Category: 55662-66-3

On August 31, 1999, Al Mamun, Abu Amar M.; Rahman, M. Sayeedur; Humayun, M. Zafri published an article.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was Escherichia coli cells bearing mutA, a mutant glyV tRNA gene, express a recA-dependent error-prone DNA replication activity. And the article contained the following:

A base substitution mutation (mutA) in the Escherichia coli glyV tRNA gene potentiates asp → gly mistranslation and confers a strong mutator phenotype that is SOS independent, but requires recA, recB and recC genes. Here, we demonstrate that mutA cells express an error-prone DNA polymerase by using an in vitro exptl. system based on the conversion of phage M13 single-stranded viral DNA bearing a model mutagenic lesion to the double-stranded replicative form. Amplification of the newly synthesized strand followed by multiplex DNA sequence anal. revealed that mutation fixation at 3,N4-ethenocytosine (εC) was ≈3% when the DNA was replicated by normal cell extracts, ≈48% when replicated by mutA cell extracts and ≈3% when replicated by mutA recA double mutant cell extracts, in complete agreement with previous in vivo results. Mutagenesis at undamaged DNA sites was significantly elevated by mutA cell-free extracts in the M13 lacZ(α) forward mutagenesis system. Neither polA (DNA polymerase I) nor polB (DNA polymerase II) genes are required for the mutA phenotype, suggesting that the phenotype is mediated through a modification of DNA polymerase III or the activation of a previously unidentified DNA polymerase. These findings define the major features of a novel mutagenic pathway and imply the existence of previously unrecognized links between translation, recombination and replication. 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 trna mutation reca dependent dna replication error escherichia, Biochemical Genetics: Genomic Processes and other aspects.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Barrio, Jorge R.; Sattsangi, Prem D.; Gruber, Bruce A.; Dammann, Laurence G.; Leonard, Nelson J. published an article in 1976, the title of the article was Species responsible for the fluorescence of 3,N4-ethenocytidine.Recommanded Product: 55662-66-3 And the article contains the following content:

The fluorescence properties of 3,N4-ethenocytidine (ε-cytidine) (I), substituted derivatives, and closely related 2-ring heterocycles were examined The chloroacetaldehyde-modified cytidine is fluorescent only in its protonated form. The fluorescence emission maximum is 340 nm and the pKa* is 4.0, very close to the value for the ground state. N-1-alkylation of I at the same position as protonation makes reversion to the nonfluorescent type of structure impossible, on changing the pH, and accordingly the fluorescence emission characteristics are preserved over a wide range of pH. The presence of the n→π* transition of the carbonyl group in I is responsible for the lack of fluorescence in neutral solution Even I.HCl has a low fluorescence quantum yield (Φ < 0.01) and a short fluorescence lifetime (τ = 30 psec). Ring substitution produces a red shift of the π → π* transition, due to inductive or mesomeric effects and a clear improvement in the fluorescence emission characteristics; e.g., 2-acetylamino-5,6-dihydro-5-oxo-6-β-D-ribofuranosylimidazo[1,2-c]pyrimidine, in its protonated form, shows Φ = 0.85 and τ = 4 ns. Imidazo[1,2-a]pyridine, a close model for I lacking the carbonyl group and accordingly the n → π* transition, has a high fluorescence quantum yield and long lifetime in either neutral solution or organic solvents. Both N-1-protonated and -alkylated imidazo[1,2-a]pyridines have emission maxima similar to those observed for I.HCl but higher quantum yields. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Recommanded Product: 55662-66-3

The Article related to fluorescence etherocytidine, cytidine etheno fluorescence, Carbohydrates: Nucleosides, Nucleotides and other aspects.Recommanded Product: 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On December 2, 2004, Jurado, Juan; Maciejewska, Agnieszka; Krwawicz, Joanna; Laval, Jacques; Saparbaev, Murat K. published an article.Safety of Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was Role of mismatch-specific uracil-DNA glycosylase in repair of 3,N4-ethenocytosine in vivo. And the article contained the following:

The 3,N4-ethenocytosine (εC) residue might have biol. role in vivo since it is recognized and efficiently excised in vitro by the E. coli mismatch-specific uracil-DNA glycosylase (MUG) and the human thymine-DNA glycosylase (hTDG). In the present work we have generated mug defective mutant of E. coli by insertion of a kanamycin cassette to assess the role of MUG in vivo. We show that human TDG complements the enzymic activity of MUG when expressed in a mug mutant. The εC-DNA glycosylase defective strain did not exhibit spontaneous mutator phenotype and did not show unusual sensitivity to any of the following DNA damaging treatments: methylmethanesulfonate, N-methyl-N’-nitro-N-nitrosoguanidine, UV light, H2O2, paraquat. However, plasmid DNA damaged by 2-chloroacetaldehyde treatment in vitro was inactivated at a greater rate in a mug mutant than in wild-type host, suggesting that MUG is required for the in vivo processing of the ethenobases. In addition, 2-chloroacetaldehyde treatment induces preferentially G·C → C·G and A·T → T·A transversions in mug mutant. Comparison of the mutation frequencies induced by the site-specifically incorporated εC residue in E. coli wild-type vs. mug indicates that MUG repairs more than 80% of εC residues in vivo. Furthermore, the results show that nucleotide excision repair and recombination are not involved in the processing of εC in E. coli. Based on the mutagenesis data we suggest that εC may be less toxic and less mutagenic than expected. The increased spontaneous mutation rate for G·C → A·T transition in the ung mug double mutant as compared to the single ung mutant suggest that MUG may be a back-up repair enzyme to the classic uracil-DNA glycosylase. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Safety of Imidazo[1,2-c]pyrimidin-5(6H)-one

The Article related to uracil dna glycosylase repair ethenocytosine escherichia, Biochemical Genetics: Genomic Processes and other aspects.Safety of Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On March 31, 1999, Rahman, M. Sayeedur; Humayun, M. Zafri published an article.Formula: C6H5N3O The title of the article was SOS and UVM pathways have lesion-specific additive and competing effects on mutation fixation at replication-blocking DNA lesions. And the article contained the following:

Escherichia coli cells have multiple mutagenic pathways that are induced in response to environmental and physiol. stimuli. Unlike the well-investigated classical SOS response, little is known about newly recognized pathways such as the UVM (UV modulation of mutagenesis) response. In this study, we compared the contributions of the SOS and UVM pathways on mutation fixation at two representative noninstructive DNA lesions: 3,N4-ethenocytosine (εC) and abasic (AP) sites. Because both SOS and UVM responses are induced by DNA damage, and defined UVM-defective E. coli strains are not yet available, we first constructed strains in which expression of the SOS mutagenesis proteins UmuD’ and UmuC (and also RecA in some cases) is uncoupled from DNA damage by being placed under the control of a heterologous lac-derived promoter. M13 single-stranded viral DNA bearing site-specific lesions was transfected into cells induced for the SOS or UVM pathway. Survival effects were determined from transfection efficiency, and mutation fixation at the lesion was analyzed by a quant. multiplex sequence anal. procedure. Our results suggest that induction of the SOS pathway can independently elevate mutagenesis at both lesions, whereas the UVM pathway significantly elevates mutagenesis at εC in an SOS-independent fashion and at AP sites in an SOS-dependent fashion. Although mutagenesis at εC appears to be elevated by the induction of either the SOS or the UVM pathway, the mutational specificity profiles for εC under SOS and UVM pathways are distinct. Interestingly, when both pathways are active, the UVM effect appears to predominate over the SOS effect on mutagenesis at εC, but the total mutation frequency is significantly increased over that observed when each pathway is individually induced. These observations suggest that the UVM response affects mutagenesis not only at class 2 noninstructive lesions (εC) but also at classical SOS-dependent (class 1) lesions such as AP sites. Our results add new layers of complexity to inducible mutagenic phenomena: DNA damage activates multiple pathways that have lesion-specific additive as well as suppressive effects on mutation fixation, and some of these pathways are not directly regulated by the SOS genetic network. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Formula: C6H5N3O

The Article related to sos uvm response dna repair mutagenesis, Biochemical Genetics: Genomic Processes and other aspects.Formula: C6H5N3O

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Li, Deyu; Delaney, James C.; Page, Charlotte M.; Chen, Alvin S.; Wong, Cintyu; Drennan, Catherine L.; Essigmann, John M. published an article in 2010, the title of the article was Repair of DNA alkylation damage by the Escherichia coli adaptive response protein AlkB as studied by ESI-TOF mass spectrometry.HPLC of Formula: 55662-66-3 And the article contains the following content:

DNA alkylation can cause mutations, epigenetic changes, and even cell death. All living organisms have evolved enzymic and non-enzymic strategies for repairing such alkylation damage. AlkB, one of the Escherichia coli adaptive response proteins, uses an α-ketoglutarate/Fe(II)-dependent mechanism that, by chem. oxidation, removes a variety of alkyl lesions from DNA, thus affording protection of the genome against alkylation. In an effort to understand the range of acceptable substrates for AlkB, the enzyme was incubated with chem. synthesized oligonucleotides containing alkyl lesions, and the reaction products were analyzed by electrospray ionization time-of-flight (ESI-TOF) mass spectrometry. Consistent with the literature, but studied comparatively here for the first time, it was found that 1-methyladenine, 1,N6-ethenoadenine, 3-methylcytosine, and 3-ethylcytosine were completely transformed by AlkB, while 1-methylguanine and 3-methylthymine were partially repaired. The repair intermediates (epoxide and possibly glycol) of 3,N4-ethenocytosine are reported for the first time. It is also demonstrated that O6-methylguanine and 5-methylcytosine are refractory to AlkB, lending support to the hypothesis that AlkB repairs only alkyl lesions attached to the nitrogen atoms of the nucleobase. ESI-TOF mass spectrometry is shown to be a sensitive and efficient tool for probing the comparative substrate specificities of DNA repair proteins in vitro. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).HPLC of Formula: 55662-66-3

The Article related to dna alkylation repair escherichia alkb, Biochemical Genetics: Genomic Processes and other aspects.HPLC of Formula: 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Bartholomew, David G.; Dea, Phoebe; Robins, Roland K.; Revankar, Ganapathi R. published an article in 1975, the title of the article was Imidazo[1,2-c]pyrimidine nucleosides. Synthesis of N-bridgehead inosine monophosphate and guanosine monophosphate analogs related to 3-deazapurines.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one And the article contains the following content:

Cyclization of 4-amino-6-chloro-2-pyrimidinol with BrCH2CH(OEt)2 gave 7-chloroimidazo[1,2-c]pyrimidin-5-one (I). Direct glycosylation of the trimethylsilyl derivative of I with 2,3,5-tri-O-acetyl-D-ribofuranosyl bromide in MeCN gave an anomeric mixture of 7-chloro-1-(2,3,5-tri-O-acetyl-D-ribofuranosyl)imidazo[1,2-c]pyrimidin-5-one, which on deacetylation and separation of anomers furnished 7-chloro-1-β-D-ribofuranosylimidazo[1,2-c]pyrimidin-5-one (II) and its α anomer (III). However, the glycosylation of trimethylsilylated I with tetra-O-acetyl-β-D-ribofuranose in dichloroethane containing SnCl4, followed by aminolysis gave only II. Catalytic dehalogenation of II and III gave 1-β-D-ribofuranosylimidazo[1,2-c]pyrimidin-5-one (IV) and its α anomer (V), resp. Amination of II gave 7-amino-1-β-D-ribofuranosylimidazo[1,2-c]pyrimidin-5-one (VI). Phosphorylation of IV, V, and VI gave 1-β-D-ribofuranosylimidazo[1,2-c]pyrimidin-5-one 5′-monophosphate, the IMP analog α anomer and 7-amino-1-β-D-ribofuranosylimidazo[1,2-c]pyrimidin-5-one 5′-monophosphate, resp. The ribosylation site was determined by using 13C NMR and the anomeric configurations were established by using PMR of the 2′,3′-O-isopropylidene derivatives of II and III. 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 imidazopyrimidine nucleoside analog, Carbohydrates: Nucleosides, Nucleotides and other aspects.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On September 1, 2001, Privezentzev, C. V.; Saparbaev, M.; Laval, J. published an article.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was The HAP1 protein stimulates the turnover of human mismatch-specific thymine-DNA-glycosylase to process 3,N4-ethenocytosine residues. And the article contained the following:

When present in DNA, 3,N4-ethenocytosine (εC) residues are potentially mutagenic and carcinogenic in vivo. The enzymic activity responsible for the repair of the εC residues in human cells is the hTDG protein, the human thymine-DNA-glycosylase that removes thymine in a T/G base pair [Proc. Natl. Acad. Sci., U.S.A., 95 (1998) 8508]. One of the distinctive properties of the hTDG protein is that it remains tightly bound to the AP-site resulting from its glycosylase activity. In this paper we report that the human AP endonuclease, the HAP1 (Ape1, APEX Ref-1) protein, stimulates the processing of εC residues by the hTDG protein in vitro, in a dose-dependent manner. This property of HAP1 protein is specific since E.coli Fpg, Nfo and Nth proteins, all endowed with an AP nicking activity, do not show similar features. The results suggest that the HAP1 protein displaces the hTDG protein bound to the AP-site and therefore increases the turnover of the hTDG protein. However, using a variety of techniques including gel retardation assay, surface plasmon resonance and two-hybrid system, it was not possible to detect evidence for a complex including the substrate, the hTDG and HAP1 proteins. 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 hap1 ap endonuclease ethenocytosine dna excision repair, thymine dna glycosylase ref1 endonuclease ethenocytosine mutagen, Mammalian Biochemistry: Metabolism and other aspects.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On August 5, 1997, Wang, Ge; Rahman, M. Sayeedur; Humayun, M. Zafri published an article.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was Replication of M13 Single-Stranded Viral DNA Bearing Single Site-Specific Adducts by Escherichia coli Cell Extracts: Differential Efficiency of Translesion DNA Synthesis for SOS-Dependent and SOS-Independent Lesions. And the article contained the following:

To characterize mutagenic translesion DNA synthesis in UVM-induced Escherichia coli, we have developed a high-resolution DNA replication system based on E. coli cell extracts and M13 genomic DNA templates bearing mutagenic lesions. The assay is based on the conversion of M13 viral single-stranded DNA (ssDNA) bearing a single site-specific DNA lesion to the double-stranded replicative form (RF) DNA, and permits one to quant. measure the efficiency of translesion synthesis. DNA replication is most strongly inhibited by an abasic site, a classic SOS-dependent noninstructive lesion. In contrast, the efficiency of translesion synthesis across SOS-independent lesions such as O6-methylguanine and DNA uracil is around 90%, very close to the values obtained for control DNA templates. The efficiency of translesion synthesis across 3,N4-ethenocytosine and 1,N6-ethenoadenine is around 20%, a value that is similar to the in vivo efficiency deduced from the effect of the lesions on the survival of transfected M13 ssDNA. Neither DNA polymerase I nor polymerase II appears to be required for the observed translesion DNA synthesis because essentially similar results are obtained with extracts from polA- or polB-defective cells. The close parallels in the efficiency of translesion DNA synthesis in vitro and in vivo for the five site-specific lesions included in this study suggest that the assay may be suitable for modeling mutagenesis in an accessible in vitro environment. 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 replication system development escherichia, Biochemical Methods: Immunological and other aspects.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Maggiali, C. A.; Mingiardi, M. R.; Morini, G.; Ronchini, F.; Mossini, F. published an article in 1982, the title of the article was Biological properties of imidazopyrimidines.COA of Formula: C6H5N3O And the article contains the following content:

Fifteen imidazo[1,2-a]pyrimidine derivatives I (R = OH, Cl, alkylamino, etc.; R1 = H or Cl) and 7 imidazo[1,2-c]pyrimidine derivatives II (R and R1 = as above) were prepared and tested for herbicidal activity against Sorghum vulgare, Hordeum hexastichum, and Pisum sativum. II (R = R1 = Cl) [85989-61-3] was the most active. I (R = R1 = Cl) [57473-32-2] was very active against S. vulgare and H. hexastichum, and moderately phytotoxic to P. sativum. Structure-activity relations are discussed. 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 imidazopyrimidine herbicide, Agrochemical Bioregulators: Plant and other aspects.COA of Formula: C6H5N3O

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Ajani, Haresh; Jansa, Josef; Kopruluoglu, Cemal; Hobza, Pavel; Krystof, Vladimir; Lycka, Antonin; Lepsik, Martin published an article in 2018, the title of the article was Imidazo[1,2-c]pyrimidin-5(6H)-one as a novel core of cyclin-dependent kinase 2 inhibitors: Synthesis, activity measurement, docking, and quantum mechanical scoring.Related Products of 55662-66-3 And the article contains the following content:

We report on the synthesis, activity testing, docking, and quantum mech. scoring of novel imidazo[1,2-c]pyrimidin-5(6H)-one scaffold for cyclin-dependent kinase 2 (CDK2) inhibition. A series of 26 compounds substituted with aromatic moieties at position 8 has been tested in in vitro enzyme assays and shown to inhibit CDK2. 2D structure-activity relationships have ascertained that small substituents at position 8 (up to the size of naphtyl or methoxyphenyl) generally lead to single-digit micromolar IC50 values, whereas bigger substituents (substituted biphenyls) decreased the compounds’ activities. The binding modes of the compounds obtained using Glide docking have exhibited up to 2 hinge-region hydrogen bonds to CDK2 and differed in the orientation of the inhibitor core and the placement of the 8-substituents. Semiempirical quantum mechanics-based scoring identified probable favorable binding modes, which will serve for future structure-based design and synthetic optimization of substituents of the heterocyclic core. In summary, we have identified a novel core for CDK2 inhibition and will explore it further to increase the potencies of the compounds and also monitor selectivities against other protein kinases. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Related Products of 55662-66-3

The Article related to cyclin dependent kinase 2 quantum mech scoring, binding mode, physics-based scoring, protein-ligand binding, Pharmacology: Structure-Activity and other aspects.Related Products of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem