Tag: 100-200

On September 24, 2020, Kilic, Ahmet; Beyazsakal, Levent; Findik, Bahar Tuba; Incebay, Hilal published an article.Application In Synthesis of N-(3-Aminopropyl)-imidazole The title of the article was Synthesis and electrochemical investigation of chiral amine bis(phenolate)-boron complexes: In vitro antibacterial activity screening of boron compounds. And the article contained the following:

A new class of low-cost, easily-synthesizable and modifiable chiral amine bis(phenolate) ligand (L), its chiral boron complex (LB), and five different salen groups (1-(3-Aminopropyl) imidazole (LB1), N,N-Diethyl-p-phenylenediamine (LB2), 2-Picolylamine (LB3), 4′-Aminoacetophenone (LB4), and 4-Amino-2,2,6,6-tetramethyl piperidine (LB5)) containing chiral boron complexes were synthesized. These newly synthesized chiral compounds were fully characterized by 1H and 13C NMR, FTIR, UV-visible, and LC-MS/MS spectroscopy, m.p., elemental anal., and cyclic voltammetry techniques. The in vitro antibacterial activity of the synthesized different chiral boron complexes was tested against four pathogenic bacteria strains using the resazurin-based broth microdilution method, and the MIC values of each boron complex were determined Based on the overall results, the N, N-Diethyl-p-phenylenediamine group containing chiral boron complex (LB2) showed the highest activity against all bacterial strains, with the lowest MIC value of 4μg/mL which is nearly in the range of values for com. antibacterial drugs. The experimental process involved the reaction of N-(3-Aminopropyl)-imidazole(cas: 5036-48-6).Application In Synthesis of N-(3-Aminopropyl)-imidazole

The Article related to preparation boron chiral amine phenolate complex, cyclic voltammetry boron chiral amine phenolate complex, antimicrobial activity boron chiral amine phenolate complex, Inorganic Chemicals and Reactions: Coordination Compounds and other aspects.Application In Synthesis of N-(3-Aminopropyl)-imidazole

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On May 12, 2021, Wang, Qing; Tan, Kaiyue; Wang, Hong; Shang, Jinhua; Wan, Yeqing; Liu, Xiaoqing; Weng, Xiaocheng; Wang, Fuan published an article.Safety of N-Methyl-7H-purin-6-amine The title of the article was Orthogonal demethylase-activated deoxyribozyme for intracellular imaging and gene regulation. And the article contained the following:

The epigenetic modification of nucleic acids represents a versatile approach for achieving high-efficient control over gene expression and transcription and could dramatically expand their biosensing and therapeutic applications. Demethylase-involved removal of N6-methyladenine (m6A) represents one of the vital epigenetic reprogramming events, yet its direct intracellular evaluation and as-guided gene regulation are extremely rare. The endonuclease-mimicking deoxyribozyme (DNAzyme) is a catalytically active DNA that enables the site-specific cleavage of the RNA substrate, and several strategies have imparted the magnificent responsiveness to DNAzyme by using chem. and light stimuli. However, the epigenetic regulation of DNAzyme has remained largely unexplored, leaving a significant gap in responsive DNA nanotechnol. Herein, we reported an epigenetically responsive DNAzyme system through the in vitro selection of an exquisite m6A-caged DNAzyme that could be specifically activated by FTO (fat mass and obesity-associated protein) demethylation for precise intracellular imaging-directed gene regulation. Based on a systematic investigation, the active DNAzyme configuration was potently disrupted by the site-specific incorporation of m6A modification and subsequently restored into the intact DNAzyme structure via the tunable FTO-specific removal of m6A-caging groups under a variety of conditions. This orthogonal demethylase-activated DNAzyme amplifier enables the robust and accurate monitoring of FTO and its inhibitors in live cells. Moreover, the simple demethylase-activated DNAzyme facilitates the assembly of an intelligent self-adaptive gene regulation platform for knocking down demethylase with the ultimate apoptosis of tumor cells. As a straightforward and scarless m6A removal strategy, the demethylase-activated DNAzyme system offers a versatile toolbox for programmable gene regulation in synthetic biol. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Safety of N-Methyl-7H-purin-6-amine

The Article related to dnazyme rnase regulation n6 methyladenine cage demethylase fto protein, human cell demethylase activated dnazyme programmable gene regulation, Enzymes: Separation-Purification-General Characterization and other aspects.Safety of N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On February 28, 2021, Cao, Yue; Zhou, Xiaoying; Luan, Lindong; Zeng, Hongmei; Zou, Guohong; Lin, Zhien published an article.Quality Control of N-(3-Aminopropyl)-imidazole The title of the article was Organically templated metal phosphate-oxalates: Solvent-free synthesis, crystal structure, and proton conduction. And the article contained the following:

Two new metal phosphate-oxalates, namely, H2api·Mn2(H2PO4)2(C2O4)2 (1) and H2mpip·Sc(H2PO4)2(C2O4)·0.5C2O4·1.5H2O (2), were prepared under solvent-free conditions, where api = 1-(3-aminopropyl)imidazole and mpip = 1-methylpiperazine. Compound 1 has a honeycomb-like structure with 12-ring windows. Compound 2 has a one-dimensional structure with scandium phosphate ladders decorated with oxalate ligands. The proton-conducting behaviors of this compound under 95% relative humidity were investigated. The experimental process involved the reaction of N-(3-Aminopropyl)-imidazole(cas: 5036-48-6).Quality Control of N-(3-Aminopropyl)-imidazole

The Article related to manganese scandium phosphate oxalate preparation crystal mol structure proton, proton conduction metal manganese scandium phosphate oxalate, Inorganic Chemicals and Reactions: Coordination Compounds and other aspects.Quality Control of N-(3-Aminopropyl)-imidazole

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On March 31, 2022, Kohlgruber, Tsuyoshi A.; Perry, Samuel N.; Sigmon, Ginger E.; Oliver, Allen G.; Burns, Peter C. published an article.Application of 5036-48-6 The title of the article was Hydrogen bond network and bond valence analysis on uranyl sulfate compounds with organic-based interstitial cations. And the article contained the following:

Seven new uranyl sulfate compounds with organic charge-balancing cations were synthesized and structurally characterized. The structural unit topologies of the two chains and five sheets were previously reported in uranyl sulfate crystal chem., although they were synthesized using different organic mols. With the inclusion of six of these structures to the 48 previously published uranyl sulfate compounds, a total of 54 known uranyl sulfate compounds with organic charge-balancing cations were compiled and analyzed. A graphical approach was used to compare the structural unit topologies, and a bond valence approach was used to quantify the H bond networks that exist between the interstitial cationic and solvent species to the uranyl sulfate anionic structural units. This anal. helped elucidate which O atoms in the structural unit receive H bonds and how the organic cations stabilize the overall crystal structures in this subclass of U(VI) materials. The experimental process involved the reaction of N-(3-Aminopropyl)-imidazole(cas: 5036-48-6).Application of 5036-48-6

The Article related to uranyl sulfate anion preparation hydrogen bond network, crystal structure uranyl sulfate interstitial organic cation, Inorganic Chemicals and Reactions: Coordination Compounds and other aspects.Application of 5036-48-6

Referemce:
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

Fu, Dragony; Samson, Leona D. published an article in 2012, the title of the article was Direct repair of 3,N 4-ethenocytosine by the human ALKBH2 dioxygenase is blocked by the AAG/MPG glycosylase.Recommanded Product: 55662-66-3 And the article contains the following content:

Exocyclic ethenobases are highly mutagenic DNA lesions strongly implicated in inflammation and vinyl chloride-induced carcinogenesis. While the alkyladenine DNA glycosylase, AAG (or MPG), binds the etheno lesions 1,N 6-ethenoadenine (εA) and 3,N 4-ethenocytosine (εC) with high affinity, only εA can be excised to initiate base excision repair. Here, we discover that the human AlkB homolog 2 (ALKBH2) dioxygenase enzyme catalyzes direct reversal of εC lesions in both double- and single-stranded DNA with comparable efficiency to canonical ALKBH2 substrates. Notably, we find that in vitro, the non-enzymic binding of AAG to εC specifically blocks ALKBH2-catalyzed repair of εC but not that of methylated ALKBH2 substrates. These results identify human ALKBH2 as a repair enzyme for mutagenic εC lesions and highlight potential consequences for substrate-binding overlap between the base excision and direct reversal DNA repair pathways. 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 alkbh2 dioxygenase human dna repair ethenocytosine inhibition aag glycosylase, Enzymes: Separation-Purification-General Characterization and other aspects.Recommanded Product: 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On October 1, 2007, Srinath, Thiruneelakantan; Bharti, Sanjay Kumar; Varshney, Umesh published an article.Synthetic Route of 55662-66-3 The title of the article was Substrate specificities and functional characterization of a thermo-tolerant uracil DNA glycosylase (UdgB) from Mycobacterium tuberculosis. And the article contained the following:

Uracil DNA glycosylases (UDGs) excise uracil from DNA and initiate the base (uracil) excision repair pathway. Ung, a highly conserved protein, is the only UDG characterized so far in mycobacteria. Here, we show that Rv1259 from Mycobacterium tuberculosis codes for a double-stranded DNA (dsDNA) specific UDG (MtuUdgB). MtuUdgB is thermo-tolerant, contains Fe-S cluster and, in addition to uracil, it excises ethenocytosine and hypoxanthine from dsDNA. MtuUdgB is product inhibited by AP-site containing dsDNA but not by uracil. While MtuUdgB excises uracil present as a single-nucleotide bulge in dsDNA, it is insensitive to inhibition by dsDNA containing AP-site in the bulge. Interestingly, in the presence of cellular factors, the uracil excision activity of MtuUdgB is enhanced, and when introduced into E. coli (ung-), it rescues its mutator phenotype and prevents C to T mutations in DNA. Novel features of the mechanism of action of MtuUdgB and the physiol. significance of the family 5 UDG in mycobacteria have been discussed. 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 thermotolerant uracil dna glycosylase udgb mycobacterium, Enzymes: Separation-Purification-General Characterization and other aspects.Synthetic Route of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On November 30, 1996, Mueller, Michael; Hutchinson, Linda K.; Guengerich, F. Peter published an article.Category: imidazoles-derivatives The title of the article was Addition of Deoxyribose to Guanine and Modified DNA Bases by Lactobacillus helveticus trans-N-Deoxyribosylase. And the article contained the following:

The use of bacterial trans-N-deoxyribosylase was evaluated as an alternative method for deoxyribosylation in the synthesis of deoxyribonucleosides containing potentially mutagenic adducts. A crude enzyme preparation was isolated from Lactobacillus helveticus and compared to Escherichia coli purine nucleoside phosphorylase. Trans-N-deoxyribosylase was more regioselective than purine nucleoside phosphorylase in the deoxyribosylation of Gua at the N9 atom, as compared to N7, as demonstrated by NMR anal. of the product. 5,6,7,9-Tetrahydro-7-acetoxy-9-oxoimidazo[1,2-a]purine was efficiently deoxyribosylated by trans-N-deoxyribosylase but not at all by purine nucleoside phosphorylase. Other substrates for trans-N-deoxyribosylase were N2-(2-oxoethyl)Gua, pyrimido[1,2-a]purin-10(3H)-one, 1,N2-ε-Gua, N2,3-ε-Gua, 3,N4-ε-Cyt, 1,N6-ε-Ade, C8-methylGua, and C8-aminoGua, most of which gave the desired isomer (bond at the nitrogen corresponding to N9 in Gua) in good yield. Neither N7-alkylpurines nor C8-(arylamino)-substituted guanines were substrates. The approach offers a relatively convenient method of enzymic preparation of many carcinogen-DNA adducts at the nucleoside level, for either use as standards or incorporation into oligonucleotides. Trans-N-deoxyribosylase can also be used to remove deoxyribose from modified deoxyribonucleosides in the presence of excess Cyt. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Category: imidazoles-derivatives

The Article related to deoxyribose dna base preparation trans deoxyribosylase, Enzymes: Separation-Purification-General Characterization and other aspects.Category: imidazoles-derivatives

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On October 18, 2002, Kavli, Bodil; Sundheim, Ottar; Akbari, Mansour; Otterlei, Marit; Nilsen, Hilde; Skorpen, Frank; Aas, Per Arne; Hagen, Lars; Krokan, Hans E.; Slupphaug, Geir published an article.Product Details of 55662-66-3 The title of the article was hUNG2 Is the Major Repair Enzyme for Removal of Uracil from U:A Matches, U:G Mismatches, and U in Single-stranded DNA, with hSMUG1 as a Broad Specificity Backup. And the article contained the following:

HUNG2 and hSMUG1 are the only known glycosylases that may remove uracil from both double- and single-stranded DNA in nuclear chromatin, but their relative contribution to base excision repair remains elusive. The present study demonstrates that both enzymes are strongly stimulated by physiol. concentrations of Mg2+, at which the activity of hUNG2 is 2-3 orders of magnitude higher than of hSMUG1. Moreover, Mg2+ increases the preference of hUNG2 toward uracil in ssDNA nearly 40-fold. APE1 has a strong stimulatory effect on hSMUG1 against dsU, apparently because of enhanced dissociation of hSMUG1 from AP sites in dsDNA. HSMUG1 also has a broader substrate specificity than hUNG2, including 5-hydroxymethyluracil and 3,N4-ethenocytosine. HUNG2 is excluded from, whereas hSMUG1 accumulates in, nucleoli in living cells. In contrast, only hUNG2 accumulates in replication foci in the S-phase. HUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U:A and U:G in vitro. Moreover, an addnl. but delayed repair of the U:G plasmid is observed that is not inhibited by neutralizing antibodies against hUNG2 or hSMUG1. We propose a model in which hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork. We also provide evidence that hUNG2 is the major enzyme for removal of deaminated cytosine outside of replication foci, with hSMUG1 acting as a broad specificity backup. 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 uracil dna glycosylase ung2 base excision repair, Enzymes: Separation-Purification-General Characterization and other aspects.Product Details of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On November 10, 1998, Hang, B.; Medina, M.; Fraenkel-Conrat, H.; Singer, B. published an article.Application of 55662-66-3 The title of the article was A 55-kDa protein isolated from human cells shows DNA glycosylase activity toward 3,N4-ethenocytosine and the G/T mismatch. And the article contained the following:

Etheno adducts in DNA arise from multiple endogenous and exogenous sources. Of these adducts we have reported that, 1,N6-ethenoadenine (εA) and 3,N4-ethenocytosine (εC) are removed from DNA by two sep. DNA glycosylases. We later confirmed these results by using a gene knockout mouse lacking alkylpurine-DNA-N-glycosylase, which excises εA. The present work is directed toward identifying and purifying the human glycosylase activity releasing εC. HeLa cells were subjected to multiple steps of column chromatog., including two εC-DNA affinity columns, which resulted in >1,000-fold purification Isolation and renaturation of the protein from SDS/polyacrylamide gel showed that the εC activity resides in a 55-kDa polypeptide. This apparent mol. mass is approx. the same as reported for the human G/T mismatch thymine-DNA glycosylase. This latter activity copurified to the final column step and was present in the isolated protein band having εC-DNA glycosylase activity. In addition, oligonucleotides containing εC·G or G/T(U), could compete for εC protein binding, further indicating that the εC-DNA glycosylase is specific for both types of substrates in recognition. The same substrate specificity for εC also was observed in a recombinant G/T mismatch DNA glycosylase from the thermophilic bacterium, Methanobacterium thermoautotrophicum THF. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Application of 55662-66-3

The Article related to ethenocytosine dna glycosylase purification, Enzymes: Separation-Purification-General Characterization and other aspects.Application of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem