In silico studies on the role of mutant Y337A to reactivate tabun inhibited mAChE with K048.

doi:10.1016/j.cbi.2015.10.016

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

Back to search

Article

In silico studies on the role of mutant Y337A to reactivate tabun inhibited mAChE with K048.

Chemico-biological interactions - 5 Dec 2015

Chandar Nellore Bhanu, Ghosh Shibaji, Lo Rabindranath, Banjo Semire, Ganguly Bishwajit

Abstract excerpt

Organophosphorus compound (OP) tabun is resistant to reactivate by many oxime drugs after the formation of OP-conjugate with AChE. The reactivation of tabun-inhibited mAChE and site-directed mutants by bispyridinium oxime, K048 (N-[4-(4-hydroxyiminomethylpyridinio)butyl]-4-carbamoylpyridinium dibromide) showed that the mutations significantly poor the overall reactivation efficacy of K048. We have unravelled the...

Topics

Acetylcholinesterase
Catalytic Domain
Cholinesterase Inhibitors
Computer Simulation
Enzyme Reactivators
Molecular Docking Simulation
Molecular Dynamics Simulation
Mutation
Organophosphates
Oximes
Pyridinium Compounds

Source

Open in PubMed

Identifiers

PMID: 26494532
DOI: 10.1016/j.cbi.2015.10.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics