3590-36-1

Usage

Uses

Used in Biotechnology and Molecular Biology:
Cytidine, 5-methyl-, 5'-(dihydrogen phosphate) (8CI) is used as a key component in the study of DNA methylation for understanding gene regulation, cellular differentiation, and the development of various diseases. It helps researchers investigate the epigenetic modifications that occur in the genome, which can lead to a better understanding of the underlying mechanisms of diseases and the development of targeted therapies.
Used in Drug Development:
In the pharmaceutical industry, Cytidine, 5-methyl-, 5'-(dihydrogen phosphate) (8CI) is used as a starting material or intermediate in the synthesis of various drugs targeting DNA methylation and gene regulation. These drugs have potential applications in treating cancer, neurological disorders, and other conditions related to abnormal gene expression.
Used in Diagnostics:
Cytidine, 5-methyl-, 5'-(dihydrogen phosphate) (8CI) is also utilized in the development of diagnostic tools and assays for detecting and monitoring DNA methylation patterns. These diagnostic tools can be employed in clinical settings to identify specific diseases, predict disease progression, and evaluate the effectiveness of treatments.

Upstream product

• 2140-61-6 5-methylcytidine 
• 327174-86-7 5-methyl-CTP 

Relevant academic research and scientific papers

Synthesis of NAD analogs to develop bioorthogonal redox system

Three new nicotinamide adenine dinucleotide (NAD) analogs were synthesized, and their characteristics as cofactors for Escherichia coli malic enzyme (ME) and its double mutant ME L310R/Q401C were analyzed. Each pair of the NAD analog and the double mutant

Structure of the N-glycosidase MilB in complex with hydroxymethyl CMP reveals its Arg23 specifically recognizes the substrate and controls its entry

5-Hydroxymethylcytosine (5hmC) is present in T-even phage and mammalian DNA as well as some nucleoside antibiotics, including mildiomycin and bacimethrin, during whose synthesis 5hmC is produced by the hydrolysis of 5-hydroxymethyl cytidine 5'-monophosphate (hmCMP) by an N-glycosidase MilB. Recently, the MilB-CMP complex structure revealed its substrate specificity for CMP over dCMP. However, hmCMP instead of CMP is the preferred substrate for MilB as supported by that its KM for CMP is ～27-fold higher than that for hmCMP. Here, we determined the crystal structures of MilB and its catalytically inactive E103A mutant in complex with hmCMP. In the structure of the complex, Phe22 and Arg23 are positioned in a cage-like active site resembling the binding pocket for the flipped 5-methylcytosine (5mC) in eukaryotic 5mC-binding proteins. Van der Waals interaction between the benzene ring of Phe22 and the pyrimidine ring of hmCMP stabilizes its binding. Remarkably, upon hmCMP binding, the guanidinium group of Arg23 was bent ～65° toward hmCMP to recognize its 5-hydroxymethyl group, inducing semi-closure of the cage-like pocket. Mutagenesis studies of Arg23 and bioinformatics analysis demonstrate that the positively charged Arg/Lys at this site is critical for the specific recognition of the 5-hydroxymethyl group of hmCMP. The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.