Tag: 100-200

Yu, Dan; Horton, John R.; Yang, Jie; Hajian, Taraneh; Vedadi, Masoud; Sagum, Cari A.; Bedford, Mark T.; Blumenthal, Robert M.; Zhang, Xing; Cheng, Xiaodong published an article in 2021, the title of the article was Human MettL3-MettL14 RNA adenine methyltransferase complex is active on double-stranded DNA containing lesions.Application In Synthesis of N-Methyl-7H-purin-6-amine And the article contains the following content:

MettL3-MettL14 methyltransferase complex has been studied widely for its role in RNA adenine methylation. This complex is also recruited to UV- and X-ray exposed DNA damaged sites, and its methyltransfer activity is required for subsequent DNA repair, though in theory this could result from RNA methylation of short transcripts made at the site of damage. We report here that MettL3-MettL14 is active in vitro on double-stranded DNA containing a cyclopyrimidine dimer – a major lesion of UV radiation-induced products – or an abasic site or mismatches. Furthermore, N6-methyladenine (N6mA) decreases misincorporation of 8-oxo-guanine (8-oxoG) opposite to N6mA by repair DNA polymerases. When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair. Finally, we observed that the N6mA reader domain of YTHDC1, which is also recruited to sites of DNA damage, binds N6mA that is located across from a single-base gap between two canonical DNA helixes. This YTHDC1 complex with a gapped duplex is structurally similar to DNA complexes with FEN1 and GEN1 – two members of the nuclease family that act in nucleotide excision repair, mismatch repair and homologous recombination, and which incise distinct non-B DNA structures. Together, the parts of our study provide a plausible mechanism for N6mA writer and reader proteins acting directly on lesion-containing DNA, and suggest in vivo experiments to test the mechanisms involving methylation of adenine. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Application In Synthesis of N-Methyl-7H-purin-6-amine

The Article related to mettl3 mettl14 double stranded dna lesion, Biochemical Genetics: Gene Structure and Organization and other aspects.Application In Synthesis of N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On May 5, 2022, Larivera, Simone; Meister, Gunter published an article.Reference of N-Methyl-7H-purin-6-amine The title of the article was Domain confusion 2: m6 A-independent role of YTHDC2. And the article contained the following:

YTH proteins utilize YTH domains to interact with N6-methyladenines (m6A); however, Li et al. (2022) show that YTHDC2 binds U-rich motifs instead and functions independently of m6A through its unusual DExD helicase domain during spermatogenesis in mice and fish. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Reference of N-Methyl-7H-purin-6-amine

The Article related to methyladenine domain confusion, General Biochemistry: Proteins and Their Constituents and other aspects.Reference of N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On March 15, 2022, Iwasaki, Yuka; Ookuro, Yurino; Iida, Keisuke; Nagasawa, Kazuo; Yoshida, Wataru published an article.Synthetic Route of 443-72-1 The title of the article was Destabilization of DNA and RNA G-quadruplex structures formed by GGA repeat due to N6-methyladenine modification. And the article contained the following:

N6-methyladenine (m6A) is the most abundant RNA modification in eukaryotic RNA. Further, m6A has been identified in the genomic DNA of both eukaryotes and prokaryotes. The G-quadruplex (G4) structure is a non-canonical nucleic acid structure formed by the stacking of G:G:G:G tetrads. In this study, we evaluated the effect of m6A modifications on G4 structures formed by GGA repeat oligonucleotides, d(GGA)8, d(GGA)4, and r(GGA)4. The d(GGA)8 forms an intramol. tetrad:heptad:heptad:tetrad G4 structure, while d(GGA)4 forms a dimerized intermol. tetrad:heptad:heptad:tetrad G4 structure. r(GGA)4 forms a dimerized intermol. tetrad:hexad:hexad:tetrad G4 structure. CD melting anal. demonstrated that (1) m6A modifications destabilized the G4 structure formed by d(GGA)8, (2) m6A modification at A3 disrupted the G4 structure formed by d(GGA)4, and (3) m6A modification at A3 destabilized the G4 structure formed by r(GGA)4. M6A modifications may be involved in controlling G4 structure formation to regulate biol. functions. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Synthetic Route of 443-72-1

The Article related to dna rna gquadruplex structure destabilization gga repeat methyladenine modification, g-quadruplex, gga repeat, n(6)-methyladenine, thermal stability, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Synthetic Route of 443-72-1

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

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

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On March 31, 2021, Zhang, Xing; Blumenthal, Robert M.; Cheng, Xiaodong published an article.Recommanded Product: N-Methyl-7H-purin-6-amine The title of the article was A Role for N6-Methyladenine in DNA Damage Repair. And the article contained the following:

The leading cause of mutation due to oxidative damage is 8-oxo-2′-deoxyguanosine (8-oxoG) mispairing with adenine (Ade), which can occur in two ways. First, guanine of a G:C DNA base pair can be oxidized. If not repaired in time, DNA polymerases can mispair Ade with 8-oxoG in the template. This 8-oxoG:A can be repaired by enzymes that remove Ade opposite to template 8-oxoG, or 8-oxoG opposite to Cyt. Second, free 8-oxo-dGTP can be misincorporated by DNA polymerases into DNA opposite template Ade. However, there is no known repair activity that removes 8-oxoG opposite to template Ade. We suggest that a major role of N6-methyladenine in mammalian DNA is minimizing incorporation of 8-oxoG opposite to Ade by DNA polymerases following adduct formation. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Recommanded Product: N-Methyl-7H-purin-6-amine

The Article related to methyladenine dna damage repair, 8-oxoguanine, dna adenine methylation, mettl3-mettl14, ythdc1, single-stranded dna, General Biochemistry: Nucleic Acids and Their Constituents and other aspects.Recommanded Product: N-Methyl-7H-purin-6-amine

Referemce:
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

Referemce:
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

Referemce:
Imidazole – Wikipedia,
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

Referemce:
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

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem