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

Insight into the modified Ibalizumab-human CD4 receptor interactions: using a computational binding free energy approach.

Journal of computer-aided molecular design - 1 Jan 2015

Wang Yeng-Tseng, Chuang Lea-Yea

Abstract excerpt

Antibody drugs are very useful tools for the treatment of many chronic diseases. Recently, however, patients and doctors have encountered the problem of drug resistance. How to improve the affinity of antibody drugs has therefore become a pressing issue. Ibalizumab is a humanized monoclonal antibody that binds human CD4, the primary receptor for human immunodeficiency virus type 1. This study investigates the...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Anti-HIV Agents
Share to Antibodies, Monoclonal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to CD4 Antigens

Share to Molecular Dynamics Simulation

Share to Mutagenesis

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 25342515
DOI: 10.1007/s10822-014-9805-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Insight into the modified Ibalizumab-human CD4 receptor interactions: using a computational binding free energy approach.PMID 25342515Read ↗

E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studies.Semantic proximity Read ↗

Insight into free energy and dynamic cross-correlations of residue for binding affinity of antibody and receptor binding domain SARS-CoV-2Semantic proximity Read ↗

Insight into crizotinib resistance mechanisms caused by three mutations in ALK tyrosine kinase using free energy calculation approaches.Semantic proximity Read ↗

Antibody humanization by molecular dynamics simulations-in-silico guided selection of critical backmutations.Semantic proximity Read ↗

Computer-aided affinity enhancement of a cross-reactive antibody against dengue virus envelope domain IIISemantic proximity Read ↗

R346K Mutation in the Mu Variant of SARS-CoV-2 Alters the Interactions with Monoclonal Antibodies from Class 2: A Free Energy Perturbation Study.Semantic proximity Read ↗

Free-energy simulations reveal that both hydrophobic and polar interactions are important for influenza hemagglutinin antibody binding.Semantic proximity Read ↗

Insights into drug resistance of mutations D30N and I50V to HIV-1 protease inhibitor TMC-114: free energy calculation and molecular dynamic simulation.Semantic proximity Read ↗

The impact of PD-1 mutations on pembrolizumab binding: insights from molecular dynamics and MM-GBSA analysis.Semantic proximity Read ↗

Drug resistance mechanisms of three mutations V32I, I47V and V82I in HIV-1 protease toward inhibitors probed by molecular dynamics simulations and binding free energy predictionsSemantic proximity Read ↗

Assessment of software methods for estimating protein-protein relative binding affinities.Semantic proximity Read ↗

Exploring the structural and functional impact of the ALK F1174L mutation using bioinformatics approach.Semantic proximity Read ↗

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