Results 21 to 30 of about 678 (148)

Non-flipping DNA glycosylase AlkD scans DNA without formation of a stable interrogation complex

open access: yesCommunications Biology, 2021
Ahmadi et al. use a single-molecule tracking method to describe the DNA scanning mode of AlkD, a HEAT-like repeat DNA glycosylase. They show that, contrary to other glycosylases that use a base-flipping mechanism, AlkD scans the DNA without forming a ...
Arash Ahmadi   +10 more
doaj   +1 more source

Mono- and biallelic germline variants of DNA glycosylase genes in colon adenomatous polyposis families from two continents

open access: yesFrontiers in Oncology, 2022
Recently, biallelic germline variants of the DNA glycosylase genes MUTYH and NTHL1 were linked to polyposis susceptibility. Significant fractions remain without a molecular explanation, warranting searches for underlying causes.
Alisa Petriina Olkinuora   +23 more
doaj   +1 more source

Inhibitors of DNA Glycosylases as Prospective Drugs [PDF]

open access: yesInternational Journal of Molecular Sciences, 2020
DNA glycosylases are enzymes that initiate the base excision repair pathway, a major biochemical process that protects the genomes of all living organisms from intrinsically and environmentally inflicted damage. Recently, base excision repair inhibition proved to be a viable strategy for the therapy of tumors that have lost alternative repair pathways,
Grigory V. Mechetin   +3 more
openaire   +2 more sources

A New Family of HEAT-Like Repeat Proteins Lacking a Critical Substrate Recognition Motif Present in Related DNA Glycosylases. [PDF]

open access: yesPLoS ONE, 2015
DNA glycosylases are important repair enzymes that eliminate a diverse array of aberrant nucleobases from the genomes of all organisms. Individual bacterial species often contain multiple paralogs of a particular glycosylase, yet the molecular and ...
Elwood A Mullins   +3 more
doaj   +1 more source

Resistance-Guided Mining of Bacterial Genotoxins Defines a Family of DNA Glycosylases

open access: yesmBio, 2022
Unique DNA repair enzymes that provide self-resistance against therapeutically important, genotoxic natural products have been discovered in bacterial biosynthetic gene clusters (BGCs).
Noah P. Bradley   +4 more
doaj   +1 more source

Nei-like 1 (NEIL1) excises 5-carboxylcytosine directly and stimulates TDG-mediated 5-formyl and 5-carboxylcytosine excision

open access: yesScientific Reports, 2017
Thymine DNA glycosylase (TDG) and Nei-like 1 (NEIL1) have both been implicated in the base excision repair step of active DNA demethylation. The robust glycosylase activity of TDG on DNA substrates containing 5-formylcytosine (5fC) or 5-carboxylcytosine (
Anton Slyvka   +2 more
doaj   +1 more source

Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.

open access: yesPLoS ONE, 2011
Orthohepadnavirus (mammalian hosts) and avihepadnavirus (avian hosts) constitute the family of Hepadnaviridae and differ by their capability and inability for expression of protein X, respectively. Origin and functions of X are unclear.
Formijn J van Hemert   +5 more
doaj   +1 more source

Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea

open access: yesFrontiers in Microbiology, 2021
Since hyperthermophilic Archaea (HA) thrive in high-temperature environments, which accelerate the rates of deamination of base in DNA, their genomic stability is facing a severe challenge.
Tan Lin   +6 more
doaj   +1 more source

DNA Sequence Context Effects on the Glycosylase Activity of Human 8-Oxoguanine DNA Glycosylase [PDF]

open access: yesJournal of Biological Chemistry, 2012
Human 8-oxoguanine DNA glycosylase (OGG1) is a key enzyme involved in removing 7,8-dihydro-8-oxoguanine (8-oxoG), a highly mutagenic DNA lesion generated by oxidative stress. The removal of 8-oxoG by OGG1 is affected by the local DNA sequence, and this feature most likely contributes to observed mutational hot spots in genomic DNA.
Akira, Sassa   +3 more
openaire   +2 more sources

Plant and fungal Fpg homologs are formamidopyrimidine DNA glycosylases but not 8-oxoguanine DNA glycosylases [PDF]

open access: yesDNA Repair, 2009
Formamidopyrimidine DNA glycosylase (Fpg) and endonuclease VIII (Nei) share an overall common three-dimensional structure and primary amino acid sequence in conserved structural motifs but have different substrate specificities, with bacterial Fpg proteins recognizing formamidopyrimidines, 8-oxoguanine (8-oxoG) and its oxidation products ...
Scott D, Kathe   +8 more
openaire   +2 more sources

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