Month: November 2022

On July 31, 2014, Stine, Jessica M.; Michau, Tammy M.; Williams, Megan K.; Kuebelbeck, Karen Leann; Stengard, Michele E. published an article.SDS of cas: 65896-14-2 The title of the article was The effects of intravenous romifidine on intraocular pressure in clinically normal horses and horses with incidental ophthalmic findings. And the article contained the following:

Design : Original study. Objective : To evaluate the effect of sedation with romifidine hydrochloride 1% (Sedivet: Boehringer-Ingelheim) on intraocular pressure (IOP) in the normal horse and horses with incidental ophthalmic findings as measured by applanation tonometry. Animals : Nineteen clin. normal horses (13 geldings, six mares) and eight horses (three geldings, five mares) with incidental ophthalmic findings were included in this study. Procedures : All horses underwent complete ophthalmic examination with pharmacol. mydriasis a min. of 2 wk prior to IOP evaluation. Baseline intraocular pressure values were obtained following auriculopalpebral nerve block and topical anesthetic. Immediately thereafter, romifidine was administered i.v. (75 μg/kg) and the IOP recorded at 5, 15, 30, 45 and 60 min postsedation in both eyes. Five successive readings were obtained at each time point, the low and high value discarded, and three remaining readings averaged for a mean. Results : The changes with time were consistent between eyes and OD and OS results were pooled. The mean IOP at baseline was 26.35 ± 5.57 mmHg. Mean IOP values were significantly lower than baseline at 5 (P < 0.0001), 15 (P < 0.0001), 30 (P = 0.0003), 45 (P < 0.0001) and 60 (P = 0.0005) minutes. The largest change from baseline (16.7%) was noted at t = 15 min. Conclusions and clin. relevance : Administration of romifidine significantly decreased the IOP from baseline at all time points measured. The greatest decline in IOP was noted at 15 min postsedation. Results are consistent with other studies noting a decline in IOP with administration of α-2 agonists. The experimental process involved the reaction of N-(2-Bromo-6-fluorophenyl)-4,5-dihydro-1H-imidazol-2-amine hydrochloride(cas: 65896-14-2).SDS of cas: 65896-14-2

The Article related to sedivet alpha2 agonist intravenous drug delivery intraocular pressure horse, alpha-2 agonist, equine, intraocular pressure, romifidine, sedation, tonometry, Pharmacology: Other (All Agents and Effects Not Otherwise Assignable) and other aspects.SDS of cas: 65896-14-2

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Saparbaev, M.; Laval, J. published an article in 1999, the title of the article was Enzymology of the repair of etheno adducts in mammalian cells and in Escherichia coli.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one And the article contains the following content:

Exocyclic adducts are generated in cellular DNA by reaction with epoxides that are formed metabolically from various industrial pollutants and by reaction with activated aldehydes that arise during membrane lipid peroxidation The etheno (ε) derivatives of purine and pyrimidine bases, e.g. 3,N4-ethenocytosine, 1,N6-ethenoadenine, N2,3-ethenoguanine and 1,N2-ethenoguanine, are probably involved in carcinogenesis because they are highly mutagenic and genotoxic. Therefore, the repair processes that eliminate exocyclic adducts from DNA should play a crucial role in maintaining the stability of the genetic information. The DNA glycosylases implicated in the repair of etheno adducts have been identified. Human and Escherichia coli 3-methyladenine-DNA-glycosylases excise 1,N6-ethenoadenine residues. We have identified two homologous proteins present in human cells and E. coli that remove 3,N4-ethenocytosine residues by DNA glycosylase activity. The human enzyme is an activity of the mismatch-specific thymine-DNA glycosylase, while the bacterial enzyme is an activity of the double-stranded uracil-DNA glycosylase, i.e., the homolog of the human enzyme. The fact that 1,N6-ethenoadenine and 3,N4-ethenocytosine are recognized and efficiently excised by DNA glycosylases in vitro suggests that these enzymes may be responsible for the repair of these mutagenic lesions in vivo and may contribute importantly to genetic stability. 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 dna glycosylase etheno adduct repair, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Application In Synthesis of Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Li, Zutan; Jiang, Hangjin; Kong, Lingpeng; Chen, Yuanyuan; Lang, Kun; Fan, Xiaodan; Zhang, Liangyun; Cong, Pian published an article in 2021, the title of the article was Deep6mA: A deep learning framework for exploring similar patterns in DNA N6-methyladenine sites across different species.Recommanded Product: 443-72-1 And the article contains the following content:

N6-methyladenine (6mA) is an important DNA modification form associated with a wide range of biol. processes. Identifying accurately 6mA sites on a genomic scale is crucial for under-standing of 6mA’s biol. functions. However, the existing exptl. techniques for detecting 6mA sites are cost-ineffective, which implies the great need of developing new computational methods for this problem. In this paper, we developed, without requiring any prior knowledge of 6mA and manually crafted sequence features, a deep learning framework named Deep6mA to identify DNA 6mA sites, and its performance is superior to other DNA 6mA prediction tools. Specifically, the 5-fold cross-validation on a benchmark dataset of rice gives the sensitivity and specificity of Deep6mA as 92.96% and 95.06%, resp., and the overall prediction accuracy is 94%. Importantly, we find that the sequences with 6mA sites share similar patterns across different species. The model trained with rice data predicts well the 6mA sites of other three species: Arabidopsis thaliana, Fragaria vesca and Rosa chinensis with a prediction accuracy over 90%. In addition, we find that (1) 6mA tends to occur at GAGG motifs, which means the sequence near the 6mA site may be conservative; (2) 6mA is enriched in the TATA box of the promoter, which may be the main source of its regulating downstream gene expression. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Recommanded Product: 443-72-1

The Article related to arabidopsis fragaria rosa n6 methyladenine dna, Plant Biochemistry: Photosynthesis (Algae, Bacteria, and Green Plants) and other aspects.Recommanded Product: 443-72-1

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On December 31, 2012, Prorok, Paulina; Saint-Pierre, Christine; Gasparutto, Didier; Fedorova, Olga S.; Ishchenko, Alexander A.; Leh, Herve; Buckle, Malcolm; Tudek, Barbara; Saparbaev, Murat published an article.Formula: C6H5N3O The title of the article was Highly mutagenic exocyclic DNA adducts are substrates for the human nucleotide incision repair pathway. And the article contained the following:

Background: Oxygen free radicals induce lipid peroxidation (LPO) that damages and breaks polyunsaturated fatty acids in cell membranes. LPO-derived aldehydes and hydroxyalkenals react with DNA leading to the formation of etheno(ε)-bases including 1,N6-ethenoadenine (εA) and 3,N4-ethenocytosine (εC). The εA and εC residues are highly mutagenic in mammalian cells and eliminated in the base excision repair (BER) pathway and/or by AlkB family proteins in the direct damage reversal process. BER initiated by DNA glycosylases is thought to be the major pathway for the removal of non-bulky endogenous base damage. Alternatively, in the nucleotide incision repair (NIR) pathway, the apurinic/apyrimidinic (AP) endonucleases can directly incise DNA duplex 5′ to a damaged base in a DNA glycosylase-independent manner. Methodol./Principal Findings: Here we have characterized the substrate specificity of human major AP endonuclease 1, APE1, towards εA, εC, thymine glycol (Tg) and 7,8-dihydro-8-oxoguanine (8oxoG) residues when present in duplex DNA. APE1 cleaves oligonucleotide duplexes containing εA, εC and Tg, but not those containing 8oxoG. Activity depends strongly on sequence context. The apparent kinetic parameters of the reactions suggest that APE1 has a high affinity for DNA containing ε-bases but cleaves DNA duplexes at an extremely slow rate. Consistent with this observation, oligonucleotide duplexes containing an ε-base strongly inhibit AP site nicking activity of APE1 with IC50 values in the range of 5-10 nM. MALDI-TOF MS anal. of the reaction products demonstrated that APE1-catalyzed cleavage of εA·T and εC·G duplexes generates, as expected, DNA fragments containing 5′-terminal ε-base residue. Conclusions/Significance: The fact that ε-bases and Tg in duplex DNA are recognized and cleaved by APE1 in vitro, suggests that NIR may act as a backup pathway to BER to remove a large variety of genotoxic base lesions in human cells. 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 ape1 dna adduct nucleotide incision repair pathway, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Formula: C6H5N3O

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On March 31, 2020, Tsukamoto, Yumiko; Tamura, Toshiki; Maeda, Yumi; Miyake, Kensuke; Ato, Manabu published an article.Application In Synthesis of N-Methyl-7H-purin-6-amine The title of the article was N6-methylated adenine on the target sites of mamA from Mycobacterium bovis BCG enhances macrophage activation by CpG DNA in mice. And the article contained the following:

CpG motifs in DNA sequences are recognized by Toll-like receptor 9 and activate immune cells. Bacterial genomic DNA (gDNA) has modified cytosine bases (5-methylcytosine [5 mC]) and modified adenine bases (6-methyladenine [6 mA]). 5 mC inhibits immune activation by CpG DNA; however, it is unclear whether 6 mA inhibits immune activation by CpG DNA. Mycobacterium bovis BCG (BCG) has three adenine methyltransferases (MTases) that act on specific target sequences. In this study, we examined whether the 6 mA at the target sites of adenine MTases affected the immunostimulatory activity of CpG DNA. Our results showed that only 6 mA located at the target sequence of mamA, an adenine MTase from BCG, enhanced interleukin (IL)-12p40 production from murine bone marrow-derived macrophages (BMDMs) stimulated with CpG DNA. Enhancement of IL-12p40 production in BMDMs was also observed when BMDMs were stimulated with CpG DNA ligated to oligodeoxynucleotides (ODNs) harboring 6 mA. Accordingly, we then evaluated whether gDNA from adenine MTase-deficient BCG was less efficient with regard to stimulation of BMDMs. Indeed, gDNA from a mamA-deficient BCG had less ability to activate BMDMs than that from wild-type BCG. We concluded from these results that adenine methylation on ODNs and bacterial gDNA may enhance immune activity induced by CpG DNA. 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 mycobacterium cpg dna adenine methylation macrophage, Immunochemistry: Other (Immunity, Immune Suppression, Tolerance, etc.) and other aspects.Application In Synthesis of N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Maciejewska, Agnieszka M.; Poznanski, Jaroslaw; Kaczmarska, Zuzanna; Krowisz, Beata; Nieminuszczy, Jadwiga; Polkowska-Nowakowska, Agnieszka; Grzesiuk, Elzbieta; Kusmierek, Jaroslaw T. published an article in 2013, the title of the article was AlkB Dioxygenase Preferentially Repairs Protonated Substrates.Synthetic Route of 55662-66-3 And the article contains the following content:

Efficient repair by Escherichia coli AlkB dioxygenase of exocyclic DNA adducts 3,N4-ethenocytosine, 1,N6-ethenoadenine, 3,N4-α-hydroxyethanocytosine, and reported here for the first time 3,N4-α-hydroxypropanocytosine, requires higher Fe(II) concentration than the reference 3-methylcytosine. The pH optimum for the repair follows the order of pKa values for protonation of the adduct, suggesting that pos. charged substrates favorably interact with the neg. charged carboxylic group of Asp-135 side chain in the enzyme active center. This interaction is supported by mol. modeling, indicating that 1,N6-ethenoadenine and 3,N4-ethenocytosine are bound to AlkB more favorably in their protonated cationic forms. An anal. of the pattern of intermol. interactions that stabilize the location of the ligand points to a role of Asp-135 in recognition of the adduct in its protonated form. Moreover, ab initio calculations also underline the role of substrate protonation in lowering the free energy barrier of the transition state of epoxidation of the etheno adducts studied. The observed time courses of repair of mixtures of stereoisomers of 3,N4-α-hydroxyethanocytosine or 3,N4-α-hydroxypropanocytosine are unequivocally two-exponential curves, indicating that the resp. isomers are repaired by AlkB with different efficiencies. Mol. modeling of these adducts bound by AlkB allowed evaluation of the participation of their possible conformational states in the enzymic reaction. 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 alkb dioxygenase recognition exocyclic dna adduct protonation, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Synthetic Route of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On October 5, 2004, Guliaev, Anton B.; Singer, B.; Hang, Bo published an article.SDS of cas: 55662-66-3 The title of the article was Chloroethylnitrosourea-derived ethano cytosine and adenine adducts are substrates for Escherichia coli glycosylases excising analogous etheno adducts. And the article contained the following:

Exocyclic ethano DNA adducts are saturated etheno ring derivatives formed mainly by therapeutic chloroethylnitrosoureas (CNUs), which are also mutagenic and carcinogenic. In this work, we report that two of the ethano adducts, 3,N4-ethanocytosine (EC) and 1,N6-ethanoadenine (EA), are novel substrates for the Escherichia coli mismatch-specific uracil-DNA glycosylase (Mug) and 3-methyladenine DNA glycosylase II (AlkA), resp. It has been shown previously that Mug excises 3,N4-ethenocytosine (εC) and AlkA releases 1,N6-ethenoadenine (εA). Using synthetic oligonucleotides containing a single ethano or etheno adduct, we found that both glycosylases had a ∼20-fold lower excision activity toward EC or EA than that toward their structurally analogous εC or εA adduct. Both enzymes were capable of excising the ethano base paired with any of the four natural bases, but with varying efficiencies. The Mug activity toward EC could be stimulated by E. coli endonuclease IV and, more efficiently, by exonuclease III. Mol. dynamics (MD) simulations showed similar structural features of the etheno and ethano derivatives when present in DNA duplexes. However, also as shown by MD, the stacking interaction between the EC base and Phe 30 in the Mug active site is reduced as compared to the εC base, which could account for the lower EC activity observed in this study. 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 dna repair methyladenine uracil dna glycosylase ethanocytosine ethanoadenine, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.SDS of cas: 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Borys-Brzywczy, Ewa; Arczewska, Katarzyna D.; Saparbaev, Murat; Hardeland, Ulrike; Schaer, Primo; Kusmierek, Jaroslaw T. published an article in 2005, the title of the article was Mismatch dependent uracil/thymine-DNA glycosylases excise exocyclic hydroxyethano and hydroxypropano cytosine adducts.HPLC of Formula: 55662-66-3 And the article contains the following content:

Exocyclic adducts of DNA bases, such as etheno- and hydroxyalkano- ones, are generated by a variety of bifunctional agents, including endogenously formed products of lipid peroxidation In this work we selectively modified cytosines in the 5′-d(TTT TTT CTT TTT CTT TTT CTT TTT T)-3′ oligonucleotide using: chloroacetaldehyde to obtain 3,N4-α-hydroxyethano- (HEC) and 3,N4-etheno- (εC), acrolein to obtain. 3,N4-α-hydroxypropano- (HPC) and crotonaldehyde to obtain 3,N4-α-hydroxy-γ-methylpropano- (mHPC) adducts of cytosine. The studied adducts are alkali-labile which results in oligonucleotide strain breaks at the sites of modification upon strong base treatment. The oligonucleotides carrying adducted cytosines were studied as substrates of Escherichia coli Mug, human TDG and fission yeast Thp1p glycosylases. All the adducts studied are excised by bacterial Mug although with various efficiency: εC > HEC > HPC > mHPC. The yeast enzyme excises efficiently εC ≥ HEC > HPC, whereas the human enzyme excises only εC. The pH-dependence curves of excision of εC, HEC and HPC by Mug are bell shaped and the most efficient excision of adducts occurs within the pH range of 8.6-9.6. The observed increase of excision of HEC and HPC above pH 7.2 can be explained by deprotonation of these adducts, which are high pKa compounds and exist in a protonated form at neutrality. On the other hand, since εC is in a neutral form in the pH range studied, we postulate an involvement of an addnl. catalytic factor. We hypothesize that the enzyme structure undergoes a pH-induced rearrangement allowing the participation of Lys68 of Mug in catalysis via a hydrogen bond interaction of its ε-amino group with N4 of the cytosine exocyclic adducts. 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 mismatch uracil thymine dna glycosylase hydroxyethano hydroxypropano cytosine, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.HPLC of Formula: 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On July 15, 2022, Zhu, Jun; Geng, Qiang; Liu, Yuan-Yang; Pan, Jiang; Yu, Hui Lei; Xu, Jian-He published an article.SDS of cas: 73590-85-9 The title of the article was Co-Cross-Linked Aggregates of Baeyer-Villiger Monooxygenases and Formate Dehydrogenase for Repeated Use in Asymmetric Biooxidation. And the article contained the following:

Baeyer-Villiger monooxygenases (BVMOs) are versatile biocatalysts, but their applications are hindered by their poor stability and cofactor dependence. In this study, cross-linked enzyme aggregate (CLEA) technol. was adopted to coimmobilize BVMO and its accessory cofactor-regeneration enzyme. Combi-CLEAs of a pyrmetazole monooxygenase from Acinetobacter calcoaceticus (AcPSMO) and a formate dehydrogenase from Burkholderia stabili (BstFDH) were prepared for the synthesis of (S)-omeprazole. After optimization, AcPSMO and BstFDH were coprecipitated with an activity ratio of 1:6 using ammonium sulfate and then cross-linked with glutaraldehyde (0.12% w/v). The activity recoveries of AcPSMO and BstFDH in the prepared combi-CLEAs were 43% and 38%, resp. Compared with the free enzymes AcPSMO and BstFDH, the thermostabilities of AcPSMO and BstFDH in combi-CLEAs were improved by 2.5- and 1.6-fold, resp. Both enzymes were more stable against alk. buffer after being immobilized. The combi-CLEAs could be reused for seven cycles in the biooxidative synthesis of (S)-omeprazole without significant activity loss, indicating the excellent operational stability and reusability in repeated reactions for the enzymic synthesis of (S)-omeprazole. Another two combi-CLEAs prepared under the same conditions, TmCHMO-BstFDH and RpBVMO-BstFDH, can be reused for at least 15 consecutive batches for the cyclohexanone mono-oxygenation reaction, which indicates the promising potential for coimmobilization of BVMOs and FDH with CLEA methodol. The experimental process involved the reaction of 5-Methoxy-2-[[(4-methoxy-3,5-dimethyl-2-pyridyl)methyl]thio]benzimidazole(cas: 73590-85-9).SDS of cas: 73590-85-9

The Article related to baeyer villiger monooxygenase formate dehydrogenase crosslinked aggregate asym biooxidation, Fermentation and Bioindustrial Chemistry: Methods (Including Analysis) and other aspects.SDS of cas: 73590-85-9

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On May 1, 2003, Hardeland, Ulrike; Bentele, Marc; Jiricny, Josef; Schaer, Primo published an article.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs. And the article contained the following:

Human thymine-DNA glycosylase (TDG) is well known to excise thymine and uracil from G·T and G·U mismatches, resp., and was therefore proposed to play a central role in the cellular defense against genetic mutation through spontaneous deamination of 5-methylcytosine and cytosine. In this study, we characterized two newly discovered orthologs of TDG, the Drosophila melanogaster Thd1p and the Schizosaccharomyces pombe Thp1p proteins, with an objective to address the function of this subfamily of uracil-DNA glycosylases from an evolutionary perspective. A systematic biochem. comparison of both enzymes with human TDG revealed a number of biol. significant facts. (i) All eukaryotic TDG orthologs have broad and species-specific substrate spectra that include a variety of damaged pyrimidine and purine bases; (ii) the common most efficiently processed substrates of all are uracil and 3,N4-ethenocytosine opposite guanine and 5-fluorouracil in any double-stranded DNA context; (iii) 5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes; (iv) none of the proteins is able to hydrolyze a non-damaged 5′-methylcytosine opposite G; and (v) the double strand and mismatch dependency of the enzymes varies with the substrate and is not a stringent feature of this subfamily of DNA glycosylases. These findings advance our current view on the role of TDG proteins and document that they have evolved with high structural flexibility to counter a broad range of DNA base damage in accordance with the specific needs of individual species. 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 uracil thymine dna glycosylase human drosophila fission yeast, schizosaccharomyces uracil dna glycosylase, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem