Results 11 to 20 of about 43,780 (231)

Emergence of highly profibrotic and proinflammatory Lrat+Fbln2+ HSC subpopulation in alcoholic hepatitis

open access: yesHepatology, EarlyView., 2022
Lrat+ quiescent hepatic stellate cells (qHSC) give rise to Lrat+Fbln2+ activated HSC (aHSC) in alcohol‐associated hepatitis and this subpopulation is highly profibrotic, inflammatory, and immunoregulatory based on their single cell transcriptomic profile. Abstract Background and Aims Relative roles of HSCs and portal fibroblasts in alcoholic hepatitis (
Steven Balog   +12 more
wiley   +1 more source

Inhibition of DNA glycosylases via small molecule purine analogs. [PDF]

open access: yesPLoS ONE, 2013
Following the formation of oxidatively-induced DNA damage, several DNA glycosylases are required to initiate repair of the base lesions that are formed.
Aaron C Jacobs   +9 more
doaj   +1 more source

Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process

open access: yesActa Biochimica et Biophysica Sinica, 2022
DNA glycosylase, as one member of DNA repair machineries, plays an essential role in correcting mismatched/damaged DNA nucleotides by cleaving the N-glycosidic bond between the sugar and target nucleobase through the base excision repair (BER) pathways ...
Wang Lingyan   +3 more
doaj   +1 more source

Oxanine DNA Glycosylase Activity from Mammalian Alkyladenine Glycosylase [PDF]

open access: yesJournal of Biological Chemistry, 2004
Oxanine (Oxa) is a deaminated base lesion derived from guanine in which the N(1)-nitrogen is substituted by oxygen. This work reports the mutagenicity of oxanine as well as oxanine DNA glycosylase (ODG) activities in mammalian systems. Using human DNA polymerase beta, deoxyoxanosine triphosphate is only incorporated opposite cytosine (Cyt).
Hitchcock, TM   +6 more
openaire   +3 more sources

Structural and mechanistic insights into the DNA glycosylase AAG-mediated base excision in nucleosome

open access: yesCell Discovery, 2023
The engagement of a DNA glycosylase with a damaged DNA base marks the initiation of base excision repair. Nucleosome-based packaging of eukaryotic genome obstructs DNA accessibility, and how DNA glycosylases locate the substrate site on nucleosomes is ...
Lvqin Zheng, Bin Tsai, Ning Gao
doaj   +1 more source

Characterization of a conserved interaction between DNA glycosylase and ParA in Mycobacterium smegmatis and M. tuberculosis. [PDF]

open access: yesPLoS ONE, 2012
The chromosome partitioning proteins, ParAB, ensure accurate segregation of genetic materials into daughter cells and most bacterial species contain their homologs. However, little is known about the regulation of ParAB proteins.
Feng Huang, Zheng-Guo He
doaj   +1 more source

Noncatalytic Domains in DNA Glycosylases

open access: yesInternational Journal of Molecular Sciences, 2022
Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes.
Natalia A. Torgasheva   +7 more
openaire   +2 more sources

OGG1 Inhibitor TH5487 Alters OGG1 Chromatin Dynamics and Prevents Incisions

open access: yesBiomolecules, 2020
8-oxoguanine DNA glycosylase (OGG1) is the main DNA glycosylase responsible for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG) from duplex DNA to initiate base excision repair.
Bishoy M. F. Hanna   +2 more
doaj   +1 more source

Biochemical characterization and novel inhibitor identification of Mycobacterium tuberculosis Endonuclease VIII 2 (Rv3297)

open access: yesBiochemistry and Biophysics Reports, 2017
Nei2 (Rv3297) is a DNA Base Excision Repair (BER) glycosylase that is essential for survival of Mycobacterium tuberculosis in primates. We show that MtbNei2 is a bifunctional glycosylase that specifically acts on oxidized pyrimidine-containing single ...
Kiran Lata   +2 more
doaj   +1 more source

A Novel 3-Methyladenine DNA Glycosylase from Helicobacter pylori Defines a New Class within the Endonuclease III Family of Base Excision Repair Glycosylases [PDF]

open access: yes, 2000
The cloning, purification, and characterization of MagIII, a 3-methyladenine DNA glycosylase from Helicobacter pylori, is presented in this paper. Sequence analysis of the genome of this pathogen failed to identify open reading frames potentially coding ...
Boiteux, Serge   +5 more
core   +1 more source

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