325464-33-3

Upstream product

• 5707-04-0 Phenylselenyl chloride 
• 2966-50-9 silver trifluoroacetate 
• 191480-67-8 ((1S,2R)-2-Benzyloxymethyl-cyclopent-3-enyloxy)-tert-butyl-diphenyl-silane 

Downstream Products

• 325464-37-7 (1S,4S)-4-(2,2-dimethyl-1,1-diphenyl-1-silapropoxy)-3-[(phenylmethoxy)methyl]cyclopent-2-en-1-ol 
• 325464-38-8 (5S)-[5-(2,2-dimethyl-1,1-diphenyl-1-silapropoxy)cyclopent-1-enyl](phenylmethoxy)methane 
• 325464-42-4 (1R,2S,5S)-1-[(phenylmethoxy)methyl]bicyclo[3.1.0]hexan-2-ol 
• 325464-40-2 (1S)-2-[(phenylmethoxy)methyl]cyclopent-2-en-1-ol 
• 325464-35-5 (1S,2S,3R,4S)-4-(2,2-dimethyl-1,1-diphenyl-1-silapropoxy)-3-[(phenylmethoxy)methyl]-2-(phenylselenamethyl)cyclopentan-1-ol 

Relevant academic research and scientific papers

Use of oligodeoxyribonucleotides with conformationally constrained abasic sugar targets to probe the mechanism of base flipping by hhaI DNA (cytosine C5)-methyltransferase

X-ray crystallographic studies of HhaI DNA (cytosine-C5)-methyltransferase (M.HhaI) covalently linked to methylated 5-fluorocytosine in DNA provided the first direct evidence that the cytosine residue targeted for methylation was "flipped" out of the heli

Inhibition of (cytosine C5)-methyltransferase by oligonucleotides containing flexible (cyclopentane) and conformationally constrained (bicyclo[3.1.0]hexane) abasic sites

Pseudorotationally locked sugar analogues based on bicyclo[3.1.0]-hexane templates were placed in DNA duplexes as abasic target sites in the M.HhaI recognition sequence. The binding affinity of the enzyme increases when the abasic site is constrained to t