Category: imidazoles-derivatives

On June 30, 2015, Zdzalik, Daria; Domanska, Anna; Prorok, Paulina; Kosicki, Konrad; van den Born, Erwin; Falnes, Pal Oe.; Rizzo, Carmelo J.; Guengerich, F. Peter; Tudek, Barbara published an article.Electric Literature of 55662-66-3 The title of the article was Differential repair of etheno-DNA adducts by bacterial and human AlkB proteins. And the article contained the following:

AlkB proteins are evolutionary conserved Fe(II)/2-oxoglutarate-dependent dioxygenases, which remove alkyl and highly promutagenic etheno(ε)-DNA adducts, but their substrate specificity has not been fully determined We developed a novel assay for the repair of ε-adducts by AlkB enzymes using oligodeoxynucleotides with a single lesion and specific DNA glycosylases and AP-endonuclease for identification of the repair products. We compared the repair of three ε-adducts, 1,N6-ethenoadenine (εA), 3,N4-ethenocytosine (εC) and 1,N2-ethenoguanine (1,N2-εG) by nine bacterial and two human AlkBs, representing four different structural groups defined on the basis of conserved amino acids in the nucleotide recognition lid, engaged in the enzyme binding to the substrate. Two bacterial AlkB proteins, MT-2B (from Mycobacterium tuberculosis) and SC-2B (Streptomyces coelicolor) did not repair these lesions in either double-stranded (ds) or single-stranded (ss) DNA. Three proteins, RE-2A (Rhizobium etli), SA-2B (Streptomyces avermitilis), and XC-2B (Xanthomonas campestris) efficiently removed all three lesions from the DNA substrates. Interestingly, XC-2B and RE-2A are the first AlkB proteins shown to be specialized for ε-adducts, since they do not repair methylated bases. Three other proteins, EcAlkB (Escherichia coli), SA-1A, and XC-1B removed εA and εC from ds and ssDNA but were inactive toward 1,N2-εG. SC-1A repaired only εA with the preference for dsDNA. The human enzyme ALKBH2 repaired all three ε-adducts in dsDNA, while only εA and εC in ssDNA and repair was less efficient in ssDNA. ALKBH3 repaired only εC in ssDNA. Altogether, we have shown for the first time that some AlkB proteins, namely ALKBH2, RE-2A, SA-2B and XC-2B can repair 1,N2-εG and that ALKBH3 removes only εC from ssDNA. Our results also suggest that the nucleotide recognition lid is not the sole determinant of the substrate specificity of AlkB proteins. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Electric Literature of 55662-66-3

The Article related to alkb ethenodna adduct oxidative dealkylation oligodeoxynucleotide, 1,n(2)-ethenoguanine, 1,n(6)-ethenoadenine, 3,n(4)-ethenocytosine, alkb, dna repair, etheno adducts, Biochemical Genetics: Gene Structure and Organization and other aspects.Electric Literature of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On June 15, 2020, Demarteau, Jeremy; O’Harra, Kathryn E.; Bara, Jason E.; Sardon, Haritz published an article.Computed Properties of 5036-48-6 The title of the article was Valorization of Plastic Wastes for the Synthesis of Imidazolium-Based Self-Supported Elastomeric Ionenes. And the article contained the following:

Imidazolium-based ionenes are known to be high-performance materials for a great variety of applications. The preparation of these polymers requires the use of bis-imidazole starting monomers, which are commonly prepared by using toxic chloride reagents. In this study, bis-imidazole monomers are synthesized by organocatalytic chem. recycling of discarded plastics through chem. depolymerization By using poly(ethylene terephthalate) and bisphenol A polycarbonate as starting materials, different monomers containing amide or urea functionalities are prepared to produce high-mol.-weight ionic polymers. These novel ionenes show excellent elastomeric and self-healing behavior, serving as a promising means to expand the exploration of plastic wastes as a source of new materials. The experimental process involved the reaction of N-(3-Aminopropyl)-imidazole(cas: 5036-48-6).Computed Properties of 5036-48-6

The Article related to valorization plastic waste imidazolium self supported elastomeric ionene, ionenes, organocatalysis, plastics, recycling, waste valorization, Plastics Fabrication and Uses: Fabricating Techniques and other aspects.Computed Properties of 5036-48-6

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On June 30, 2021, Zhang, Pengyue; Gao, Jingjing; Li, Xinxu; Feng, Yilong; Shi, Manli; Shi, Yining; Zhang, Wenli published an article.Electric Literature of 443-72-1 The title of the article was Interplay of DNA and RNA N6-methyladenine with R-loops in regulating gene transcription in Arabidopsis. And the article contained the following:

R-loops and covalent modifications of N6-methyladenine on DNA (D-6 mA) or RNA (R-m6A) have been documented to function in various cellular processes in eukaryotes. However, the relationships between R-loops and both covalent modifications are still elusive in plants. Here, we integrated existing ssDRIP-seq with D-6 mA and R-m6A data from Arabidopsis thaliana. We found that the presence of either of both modifications facilitates R-loop formation and transcription of overlapping genes. Interestingly, our study suggests that the presence of R-m6A is key to affect R-loop intensity and pos. regulate gene transcription. Moreover, the presence of D-6 mA plays an additive role to facilitate the effect of R-m6A on R-loop intensity, however, D-6 mA may neg. regulate gene transcription when coexisted with R-m6A. Our analyses indicate that D-6 mA, R-m6A, or histone marks may act individually and cooperatively with R-loops in regulating gene transcription. Our study is the first to link R-loops with D-6 mA and R-m6A in plants, thereby providing new insights into interactions between R-loops with D-6 mA, R-m6A, and histone marks for regulating gene transcription. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Electric Literature of 443-72-1

The Article related to dna rna n6 methyladenine gene transcription arabidopsis, dna-6 ma, gene transcription, histone marks, plants, r-loops, rna-m6a, Biochemical Genetics: Gene Structure and Organization and other aspects.Electric Literature of 443-72-1

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On November 30, 2020, Zhou, Yujia; Kong, Ying; Fan, Wenguo; Tao, Tao; Xiao, Qin; Li, Na; Zhu, Xiao published an article.Name: N-Methyl-7H-purin-6-amine The title of the article was Principles of RNA methylation and their implications for biology and medicine. And the article contained the following:

RNA methylation is a post-transcriptional level of regulation. At present, more than 150 kinds of RNA modifications have been identified. They are widely distributed in mRNA (mRNA), tRNA (tRNA), rRNA (rRNA), noncoding small RNA (sncRNA) and long-chain non-coding RNA (lncRNA). In recent years, with the discovery of RNA methylation related proteins and the development of high-throughput sequencing technol., the mystery of RNA methylation has been gradually revealed, and its biol. function and application value have gradually emerged. In this review, a large number of research results of RNA methylation in recent years are collected. Through systematic summary and refinement, this review introduced RNA methylation modification-related proteins and RNA methylation sequencing technologies, as well as the biol. functions of RNA methylation, expressions and applications of RNA methylation-related genes in physiol. or pathol. states such as cancer, immunity and virus infection, and discussed the potential therapeutic strategies. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Name: N-Methyl-7H-purin-6-amine

The Article related to principle rna methylation implication biol medicine, biological function, cancer, rna methylation, regulators, m6a, Biochemical Genetics: Genetic Engineering and Cloning and other aspects.Name: N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On January 10, 2020, Wang, Baihui; Luo, Qiang; Li, Yingping; Yin, Liufan; Zhou, Nana; Li, Xiangnan; Gan, Jianhua; Dong, Aiwu published an article.Reference of N-Methyl-7H-purin-6-amine The title of the article was Structural insights into target DNA recognition by R2R3-MYB transcription factors. And the article contained the following:

As the largest group of MYB family transcription factors, R2R3-MYB proteins play essential roles during plant growth and development. However, the structural basis underlying how R2R3-MYBs recognize the target DNA remains elusive. Here, we report the crystal structure of Arabidopsis WEREWOLF (WER), an R2R3-MYB protein, in complex with its target DNA. Structural anal. showed that the third α-helixes in both the R2 and R3 repeats of WER fit in the major groove of the DNA, specifically recognizing the DNA motif 5′-AACNGC-3′. In combination with mutagenesis, in vitro binding and in vivo luciferase assays, we showed that K55, N106, K109 and N110 are critical for the function of WER. Although L59 of WER is not involved in DNA binding in the structure, ITC anal. suggested that L59 plays an important role in sensing DNA methylation at the fifth position of cytosine (5mC). Like 5mC, methylation at the sixth position of adenine (6mA) in the AAC element also inhibits the interaction between WER and its target DNA. Our study not only unravels the mol. basis of how WER recognizes its target DNA, but also suggests that 5mC and 6mA modifications may block the interaction between R2R3-MYB transcription factors and their target genes. 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 dna recognition crystal structure r2r3 myb transcription factor arabidopsis, Biochemical Genetics: Gene Structure and Organization and other aspects.Reference of N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On September 30, 2020, Fu, Ye; Zhuang, Xiaowei published an article.Recommanded Product: N-Methyl-7H-purin-6-amine The title of the article was m6A-binding YTHDF proteins promote stress granule formation. And the article contained the following:

Abstract: Diverse RNAs and RNA-binding proteins form phase-separated, membraneless granules in cells under stress conditions. However, the role of the prevalent mRNA methylation, m6A, and its binding proteins in stress granule (SG) assembly remain unclear. Here, we show that m6A-modified mRNAs are enriched in SGs, and that m6A-binding YTHDF proteins are critical for SG formation. Depletion of YTHDF1/3 inhibits SG formation and recruitment of mRNAs to SGs. Both the N-terminal intrinsically disordered region and the C-terminal m6A-binding YTH domain of YTHDF proteins are important for SG formation. Super-resolution imaging further reveals that YTHDF proteins appear to be in a super-saturated state, forming clusters that often reside in the periphery of or at the junctions between SG core clusters, and potentially promote SG formation by reducing the activation energy barrier and critical size for SG condensate formation. Our results suggest a new function of the m6A-binding YTHDF proteins in regulating SG 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 human ythdf protein mrna methylation m6a stress granule formation, General Biochemistry: Proteins and Their Constituents and other aspects.Recommanded Product: N-Methyl-7H-purin-6-amine

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Yang, Zuxiao; Wang, Jiayin; Huang, Lin; Lilley, David M. J.; Ye, Keqiong published an article in 2020, the title of the article was Functional organization of box C/D RNA-guided RNA methyltransferase.HPLC of Formula: 443-72-1 And the article contains the following content:

Box C/D RNA protein complexes (RNPs) catalyze site-specific 2′-O-methylation of RNA with specificity determined by guide RNAs. In eukaryotic C/D RNP, the paralogous Nop58 and Nop56 proteins specifically associate with terminal C/D and internal C’/D’ motifs of guide RNAs, resp. We have reconstituted active C/D RNPs with recombinant proteins of the thermophilic yeast Chaetomium thermophilum. Nop58 and Nop56 could not distinguish between the two C/D motifs in the reconstituted enzyme, suggesting that the assembly specificity is imposed by trans-acting factors in vivo. The two C/D motifs are functionally independent and halfmer C/D RNAs can also guide site-specific methylation. Extensive pairing between C/D RNA and substrate is inhibitory to modification for both yeast and archaeal C/D RNPs. N6-methylated adenine at box D/D interferes with the function of the coupled guide. Our data show that all C/D RNPs share the same functional organization and mechanism of action and provide insight into the assembly specificity of eukaryotic C/D RNPs. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).HPLC of Formula: 443-72-1

The Article related to box cd rna methyltransferase n6 methylation protein complexe, Biochemical Genetics: Gene Structure and Organization and other aspects.HPLC of Formula: 443-72-1

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On December 31, 2022, Rodriguez, Fernando; Yushenova, Irina A.; DiCorpo, Daniel; Arkhipova, Irina R. published an article.SDS of cas: 443-72-1 The title of the article was Bacterial N4-methylcytosine as an epigenetic mark in eukaryotic DNA. And the article contained the following:

DNA modifications are used to regulate gene expression and defend against invading genetic elements. In eukaryotes, modifications predominantly involve C5-methylcytosine (5mC) and occasionally N6-methyladenine (6mA), while bacteria frequently use N4-methylcytosine (4mC) in addition to 5mC and 6mA. Here we report that 4mC can serve as an epigenetic mark in eukaryotes. Bdelloid rotifers, tiny freshwater invertebrates with transposon-poor genomes rich in foreign genes, lack canonical eukaryotic C5-methyltransferases for 5mC addition, but encode an amino-methyltransferase, N4CMT, captured from bacteria >60 Mya. N4CMT deposits 4mC at active transposons and certain tandem repeats, and fusion to a chromodomain shapes its “histone-read-DNA-write” architecture recognizing silent chromatin marks. Furthermore, amplification of SETDB1 H3K9me3 histone methyltransferases yields variants preferentially binding 4mC-DNA, suggesting “DNA-read-histone-write” partnership to maintain chromatin-based silencing. Our results show how non-native DNA Me groups can reshape epigenetic systems to silence transposons and demonstrate the potential of horizontal gene transfer to drive regulatory innovation in eukaryotes. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).SDS of cas: 443-72-1

The Article related to bdelloid epigenetics n4 methylcytosine dna, General Biochemistry: Proteins and Their Constituents and other aspects.SDS of cas: 443-72-1

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

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