Category: 55662-66-3

On April 30, 2015, Shivange, Gururaj; Kodipelli, Naveena; Anindya, Roy published an article.Electric Literature of 55662-66-3 The title of the article was 2-Hydrazinobenzothiazole-based etheno-adduct repair protocol (HERP): A method for quantitative determination of direct repair of etheno-bases. And the article contained the following:

Etheno-DNA adducts are mutagenic and lead to genomic instability. Enzymes belonging to Fe(II)/2-oxoglutarate-dependent dioxygenase family repair etheno-DNA adducts by directly removing alkyl chain as glyoxal. Presently there is no simple method to assess repair reaction of etheno-adducts. We have developed a rapid and sensitive assay for studying etheno-DNA adduct repair by Fe(II)/2-oxoglutarate-dependent dioxygenases. Using AlkB as model Fe(II)/2-oxoglutarate-dependent dioxygenases, we performed in vitro repair of etheno-adducts containing DNA and detected glyoxal by reacting with 2-hydrazinobenzothiazole which forms complex yellow color compound with distinct absorption spectrum with a peak absorption at 365 nm. We refer this method as 2-hydrazinobenzothiazole-based etheno-adduct repair protocol or HERP. Our novel approach for determining repair of etheno-adducts containing DNA overcomes several drawbacks of currently available radioisotope-based assay. 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 hydrazinobenzothiazole etheno adduct repair dna alkb, 1,n(2)-ethenoguanine, 1,n(6)-ethenoadenine, 3,n(4)-ethenocytosine, chloroacetaldehyde, dna repair, etheno adduct, fe(ii)/2-oxoglutarate-dependent dioxygenase, n(2),3-ethenoguanine and other aspects.Electric Literature of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

On February 7, 2020, Thelen, Adam Z.; O’Brien, Patrick J. published an article.Recommanded Product: Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was Recognition of 1,N2-ethenoguanine by alkyladenine DNA glycosylase is restricted by a conserved active-site residue. And the article contained the following:

The adenine, cytosine, and guanine bases of DNA are susceptible to alkylation by the aldehyde products of lipid peroxidation and by the metabolic byproducts of vinyl chloride pollutants. The resulting adducts spontaneously cyclize to form harmful etheno lesions. Cells employ a variety of DNA repair pathways to protect themselves from these pro-mutagenic modifications. Human alkyladenine DNA glycosylase (AAG) is thought to initiate base excision repair of both 1,N6-ethenoadenine (εA) and 1,N2-ethenoguanine (εG). However, it is not clear how AAG might accommodate εG in an active site that is complementary to εA. This prompted a thorough investigation of AAG-catalyzed excision of εG from several relevant contexts. Using single-turnover and multiple-turnover kinetic analyses, we found that εG in its natural εG·εC context is very poorly recognized relative to εA·εT. Bulged and mispaired εG contexts, which can form during DNA replication, were similarly poor substrates for AAG. Furthermore, AAG could not recognize an εG site in competition with excess undamaged DNA sites. Guided by previous structural studies, we hypothesized that Asn-169, a conserved residue in the AAG active-site pocket, contributes to discrimination against εG. Consistent with this model, the N169S variant of AAG was 7-fold more active for excision of εG compared with the wildtype (WT) enzyme. Taken together, these findings suggest that εG is not a primary substrate of AAG, and that current models for etheno lesion repair in humans should be revised. We propose that other repair and tolerance mechanisms operate in the case of εG lesions. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Recommanded Product: Imidazo[1,2-c]pyrimidin-5(6H)-one

The Article related to human alkyladenine dna glycosylase active site recognition ethenoguanine repair, dna alkylation, dna damage, dna repair, alkyladenine dna glycosylase, base excision repair (ber), enzyme kinetics, ethenoguanine, substrate specificity and other aspects.Recommanded Product: Imidazo[1,2-c]pyrimidin-5(6H)-one

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem

Matkarimov, Bakhyt T.; Saparbaev, Murat K. published an article in 2020, the title of the article was DNA Repair and Mutagenesis in Vertebrate Mitochondria: Evidence for Asymmetric DNA Strand Inheritance.Electric Literature of 55662-66-3 And the article contains the following content:

A variety of endogenous and exogenous factors induce chem. and structural alterations in cellular DNA in addition to the errors occurring throughout DNA synthesis. These types of DNA damage are cytotoxic, miscoding or both and are believed to be at the origin of cancer and other age-related diseases. A human cell, aside from nuclear DNA, contains thousands of copies of mitochondrial DNA (mtDNA), a double-stranded, circular mol. of 16,569 bp. It has been proposed that mtDNA is a critical target of reactive oxygen species: byproducts of oxidative phosphorylation that are generated in the organelle during aerobic respiration. Indeed, oxidative damage to mtDNA is more extensive and persistent as compared to that to nuclear DNA. Although transversions are the hallmark of mutations induced by reactive oxygen species, paradoxically, the majority of mtDNA mutations that occur during aging and cancer are transitions. Furthermore, these mutations show a striking strand orientation bias: T→C/G→A transitions preferentially occur on the light strand, whereas C→T/A→G on the heavy strand of mtDNA. Here, we propose that the majority of mtDNA progenies, created after multiple rounds of DNA replication, are derived from the heavy strand only, owing to asym. replication of the DNA strand anchored to the inner membrane via the D-loop structure. 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 review mitochondrial dna mismatch repair damage mutagenesis oxidative phosphorylation, review2 ros nucleotide excision uracil, abasic sites, dna excision repair, dna glycosylases, mitochondrial dna, oxidative dna damage, uracil and other aspects.Electric Literature of 55662-66-3

Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem