White crystalline powder
peels of Punica granatum L.
1-(b-D-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine/4-Amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydro-2-furanyl]-2(1H)-pyrimidinone/2(1H)-Pyrimidinone, 4-amino-1-β-D-ribofuranosyl-/1-β-D-Ribofuranosylcytosine/4-Amino-1-β-δ-ribofuranosyl-2(1H)-pyrimidinone/4-Amino-1-(β-D-ribofuranosyl)pyrimidin-2(1H)-on/Cytidine/4-Amino-1-b-D-ribofuranosyl-2(1H)-pyrimidinone/Cyd/Cytidin/1-β-D-ribofuranosyl-Cytosine/Citidine/1-(b-δ-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine/Cytosine, 1-β-D-ribofuranosyl-/d-cytidine/1-β-δ-Ribofuranosylcytosine/CYTIDINE extrapure/1-b-D-Ribofuranosylcytosine/2-Pyrimidinol, 1,4-dihydro-4-imino-1-β-D-ribofuranosyl-/4-Imino-1-(β-D-ribofuranosyl)-1,4-dihydro-2-pyrimidinol
529.7±60.0 °C at 760 mmHg
210-220 °C (dec.)(lit.)
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:65-46-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Post-transcriptional RNA modifications, the epitranscriptome, play important roles in modulating the functions of RNA species. Modifications of rRNA are key for ribosome production and function. Identification and characterization of enzymes involved in epitranscriptome shaping is instrumental for the elucidation of the functional roles of specific RNA modifications. Ten modified sites have been thus far identified in the mammalian mitochondrial rRNA. Enzymes responsible for two of these modifications have not been characterized. Here, we identify METTL15, show that it is the main N4-methylcytidine (m4C) methyltransferase in human cells and demonstrate that it is responsible for the methylation of position C839 in mitochondrial 12S rRNA. We show that the lack of METTL15 results in a reduction of the mitochondrial de novo protein synthesis and decreased steady-state levels of protein components of the oxidative phosphorylation system. Without functional METTL15, the assembly of the mitochondrial ribosome is decreased, with the late assembly components being unable to be incorporated efficiently into the small subunit. We speculate that m4C839 is involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits. Taken together our data show that METTL15 is a novel protein necessary for efficient translation in human mitochondria.
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
METTL15 introduces N4-methylcytidine into human mitochondrial 12S rRNA and is required for mitoribosome biogenesis.
Van Haute L1, Hendrick AG2, D'Souza AR1, Powell CA1, Rebelo-Guiomar P1,3, Harbour ME1,2, Ding S1, Fearnley IM1, Andrews B2, Minczuk M1.
2019 Nov 4
To restrict pathogens, in a normal human cell, APOBEC3 enzymes mutate cytosine to uracil in foreign single-stranded DNAs. However, in cancer cells, APOBEC3B (one of seven APOBEC3 enzymes) has been identified as the primary source of genetic mutations. As such, APOBEC3B promotes evolution and progression of cancers and leads to development of drug resistance in multiple cancers. As APOBEC3B is a non-essential protein, its inhibition can be used to suppress emergence of drug resistance in existing anti-cancer therapies. Because of the vital role of APOBEC3 enzymes in innate immunity, selective inhibitors targeting only APOBEC3B are required. Here, we use the discriminative properties of wild-type APOBEC3A, APOBEC3B and APOBEC3G to deaminate different cytosines in the CCC-recognition motif in order to best place the cytidine analogue 2′-deoxyzebularine (dZ) in the CCC-motif. Using several APOBEC3 variants that mimic deamination patterns of wild-type enzymes, we demonstrate that selective inhibition of APOBEC3B in preference to other APOBEC3 constructs is feasible for the dZCC motif. This work is an important step towards development of in vivo tools to inhibit APOBEC3 enzymes in living cells by using short, chemically modified oligonucleotides.
Selective inhibition of APOBEC3 enzymes by single-stranded DNAs containing 2'-deoxyzebularine.
Barzak FM1, Harjes S, Kvach MV, Kurup HM, Jameson GB, Filichev VV, Harjes E.
2019 Nov 6
DNA methylation is a typical epigenetic phenomenon. Numerous methods for detecting global DNA methylation levels have been developed, among which LC-MS/MS has emerged as an excellent method from the viewpoint of sensitivity, reproducibility, and cost. However, LC-MS/MS methods have limitations due to a lack of the stability and the standardization required for a laboratory assay. The present study aimed to establish a robust assay that guarantees highly accurate measurements of global DNA methylation levels. There are at least three facets of the developed method. The first is discovery of the solvent conditions to minimize sodium adducts. The second is improvement of separation of nucleosides by LC using the columns that had not been used in previous similar studies. The third is success in reduction of the uncertainty of the measurement results, which was achieved by the calibration using the ratio of mdC but not the absolute amount in the presence of internal standards. These facets represent the advantage over methods reported previously. Our developed method enables quantification of DNA methylation with a short time length (8 min) for one analysis as well as with the high reproducibility of measurements that is represented by the inter-day CV% being less than 5%. In addition, data obtained from measuring global DNA methylation levels in cultured cell lines, with or without pharmacological demethylation, support its use for biomedical research. This assay is expected to allow us to conduct initial screening of epigenetic alterations or aberration in a variety of cells.
DNA methylation; LC-MS/MS; Measurement uncertainty; Nucleoside; Optimization
Intensive optimization and evaluation of global DNA methylation quantification using LC-MS/MS.
Nakagawa T1, Wakui M2, Hayashida T3, Nishime C4, Murata M1.
Cytidine is a nucleoside molecule that is formed when cytosine is attached to a ribose ring, cytidine is a component of RNA.Target: Nucleoside antimetabolite/analogCytidine is a nucleoside molecule that is formed when cytosine is attached to a ribose ring (also known as a ribofuranose) via a β-N1-glycosidic bond. Cytidine is a component of RNA. If cytosine is attached to a deoxyribose ring, it is known as a deoxycytidine. Dietary sources of cytidine include foods with high RNA (ribonucleic acid) content, such as organ meats, Brewer's yeast, as well as pyrimidine-rich foods such as beer. During digestion, RNA-rich foods are broken-down into ribosyl pyrimidines (cytidine and uridine), which are absorbed intact. In humans, dietary cytidine is converted into uridine, which is probably the compound behind cytidine's metabolic effects.There are a variety of cytidine analogs with potentially useful pharmacology. For example, KP-1461 is an anti-HIV agent that works as a viral mutagen, and zebularine exists in E. coli and is being examined for chemotherapy. Low doses of azacitidine and its analog decitabine have shown results against cancer through epigenetic demethylation.