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

Inhibition of type IA topoisomerase by a monoclonal antibody through perturbation of DNA cleavage-religation equilibrium.

The FEBS journal - 1 Jan 2012

Leelaram Majety Naga, Bhat Anuradha Gopal, Hegde Shivanand Manjunath, Manjunath Ramanathapuram, Nagaraja Valakunja

Abstract excerpt

Type IA DNA topoisomerases, typically found in bacteria, are essential enzymes that catalyse the DNA relaxation of negative supercoils. DNA gyrase is the only type II topoisomerase that can carry out the opposite reaction (i.e. the introduction of the DNA supercoils). A number of diverse molecules target DNA gyrase. However, inhibitors that arrest the activity of bacterial topoisomerase I at low concentrations...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Monoclonal
Share to DNA Adducts

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

Share to DNA, Bacterial

Share to DNA Cleavage

Share to DNA, Superhelical

Share to DNA Topoisomerases, Type I

Share to Kinetics

Share to Mycobacterium smegmatis

Source

Identifiers

PMID: 22008463
DOI: 10.1111/j.1742-4658.2011.08398.x

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibition of type IA topoisomerase by a monoclonal antibody through perturbation of DNA cleavage-religation equilibrium.PMID 22008463Read ↗

Type IA topoisomerase inhibition by clamp closure.Semantic proximity Read ↗

Mutation adjacent to the active site tyrosine can enhance DNA cleavage and cell killing by the TOPRIM Gly to Ser mutant of bacterial topoisomerase I.Semantic proximity Read ↗

Deciphering the distinct role for the metal coordination motif in the catalytic activity of Mycobacterium smegmatis topoisomerase I.Semantic proximity Read ↗

Bacterial cell killing mediated by topoisomerase I DNA cleavage activity.Semantic proximity Read ↗

Bacterial topoisomerase I as a target for discovery of antibacterial compounds.Semantic proximity Read ↗

Pathogenic and Epiphenomenal Anti-DNA Antibodies in SLESemantic proximity Read ↗

Interactions between Zoliflodacin and Neisseria gonorrhoeae Gyrase and Topoisomerase IV: Enzymological Basis for Cellular TargetingSemantic proximity Read ↗

Heavy and Light Chain Variable Single Domains of an Anti-DNA Binding Antibody Hydrolyze Both Double- and Single-stranded DNAs without Sequence SpecificitySemantic proximity Read ↗

Mutational analysis of a type II topoisomerase cleavage site: distinct requirements for enzyme and inhibitors.Semantic proximity Read ↗

The antibiotic microcin B17 is a DNA gyrase poison: characterisation of the mode of inhibition.Semantic proximity Read ↗

Mechanism of DNA transesterification by vaccinia topoisomerase: catalytic contributions of essential residues Arg-130, Gly-132, Tyr-136 and Lys-167.Semantic proximity Read ↗

Mutations within a conserved region of vaccinia topoisomerase affect the DNA cleavage-religation equilibrium.Semantic proximity Read ↗

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