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

Structural insight into the DNA polymerase beta deoxyribose phosphate lyase mechanism.

DNA repair - 8 Dec 2005

Prasad Rajendra, Batra Vinod K, Yang Xiao-Ping, Krahn Joseph M, Pedersen Lars C, Beard William A, Wilson Samuel H

Abstract excerpt

A large number of biochemical and genetic studies have demonstrated the involvement of DNA polymerase beta (Pol beta) in mammalian base excision repair (BER). Pol beta participates in BER sub-pathways by contributing gap filling DNA synthesis and lyase removal of the 5'-deoxyribose phosphate (dRP) group from the cleaved abasic site. To better understand the mechanism of the dRP lyase reaction at an atomic level,...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Polymerase beta

Share to DNA Repair

Share to Lysine

Share to Phosphorus-Oxygen Lyases

Share to Protein Conformation

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 16172026
DOI: 10.1016/j.dnarep.2005.08.009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural insight into the DNA polymerase beta deoxyribose phosphate lyase mechanism.PMID 16172026Read ↗

A triad interaction in the fingers subdomain of DNA polymerase beta controls polymerase activity.Semantic proximity Read ↗

DNA polymerase beta is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts.Semantic proximity Read ↗

A DNA polymerase beta mutator mutant with reduced nucleotide discrimination and increased protein stability.Semantic proximity Read ↗

Hinge residue I174 is critical for proper dNTP selection by DNA polymerase beta.Semantic proximity Read ↗

Involvement of phenylalanine 272 of DNA polymerase beta in discriminating between correct and incorrect deoxynucleoside triphosphates.Semantic proximity Read ↗

Hinge residue Ile260 of DNA polymerase beta is important for enzyme activity and fidelity.Semantic proximity Read ↗

Mechanistic Insight through Irreversible Inhibition: DNA Polymerase θ Uses a Common Active Site for Polymerase and Lyase Activities.Semantic proximity Read ↗

Structural basis of transcriptional stalling and bypass of abasic DNA lesion by RNA polymerase II.Semantic proximity Read ↗

The Impact of SNP-Induced Amino Acid Substitutions L19P and G66R in the dRP-Lyase Domain of Human DNA Polymerase β on Enzyme Activities.Semantic proximity Read ↗

Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity.Semantic proximity Read ↗

POLθ processes ssDNA gaps and promotes replication fork progression in BRCA1-deficient cells.Semantic proximity Read ↗

Substrate rescue of DNA polymerase β containing a catastrophic L22P mutation.Semantic proximity Read ↗

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