 and 7 sites of cyclen was prepared and tested as an artificial ribonuclease. The conjugate in the presence of five equivalents of zinc nitrate expectedly showed uridine selectivity comparable to that 1,3,5-tris(1,5,9-triazacyclododecan-3-yl)benzene (2), a compound known to bind to two adjacent uridine residues and cleave the intervening phosphodiester bond. 5a was, however, unable to discriminate between two and three adjacent uridine residues, but cleaved oligonucleotides containing a UpU and UpUpU site at a comparable rate, even when present at sub-saturating concentrations.
Guanidine based self-assembled monolayers on Au nanoparticles as artificial phosphodiesterases
Salvio, Riccardo,Cincotti, Antonio
, p. 28678 - 28682 (2014/07/22)
Gold nanoparticles passivated with a long chain alkanethiol decorated with a phenoxyguanidine moiety were prepared and investigated as catalysts in the cleavage of the RNA model compound HPNP and diribonucleoside monophosphates. The catalytic efficiency and the high effective molarity value of the Au monolayer protected colloids points to a high level of cooperation between the catalytic groups.
An RNA modification with remarkable resistance to RNase A
Ghidini, Alice,Ander, Charlotte,Winqvist, Anna,Stroemberg, Roger
supporting information, p. 9036 - 9038 (2013/09/24)
A 3′-deoxy-3′-C-methylenephosphonate modified diribonucleotide is highly resistant to degradation by spleen phosphodiesterase and not cleaved at all by snake venom phosphodiesterase. The most remarkable finding is that, despite the fact that both the vicinal 2-hydroxy nucleophile and the 5′-oxyanion leaving group are intact, the 3′-methylenephosponate RNA modification is also highly resistant towards the action of RNase A.