256643-14-8

Upstream product

• 68144-26-3 5'-azido-5'-deoxy-N⁶-benzoyl-2',3'-O-isopropylidene adenosine 
• 4546-55-8 N-benzoyladenosine 
• 77-76-9 2,2-dimethoxy-propane 
• 39947-04-1 N-6-benzoyl-2',3'-O-isopropylideneadenosine 
• 40653-96-1 N⁶-benzoyl-2',3'-O-isopropylidene-5'-O-methylsulfonyladenosine 

Downstream Products

• 256643-15-9 5'-aminosulfamoyl-5'-deoxy-2',3'-O-isopropylidene-N⁶-benzoyladenosine 
• 213554-36-0 C₂₇H₃₆N₈O₉S 
• 949572-36-5 C₂₃H₂₄N₇O₆Cl 

Relevant academic research and scientific papers

Oligonucleotide analogues with integrated bases and backbones. Part 24: Synthesis, conformational analysis, and association of aminomethylene-linked self-complementary adenosine and uridine dinucleosides

Inspection of Maruzen models and force-field calculations suggest that oligonucleotide analogues integrating backbone and bases (ONIBs) with an aminomethylene linker form similar cyclic duplexes as the analogous oxymethylene linked dinucleosides. The self

Design, synthesis, and molecular modeling studies of 5′-deoxy-5′-ureidoadenosine: 5′-ureido group as multiple hydrogen bonding donor in the active site of S-adenosylhomocysteine hydrolase

5′-Deoxy-5′-ureidoadenosine was designed and synthesized as a potent inhibitor of S-adenosylhomocysteine hydrolase (SAH), in which 5′-ureido group acted as multiple hydrogen bonding donor in binding with active site residues of SAH in the molecular modeli

Molecular recognition of tyrosinyl adenylate analogues by prokaryotic tyrosyl tRNA synthetases

Molecular modelling and synthetic studies have been carried out on tyrosinyl adenylate and analogues to probe the interactions seen in the active site of the X-ray crystal structure of tyrosyl tRNA synthetase from Bacillus stearothermophilus, and to search for new inhibitors of this enzyme. Micromolar and sub-micromolar inhibitors of tyrosyl tRNA synthetases from both B. stearothermophilus and Staphylococcus aureus have been synthesised. The importance of the adenine ring to the binding of tyrosinyl adenylate to the enzyme, and the importance of water-mediated hydrogen bonding interactions, have been highlighted. The inhibition data has been further supported by homology modelling with the S. aureus enzyme, and by ligand docking studies. (C) 1999 Elsevier Science Ltd.