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

Topics Community

Article

A new role for the nonpathogenic nonsynonymous single-nucleotide polymorphisms of acetylcholinesterase in the treatment of Alzheimer's disease: a computational study.

Journal of computational biology : a journal of computational molecular cell biology - 1 Aug 2014

Saravanaraman Ponne, Chinnadurai Raj Kumar, Boopathy Rathanam

Abstract excerpt

Single-nucleotide polymorphisms (SNPs) are implicated in the complexity of understanding the genetics of diseases and their therapeutics. Here we have attempted to determine the impact of nonsynonymous SNPs (nsSNPs) on structure, dynamics, and ligand-binding properties of the human acetylcholinesterase (hAChE) protein, which has been targeted in the treatment of Alzheimer's disease. Of the reported 153 SNPs, 4...

Topics

Acetylcholinesterase
Alzheimer Disease
Amino Acid Sequence
Cholinesterase Inhibitors
Humans
Molecular Docking Simulation
Molecular Dynamics Simulation
Molecular Sequence Data
Polymorphism, Single Nucleotide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Conformation

Sequence Alignment

Source

Identifiers

PMID: 24611490
DOI: 10.1089/cmb.2014.0005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

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

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A new role for the nonpathogenic nonsynonymous single-nucleotide polymorphisms of acetylcholinesterase in the treatment of Alzheimer's disease: a computational study.PMID 24611490Read ↗

In silico analyses of acetylcholinesterase (AChE) and its genetic variants in interaction with the anti‐Alzheimer drug RivastigmineSemantic proximity Read ↗

Computational prediction of high-risk non-synonymous SNPs in human ApoE and their structural impact on amyloid-β interaction in Alzheimer’s disease pathogenesisSemantic proximity Read ↗

Analysis of Alzheimer's disease associated deleterious non-synonymous single nucleotide polymorphisms and their impacts on protein structure and function by performing in-silico methods.Semantic proximity Read ↗

Single nucleotide polymorphisms affecting galantamine binding to acetylcholinesterase in Alzheimer's disease: a structural bioinformatics study.Semantic proximity Read ↗

Functional non-synonymous polymorphisms prediction methods: current approaches and future developments.Semantic proximity Read ↗

Exploration of deleterious single nucleotide polymorphisms in late-onset Alzheimer disease susceptibility genes.Semantic proximity Read ↗

Integrative bioinformatics analysis of APOE variants in Alzheimer's disease and clinical therapeutics.Semantic proximity Read ↗

Functional impacts of non-synonymous single nucleotide polymorphisms: selective constraint and structural environments.Semantic proximity Read ↗

Computational Screening and Exploration of Disease-Associated Genes in Alzheimer's Disease.Semantic proximity Read ↗

Computational Insights into the Deleterious Impacts of Missense Variants on N-Acetyl-d-glucosamine Kinase Structure and Function.Semantic proximity Read ↗

A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene.Semantic proximity Read ↗

In-silico screening and microsecond molecular dynamics simulations to identify single point mutations that destabilize β-hexosaminidase A causing Tay-Sachs disease.Semantic proximity Read ↗

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