Tag: 100-200

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

On September 15, 2020, Kundu, Biswajit; Sarkar, Dipayan; Chowdhuri, Srijita Paul; Pal, Sourav; Das, Subhendu K.; Das, Benu Brata; Talukdar, Arindam published an article.Product Details of 5036-48-6 The title of the article was Development of a metabolically stable topoisomerase I poison as anticancer agent. And the article contained the following:

We have recently reported a new chemotype of a potent topoisomerase I poison with compound 1 as a potential anticancer chemotherapeutic agent. During further optimization, it has been observed that compound 1 suffers from high intrinsic clearance in human liver microsomes. To overcome the metabolic instability of compound 1, we report design and synthesis of metabolically stable Top1 poison 3. Newly identified Top1 poison 3 exhibits t1/2 of 69.1 min in human liver microsomes in comparison to compound 1 with t1/2 of 9.9 min. Mol. dynamic study of the newly optimized Top1 poison 3 was performed to get the insight into the stability of the binding pose in the active site. Compound 3 was able to trap DNA-Top1 cleavage complex and found to be less cytotoxic in non-cancerous cell line as compared to compound 1. The experimental process involved the reaction of N-(3-Aminopropyl)-imidazole(cas: 5036-48-6).Product Details of 5036-48-6

The Article related to preparation stable topoisomerase i inhibitor cancer, camptothecin, in vitro pharmacokinetics, metabolic stability, molecular dynamics, poison, topoisomerase 1, Pharmacology: Structure-Activity and other aspects.Product Details of 5036-48-6

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

On February 15, 2012, Khan, K. M.; Shah, Zarbad; Ahmad, V. U.; Ambreen, N.; Khan, M.; Taha, M.; Rahim, F.; Noreen, S.; Perveen, S.; Choudhary, M. I.; Voelter, W. published an article.Quality Control of 2-Nitro-1H-benzo[d]imidazole The title of the article was 6-Nitrobenzimidazole derivatives: Potential phosphodiesterase inhibitors: Synthesis and structure-activity relationship. And the article contained the following:

6-Nitrobenzimidazole derivatives (1-30) synthesized and their phosphodiesterase inhibitory activities determined Out of thirty tested compounds, ten showed a varying degrees of phosphodiesterase inhibition with IC50 values between 1.5 ± 0.043 and 294.0 ± 16.7 μM. Compounds 30 (IC50 = 1.5 ± 0.043 μM), 1 (IC50 = 2.4 ± 0.049 μM), 11 (IC50 = 5.7 ± 0.113 μM), 13 (IC50 = 6.4 ± 0.148 μM), 14 (IC50 = 10.5 ± 0.51 μM), 9 (IC50 = 11.49 ± 0.08 μM), 3 (IC50 = 63.1 ± 1.48 μM), 10 (IC50 = 120.0 ± 4.47 μM), and 6 (IC50 = 153.2 ± 5.6 μM) showed excellent phosphodiesterase inhibitory activity, much superior to the standard EDTA (IC50 = 274 ± 0.007 μM), and thus are potential mols. for the development of a new class of phosphodiesterase inhibitors. A structure-activity relationship is evaluated. All compounds are characterized by spectroscopic parameters. The experimental process involved the reaction of 2-Nitro-1H-benzo[d]imidazole(cas: 5709-67-1).Quality Control of 2-Nitro-1H-benzo[d]imidazole

The Article related to nitrobenzimidazole derivative preparation structure phosphodiesterase inhibitor, Pharmacology: Structure-Activity and other aspects.Quality Control of 2-Nitro-1H-benzo[d]imidazole

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Tawari, Nilesh; Lele, Arundhati; Khambete, Mihir; Degani, Mariam published an article in 2014, the title of the article was Mutagenicity prediction for nitroaromatic compounds using qstr modeling.Category: imidazoles-derivatives And the article contains the following content:

Objective: Nitroarom. compounds are important industrial chems. widely used in the synthesis of many diverse products including drugs, dyes, polymers, pesticides and explosives. However, the mutagenicity associated with nitroarom. compounds is a toxicol. feature which poses great concern. On the other hand, there are successful examples of non-mutagenic nitroarom. mols.; indicating that safer nitroarom. compounds can be developed. In this light the aim of the present work was to predict the mutagenicity of nitroarom. compounds using an atom based QSTR model. Methods: An atom based QSTR model was developed using PHASE. In addition, mols. were studied by complete geometry optimization using DFT at B3LYP/3-21G* level of theory. Results: An atom based QSTR model was generated for prediction of mutagenicity of the compounds Conclusion: The visualization of different properties highlighted key inferences. These include the likelihood of mutagenicity for the mols. with more fused planar hydrophobic rings having hydrogen bond acceptor and electron donating substitutions. Also, all highly mutagenic compounds have two or more neg. potential regions. Specific electronic properties such as HOMO and LUMO indicate that most of the mutagenic mols. are very reactive in nature. The results of this study would be useful as a predictive tool to screen out mutagenic nitroarenes and design safer non-mutagenic nitro compounds The experimental process involved the reaction of 2-Nitro-1H-benzo[d]imidazole(cas: 5709-67-1).Category: imidazoles-derivatives

The Article related to nitroarom compound mutagenicity quant structure toxicity relationship modeling, Pharmacology: Structure-Activity and other aspects.Category: imidazoles-derivatives

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Alriquet, Marion; Calloni, Giulia; Martinez-Limon, Adrian; Ponti, Riccardo Delli; Hanspach, Gerd; Hengesbach, Martin; Tartaglia, Gian G.; Vabulas, R. Martin published an article in 2020, the title of the article was The protective role of m1A during stress-induced granulation.Quality Control of N-Methyl-7H-purin-6-amine And the article contains the following content:

Post-transcriptional methylation of N6-adenine and N1-adenine can affect transcriptome turnover and translation. Furthermore, the regulatory function of N6-methyladenine (m6A) during heat shock has been uncovered, including the enhancement of the phase separation potential of RNAs. In response to acute stress, e.g. heat shock, the orderly sequestration of mRNAs in stress granules (SGs) is considered important to protect transcripts from the irreversible aggregation. Until recently, the role of N1-methyladenine (m1A) on mRNAs during acute stress response remains largely unknown. Here we show that the methyltransferase complex TRMT6/61A, which generates the m1A tag, is involved in transcriptome protection during heat shock. Our bioinformatics anal. indicates that occurrence of the m1A motif is increased in mRNAs known to be enriched in SGs. Accordingly, the m1A-generating methyltransferase TRMT6/61A accumulated in SGs and mass spectrometry confirmed enrichment of m1A in the SG RNAs. The insertion of a single methylation motif in the untranslated region of a reporter RNA leads to more efficient recovery of protein synthesis from that transcript after the return to normal temperature Our results demonstrate far-reaching functional consequences of a minimal RNA modification on N1-adenine during acute proteostasis stress. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Quality Control of N-Methyl-7H-purin-6-amine

The Article related to transcriptome n1 methyladenine protective role granulation, n1-methyladenine, stress granules, stress response, Mammalian Pathological Biochemistry: Other and other aspects.Quality Control of N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On August 31, 2012, Olipitz, Werner; Wiktor-Brown, Dominika; Shuga, Joe; Pang, Bo; McFaline, Jose; Lonkar, Pallavi; Thomas, Aline; Mutamba, James T.; Greenberger, Joel S.; Samson, Leona D.; Dedon, Peter C.; Yanch, Jacquelyn C.; Engelward, Bevin P. published an article.Formula: C6H5N3O The title of the article was Integrated molecular analysis indicates undetectable change in DNA damage in mice after continuous irradiation at ∼ 400-fold natural background radiation. And the article contained the following:

Background: In the event of a nuclear accident, people are exposed to elevated levels of continuous low dose-rate radiation. Nevertheless, most of the literature describes the biol. effects of acute radiation. Objectives: DNA damage and mutations are well established for their carcinogenic effects. We assessed several key markers of DNA damage and DNA damage responses in mice exposed to low dose-rate radiation to reveal potential genotoxic effects associated with low dose-rate radiation. Methods: We studied low dose-rate radiation using a variable low dose-rate irradiator consisting of flood phantoms filled with 125Iodine-containing buffer. Mice were exposed to 0.0002 cGy/min (∼400-fold background radiation) continuously over 5 wk. We assessed base lesions, micronuclei, homologous recombination (HR; using fluorescent yellow direct repeat mice), and transcript levels for several radiation-sensitive genes. Results: We did not observe any changes in the levels of the DNA nucleobase damage products hypoxanthine, 8-oxo-7,8-dihydroguanine, 1,N6-ethenoadenine, or 3,N4-ethenocytosine above background levels under low dose-rate conditions. The micronucleus assay revealed no evidence that low dose-rate radiation induced DNA fragmentation, and there was no evidence of double strand break-induced HR. Furthermore, low dose-rate radiation did not induce Cdkn1a, Gadd45a, Mdm2, Atm, or Dbd2. Importantly, the same total dose, when delivered acutely, induced micronuclei and transcriptional responses. Conclusions: These results demonstrate in an in vivo animal model that lowering the dose-rate suppresses the potentially deleterious impact of radiation and calls attention to the need for a deeper understanding of the biol. impact of low dose-rate radiation. 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 ionizing radiation background radioactivity dna damage, Radiation Biochemistry: Effects In Mammals and other aspects.Formula: C6H5N3O

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Li, Yang; Niu, Yimin; Zhu, Jianhua; Gao, Cuicui; Xu, Qunwei; He, Zhiyu; Chen, Dawei; Xu, Ming; Liu, Yang published an article in 2020, the title of the article was Tailor-made legumain/pH dual-responsive doxorubicin prodrug-embedded nanoparticles for efficient anticancer drug delivery and in situ monitoring of drug release.Safety of N-(3-Aminopropyl)-imidazole And the article contains the following content:

Legumain enzyme is a well-conserved lysosomal cysteine protease and is over-expressed in many tumor cells and tumor stromal cells and exhibits higher protease activity under acidic conditions, such as in lysosomes and endosomes. Legumain enzyme-triggered drug delivery systems have demonstrated potential therapeutic values in cancer targeted therapy. In tumor cells, DS-NA could disassemble rapidly in acidic environments, and then release doxorubicin through legumain digestion. Except as a drug vector, the drug release process from DS-NA could also be dynamically monitored by CLSM as the DOX was released from the surface of CDs through the AANL peptide linker digested by legumain, then transferred into the cell nucleus and exerted cytotoxicity, while the CDs themselves remained in the cytoplasm. As a control, the CDs-C9-DOX, which did not contain the AANL peptide linker, also still resided in the cytoplasm. Furthermore, in vivo studies show that DS-NA had a stronger inhibitory effect on tumor tissue with attenuated side effects to normal tissues than control nanoparticles or free drugs, which may be due to comprehensive effects including pH/legumain dual-triggered drug release, long blood circulation periods, and EPR effects. Together, a combination strategy of acid sensitivity and legumain enzyme sensitivity used for site-specific controlled release of drugs provides a novel method for enhanced and precise antitumor chemotherapy. The experimental process involved the reaction of N-(3-Aminopropyl)-imidazole(cas: 5036-48-6).Safety of N-(3-Aminopropyl)-imidazole

The Article related to ductal breast cancer legumain ph doxorubicin release nanoparticle anticancer, Pharmaceuticals: Pharmacognostic Products and other aspects.Safety of N-(3-Aminopropyl)-imidazole

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem