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

Dynamics of fluoroquinolones induced resistance in DNA gyrase of Mycobacterium tuberculosis.

Journal of biomolecular structure & dynamics - 1 Feb 2018

Pandey Bharati, Grover Sonam, Tyagi Chetna, Goyal Sukriti, Jamal Salma, Singh Aditi, Kaur Jagdeep, Grover Abhinav

Abstract excerpt

DNA gyrase is a validated target of fluoroquinolones which are key components of multidrug resistance tuberculosis (TB) treatment. Most frequent occurring mutations associated with high level of resistance to fluoroquinolone in clinical isolates of TB patients are A90V, D94G, and A90V-D94G (double mutant [DM]), present in the larger subunit of DNA Gyrase. In order to explicate the molecular mechanism of drug...

Read the complete abstract on PubMed

Topics

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

Share to DNA Gyrase
Share to Fluoroquinolones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Docking Simulation

Share to Molecular Structure

Share to Moxifloxacin

Share to Mycobacterium tuberculosis

Share to Topoisomerase II Inhibitors

Share to Tuberculosis

Source

Identifiers

PMID: 28071975
DOI: 10.1080/07391102.2016.1277784

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dynamics of fluoroquinolones induced resistance in DNA gyrase of Mycobacterium tuberculosis.PMID 28071975Read ↗

Molecular dynamics simulations to investigate Mycobacterium tuberculosis DNA-gyrase-fluoroquinolone complexes.Semantic proximity Read ↗

Application of Computational Methods in Understanding Mutations in Mycobacterium tuberculosis Drug ResistanceSemantic proximity Read ↗

Molecular Dynamics Assisted Mechanistic Insight of Val430-Ala Mutation of Rv1592c Protein in Isoniazid Resistant Mycobacterium Tuberculosis.Semantic proximity Read ↗

Structural analyses and classification of novel isoniazid resistance coupled mutational landscapes in Mycobacterium tuberculosis: a combined molecular docking and MD simulation study.Semantic proximity Read ↗

Exploration of fluoroquinolone resistance in Streptococcus pyogenes: comparative structure analysis of wild-type and mutant DNA gyrase.Semantic proximity Read ↗

Molecular Dynamics Simulations of Quinolone Resistance-Associated T86I and P104S Mutations in Campylobacter jejuni gyrA: Unraveling Structural Repercussions.Semantic proximity Read ↗

Probing the Molecular Mechanism of Rifampin Resistance Caused by the Point Mutations S456L and D441V on Mycobacterium tuberculosis RNA Polymerase through Gaussian Accelerated Molecular Dynamics Simulation.Semantic proximity Read ↗

Docking studies on novel analogues of 8 methoxy fluoroquinolones against GyrA mutants of Mycobacterium tuberculosis.Semantic proximity Read ↗

Characterization of Ofloxacin Interaction with Mutated (A91V) Quinolone Resistance Determining Region of DNA Gyrase in Mycobacterium Leprae through Computational Simulation.Semantic proximity Read ↗

Exploration of potential inhibitors for tuberculosis via structure‐based drug design, molecular docking, and molecular dynamics simulation studiesSemantic proximity Read ↗

Identification of hotspot regions of MurB oxidoreductase enzyme using homology modeling, molecular dynamics and molecular docking techniques.Semantic proximity Read ↗

Computational structure-guided approach to simulate delamanid and pretomanid binding to mycobacterial F420 redox cycling proteins: identification of key determinants of resistance.Semantic proximity Read ↗

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