Category: 55662-66-3

Kost, A. A.; Ermolin, S. V. published an article in 1978, the title of the article was Fluorescent derivatives of cytosine.Recommanded Product: Imidazo[1,2-c]pyrimidin-5(6H)-one And the article contains the following content:

The fluorescence of ethenocytosines, e.g., I (R = Me, H, Ph; R1 = H, Me), was investigated by PPP MO calculations The π-electronic charges of the atoms do not change appreciably on excitation of the mols. The electronic excitation of these compounds is more diffuse than that of cytosine. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Recommanded Product: Imidazo[1,2-c]pyrimidin-5(6H)-one

The Article related to fluorescent ethenocytosine mo, Physical Organic Chemistry: Spectral and Related Studies and other aspects.Recommanded Product: Imidazo[1,2-c]pyrimidin-5(6H)-one

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Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On February 1, 1994, Dosanjh, M. K.; Chenna, A.; Kim, E.; Fraenkel-Conrat, H.; Samson, L.; Singer, B. published an article.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was All four known cyclic adducts formed in DNA by the vinyl chloride metabolite chloroacetaldehyde are released by a human DNA glycosylase. And the article contained the following:

The authors have previously reported that human cells and tissues contain a 1,N6-ethenoadenine (εA)-binding protein, which, through glycosylase activity, releases both 3-methyladenine (m3A) and εA from DNA treated with methylating agents or the vinyl chloride metabolite chloroacetaldehyde, resp. The authors now find that both the partially purified human εA-binding protein and cell-free extracts containing the cloned human m3A-DNA glycosylase release all 4 cyclic etheno adducts – namely εA, 3,N4-ethenocytosine (εC), N2,3-ethenoguanine (N2,3-εG), and 1,N2-ethenoguanine (1,N2-εG). Base release was both time- and protein concentration-dependent. Both εA and εC were excised at similar rates, while 1,N2-εG and N2,3-εG were released much more slowly under identical conditions. The cleavage of glycosyl bonds of several heterocyclic adducts as well as those of simple methylated adducts by the same human glycosylase appears unusual in enzymol. This raises the question of how such a multiple, divergent activity evolved in humans and what may be its primary substrate. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one

The Article related to chloroacetaldehyde cyclic etheno adduct release, methyladenine dna glycosylase human chloroacetaldehyde, Toxicology: Chemicals (Household, Industrial, General) and other aspects.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one

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Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On June 30, 2015, Zdzalik, Daria; Domanska, Anna; Prorok, Paulina; Kosicki, Konrad; van den Born, Erwin; Falnes, Pal Oe.; Rizzo, Carmelo J.; Guengerich, F. Peter; Tudek, Barbara published an article.Electric Literature of 55662-66-3 The title of the article was Differential repair of etheno-DNA adducts by bacterial and human AlkB proteins. And the article contained the following:

AlkB proteins are evolutionary conserved Fe(II)/2-oxoglutarate-dependent dioxygenases, which remove alkyl and highly promutagenic etheno(ε)-DNA adducts, but their substrate specificity has not been fully determined We developed a novel assay for the repair of ε-adducts by AlkB enzymes using oligodeoxynucleotides with a single lesion and specific DNA glycosylases and AP-endonuclease for identification of the repair products. We compared the repair of three ε-adducts, 1,N6-ethenoadenine (εA), 3,N4-ethenocytosine (εC) and 1,N2-ethenoguanine (1,N2-εG) by nine bacterial and two human AlkBs, representing four different structural groups defined on the basis of conserved amino acids in the nucleotide recognition lid, engaged in the enzyme binding to the substrate. Two bacterial AlkB proteins, MT-2B (from Mycobacterium tuberculosis) and SC-2B (Streptomyces coelicolor) did not repair these lesions in either double-stranded (ds) or single-stranded (ss) DNA. Three proteins, RE-2A (Rhizobium etli), SA-2B (Streptomyces avermitilis), and XC-2B (Xanthomonas campestris) efficiently removed all three lesions from the DNA substrates. Interestingly, XC-2B and RE-2A are the first AlkB proteins shown to be specialized for ε-adducts, since they do not repair methylated bases. Three other proteins, EcAlkB (Escherichia coli), SA-1A, and XC-1B removed εA and εC from ds and ssDNA but were inactive toward 1,N2-εG. SC-1A repaired only εA with the preference for dsDNA. The human enzyme ALKBH2 repaired all three ε-adducts in dsDNA, while only εA and εC in ssDNA and repair was less efficient in ssDNA. ALKBH3 repaired only εC in ssDNA. Altogether, we have shown for the first time that some AlkB proteins, namely ALKBH2, RE-2A, SA-2B and XC-2B can repair 1,N2-εG and that ALKBH3 removes only εC from ssDNA. Our results also suggest that the nucleotide recognition lid is not the sole determinant of the substrate specificity of AlkB proteins. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Electric Literature of 55662-66-3

The Article related to alkb ethenodna adduct oxidative dealkylation oligodeoxynucleotide, 1,n(2)-ethenoguanine, 1,n(6)-ethenoadenine, 3,n(4)-ethenocytosine, alkb, dna repair, etheno adducts, Biochemical Genetics: Gene Structure and Organization and other aspects.Electric Literature of 55662-66-3

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On June 30, 1978, Marzilli, Luigi G.; Hanson, Brian E.; Kapili, Leilani; Rose, Seth D.; Beer, Michael published an article.Computed Properties of 55662-66-3 The title of the article was Osmium-labeled polynucleotides: reaction of osmium tetraoxide, with poly-1,N6-ethenoadenylic acid. And the article contained the following:

OsO4, in the presence of ligands such as pyridine and bipyridine, added across the etheno bridge of 1,N6-etheno-9-methyladenine and poly(1,N6-ethenoadenylic acid). The Os:P ratio in the labeled polynucleotide was ≃1 when bipyridine was used as the stabilizing ligand. A similar study with poly(C), which was partially modified with chloroacetaldehyde so that some bases were converted to 3,N4-ethenocytosine, gave an Os:P ratio of ≃1.3. Calf thymus DNA, in which adenine and cytosine bases were modified by chloroacetaldehyde, gave an Os:P ratio of ≃1 after 24 h. Thus, 3,N4-ethenocytosine may add 2 Os labels. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Computed Properties of 55662-66-3

The Article related to polyethenoadenylate addition reaction osmium, ethenoadenylate polymer reaction osmium, ethenycytosine reaction osmium, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Computed Properties of 55662-66-3

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Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On September 30, 2000, Sagi, Janos; Perry, Alex; Hang, Bo; Singer, B. published an article.Product Details of 55662-66-3 The title of the article was Differential Destabilization of the DNA Oligonucleotide Double Helix by a T·G Mismatch, 3,N4-Ethenocytosine, 3,N4-Ethanocytosine, or an 8-(Hydroxymethyl)-3,N4-ethenocytosine Adduct Incorporated into the Same Sequence Contexts. And the article contained the following:

The T·G mismatch and the exocyclic adduct 3,N4-ethenocytosine (εC) are repaired by the same enzyme, the human G/T(U) mismatch-DNA glycosylase (TDG). This enzyme removes the T, U, or εC base from duplex DNA. The rate of cleavage was found to differ with the lesion and was also affected by neighbor sequences [Hang, B., Medina, M., Fraenkel-Conrat, H., and Singer, B. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 13561-13566]. Since sequence influences duplex stability, we determined the thermodn. stability of T·G and εC-containing 15-mer duplexes in which the bases flanking the lesion were systematically varied. The duplexes contained central 5′-TTXTT, 5′-AAXAA, 5′-CCXCC, or 5′-GGXGG sequences, where X is T, εC, or two closely related structural derivatives of εC: 3,N4-ethanocytosine (EC) and 8-(hydroxymethyl)-εC (8-HM-εC). Each of the four lesions, incorporated opposite G, decreased both the thermal (Tm) and thermodn. stability (ΔG°37) of the 15-mer control duplexes. On the basis of the Tm and ΔG°37 values, the order of destabilization of the TTXTT sequence in 15-mer duplexes was as follows: 8-HM-εC > EC > εC > T·G. The ΔTm values range from -15.8 to -9.5 °C when Ct = 8 μM. Duplexes with flanking AA or TT neighbors were more destabilized, by an average of 2 °C, than those with flanking GG or CC neighbors. The base opposite the modified base also influenced duplex stability. Within the TT context, of the four changed bases opposite the adducts, C had the greatest destabilizing effect, up to -18.4 °C. In contrast, a G opposite an adduct was generally the least destabilizing, and the smallest value was -3.0 °C. Destabilizations were enthalpic in origin. Thus, this work shows that independently changing the modified base, the sequence, or the base opposite the lesion each affects the stability of the duplex, to significantly varying extents. The potential contribution of the thermodn. stability to repair efficiency is discussed. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Product Details of 55662-66-3

The Article related to dna thermodn stability mismatch, oligodeoxyribonucleotide cytosine derivative adduct stability, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Product Details of 55662-66-3

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Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On December 24, 2015, Lenz, Stefan A. P.; Kellie, Jennifer L.; Wetmore, Stacey D. published an article.COA of Formula: C6H5N3O The title of the article was Glycosidic Bond Cleavage in DNA Nucleosides: Effect of Nucleobase Damage and Activation on the Mechanism and Barrier. And the article contained the following:

Although DNA damage can have a variety of deleterious effects on cells (e.g., senescence, death, and rapid growth), the base excision repair (BER) pathway combats the effects by removing several types of damaged DNA. Since the first BER step involves cleavage of the bond between the damaged nucleobase and the DNA sugar-phosphate backbone, we have used d. functional theory to compare the intrinsic stability of the glycosidic bond in a number of common DNA oxidation, deamination, and alkylation products to the corresponding natural nucleosides. Our calculations predict that the dissociative (SN1) and associative (SN2) pathways are nearly isoenergetic, with the dissociative pathway only slightly favored on the Gibbs reaction surface for all canonical and damaged nucleosides, which suggests that DNA damage does not affect the inherently most favorable deglycosylation pathway. More importantly, with the exception of thymine glycol, all DNA lesions exhibit reduced glycosidic bond stability relative to the undamaged nucleosides. Furthermore, the trend in the magnitude of the deglycosylation barrier reduction directly correlates with the relative nucleobase acidity (at N9 for purines or N1 for pyrimidines), which thereby provides a computationally efficient, qual. measure of the glycosidic bond stability in DNA damage. The effect of nucleobase activation (protonation) at different sites predicts that the positions leading to the largest reductions in the deglycosylation barrier are typically used by DNA glycosylases to facilitate base excision. Finally, deaza purine derivatives are found to have greater glycosidic bond stability than the canonical counterparts, which suggests that alterations to excision rates measured using these derivatives to probe DNA glycosylase function must be interpreted in reference to the inherent differences in the nucleoside reactivity. Combined with previous studies of the deglycosylation of DNA nucleosides, the current study provides a greater fundamental understanding about the reactivity of the glycosidic bond in damaged DNA, which has direct implications to the function of critical DNA repair enzymes. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).COA of Formula: C6H5N3O

The Article related to glycosidic bond cleavage dna damage nucleoside nucleobase deglycosylation, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.COA of Formula: C6H5N3O

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Imidazole | C3H4N2 – PubChem

On September 13, 2012, Srinivasadesikan, Venkatesan; Sahu, Prabhat K.; Lee, Shyi-Long published an article.Synthetic Route of 55662-66-3 The title of the article was Quantum Mechanical Calculations for the Misincorporation of Nucleotides Opposite Mutagenic 3,N4-Ethenocytosine. And the article contained the following:

The ubiquitous nature and persistence of exocyclic DNA adducts suggest their involvement as initiators of carcinogenesis. We have investigated the misincorporation properties of the exocyclic DNA adduct, 3,N4-ethenocytosine (εC), using DFT and DFT-D methods. Computational investigations have been carried out by using the B3LYP, M062X, and wB97XD methods with the 6-31+G* basis set to determine the hydrogen bonding strengths, binding energy, and phys. parameters. The single point energy calculations have been carried out at MP2/6-311++G** on corresponding optimized geometries. The energies were compared among the 3,N4-ethenocytosine adduct with DNA bases to find the most stable conformer. The solvent phase calculations have also been carried out using the CPCM model. The computed reaction enthalpy values provide computational insights to the earlier exptl. observation in in vitro, E.coli, and mammalian cells of a high level of substitution mutation in which C → A transversion results from εC-T pairing [εC-T3 and εC-T4] in the adduct containing DNA sequence. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Synthetic Route of 55662-66-3

The Article related to ethenocytosine base pairing mismatch nucleotide misincorporation dna, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Synthetic Route of 55662-66-3

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Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Aliakbar Tehrani, Zahra; Torabifard, Hedieh; Fattahi, Alireza published an article in 2012, the title of the article was Thermochemical properties of some vinyl chloride-induced DNA lesions: detailed view from NBO & AIM analysis.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one And the article contains the following content:

Etheno-damaged DNA adducts such as 3,N4-ethenocytosine, N2,3-ethenoguanine, and 1,N2-ethenoguanine are associated with carcinogenesis and cell death. These inevitable damages are counteracted by glycosylase enzymes, which cleave damaged nucleobases from DNA. Escherichia coli alkyl purine DNA glycosylase is the enzyme responsible for excising damaged etheno adducts from DNA in humans. In an effort to understand the intrinsic properties of these mols., we examined gas-phase acidity values and proton affinities (PA) of multiple sites of these mols. as well as equilibrium tautomerization and base pairing properties by quantum mech. calculations We also used calculations to compare the acidic and basic properties of these etheno adduct with those of the normal bases-cytosine and guanine nucleobases. We hypothesize that alkyl DNA glycosylase may cleave certain damaged nucleobases as anions and that the active site may take advantage of a nonpolar environment to favor deprotonated cytosine or guanine as a leaving group vs. damaged nucleobases. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Name: Imidazo[1,2-c]pyrimidin-5(6H)-one

The Article related to dna damage thermochem property ethenocytosine ethenoguanine, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Talhaoui, Ibtissam; Couve, Sophie; Ishchenko, Alexander A.; Kunz, Christophe; Schaer, Primo; Saparbaev, Murat published an article in 2013, the title of the article was 7,8-dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by Escherichia coli and human mismatch-specific uracil/thymine-DNA glycosylases.Computed Properties of 55662-66-3 And the article contains the following content:

Hydroxyl radicals predominantly react with the C8 of purines in DNA forming 7,8-dihydro-8-oxoguanine (8oxoG) and 7,8-dihydro-8-oxoadenine (8oxoA) adducts, which are highly mutagenic in mammalian cells. The majority of oxidized DNA bases are removed by DNA glycosylases in the base excision repair pathway. Here, the authors report for the 1st time that human thymine-DNA glycosylase (hTDG) and Escherichia coli mismatch-specific uracil-DNA glycosylase (MUG) can remove 8oxoA from 8oxoA·T, 8oxoA·G, and 8oxoA·C pairs. Comparison of the kinetic parameters of the reaction indicated that full-length hTDG excised 8oxoA, 3,N4-ethenocytosine (εC) and T with similar efficiency (kmax = 0.35, 0.36, and 0.16 min-1, resp.) and was more proficient as compared with its bacterial homolog MUG. The N-terminal domain of the hTDG protein was essential for 8oxoA-DNA glycosylase activity, but not for εC repair. Interestingly, the TDG status had little or no effect on the proliferation rate of mouse embryonic fibroblasts after exposure to γ-irradiation Nevertheless, using whole cell-free extracts from DNA glycosylase-deficient murine embryonic fibroblasts and E. coli, the authors demonstrated that the excision of 8oxoA from 8oxoA·T and 8oxoA·G had an absolute requirement for TDG and MUG, resp. The data established that MUG and TDG can counteract the genotoxic effects of 8oxoA residues in vivo. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Computed Properties of 55662-66-3

The Article related to dna repair oxoadenine removal uracil thymine glycosylase, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Computed Properties of 55662-66-3

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Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On August 22, 2000, Sung, Jung-Suk; Mosbaugh, Dale W. published an article.SDS of cas: 55662-66-3 The title of the article was Escherichia coli Double-Strand Uracil-DNA Glycosylase: Involvement in Uracil-Mediated DNA Base Excision Repair and Stimulation of Activity by Endonuclease IV. And the article contained the following:

Escherichia coli double-strand uracil-DNA glycosylase (Dug) was purified to apparent homogeneity as both a native and recombinant protein. The mol. weight of recombinant Dug was 18,670, as determined by matrix-assisted laser desorption-ionization mass spectrometry. Dug was active on duplex oligonucleotides (34-mers) that contained site-specific U·G, U·A, ethenoC·G, and ethenoC·A targets; however, activity was not detected on DNA containing a T·G mispair or single-stranded DNA containing either a site-specific uracil or ethenoC residue. One of the distinctive characteristics of Dug was that the purified enzyme excised a near stoichiometric amount of uracil from U·G-containing oligonucleotide substrate. Electrophoretic mobility shift assays revealed that the lack of turnover was the result of strong binding by Dug to the reaction product apyrimidinic-site (AP) DNA. Addition of E. coli endonuclease IV stimulated Dug activity by enhancing the rate and extent of uracil excision by promoting dissociation of Dug from the AP·G-containing 34-mer. Catalytically active endonuclease IV was apparently required to mediate Dug turnover, since the addition of 5 mM EDTA mitigated the effect. Further support for this interpretation came from the observations that Dug preferentially bound 34-mer containing an AP·G target, while binding was not observed on a substrate incised 5′ to the AP-site. We also investigated whether Dug could initiate a uracil-mediated base excision repair pathway in E. coli NR8052 cell extracts using M13mp2op14 DNA (form I) containing a site-specific U·G mispair. Anal. of reaction products revealed a time dependent appearance of repaired form I DNA; addition of purified Dug to the cell extract stimulated the rate of repair. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).SDS of cas: 55662-66-3

The Article related to escherichia dsdna uracil dna glycosylase, endonuclease iv dsdna uracil dna glycosylase stimulation, Enzymes: Separation-Purification-General Characterization and other aspects.SDS of cas: 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem