Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Substrate-Specific Inactivation of Human AAG by Tumor-Associated Single Nucleotide Polymorphic Variants.

International journal of molecular sciences - 24 Jul 2026

Kladova Olga A, Tyugashev Timofey E, Bakman Artemiy S, Kuznetsova Aleksandra A

Abstract excerpt

Human alkyladenine DNA glycosylase (AAG) initiates base excision repair of various alkylated and deaminated purines. Single nucleotide polymorphisms (SNPs) in the AAG gene occur frequently in populations and tumors, but the functional impact of most variants remains unknown. Previously, we identified three SNPs-P94L, V158M, and E293K-which have been predicted to have a high deleterious potential. This study aimed...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenine
Share to Adenosine
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA Glycosylases

Share to Molecular Dynamics Simulation

Share to Neoplasms

Share to Polymorphism, Single Nucleotide

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 42589254
DOI: 10.3390/ijms27156595
PMCID: PMC13465763

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 17 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substrate-Specific Inactivation of Human AAG by Tumor-Associated Single Nucleotide Polymorphic Variants.PMID 42589254Read ↗

Activity of natural single nucleotide variants of human alkyladenine DNA glycosylase AAG R145H, G163S and R197C involved in DNA binding.Semantic proximity Read ↗

The Link Between Human Alkyladenine DNA Glycosylase and Cancer DevelopmentSemantic proximity Read ↗

Substrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survival.Semantic proximity Read ↗

The substrate binding interface of alkylpurine DNA glycosylase AlkD.Semantic proximity Read ↗

Frameshift mutagenesis and microsatellite instability induced by human alkyladenine DNA glycosylase.Semantic proximity Read ↗

Germ line variants of human N-methylpurine DNA glycosylase show impaired DNA repair activity and facilitate 1,N6-ethenoadenine-induced mutations.Semantic proximity Read ↗

Critical role of DNA intercalation in enzyme-catalyzed nucleotide flipping.Semantic proximity Read ↗

Molecular and structural characterization of disease-associated APE1 polymorphisms.Semantic proximity Read ↗

Disease-Associated Mutations Impact DNA Methyltransferase 1 Function through Dynamic Allosteric Effects and Solvent Exposure.Semantic proximity Read ↗

Modulation of the Apurinic/Apyrimidinic Endonuclease Activity of Human APE1 and of Its Natural Polymorphic Variants by Base Excision Repair Proteins.Semantic proximity Read ↗

Search for DNA damage by human alkyladenine DNA glycosylase involves early intercalation by an aromatic residue.Semantic proximity Read ↗

Mutations in the alpha8 loop of human APE1 alter binding and cleavage of DNA containing an abasic site.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.