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

An all-atom molecular dynamics study of the anti-interferon signaling of Ebola virus: interaction mechanisms of EBOV VP24 binding to Karyopherin alpha5.

Molecular bioSystems - 2 May 2017

Ding Jing-Na, Zhang Yan-Jun, Zhong Hui, Ao Cheng-Cheng, Li Jing, Han Ju-Guang

Abstract excerpt

Ebola virus (EBOV) is highly lethal due to virally encoded immune antagonists, and the combination of EBOV VP24 with karyopherin alpha (KPNA) will trigger anti-interferon (IFN) signaling. The crystal structure of VP24-KPNA5 has been proposed in recent studies, but the precise binding mechanisms are still unclear. In order to explore the VP24-KPNA5 protein binding micro-mechanisms, Molecular Dynamic (MD)...

Read the complete abstract on PubMed

Topics

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

Share to alpha Karyopherins
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Ebolavirus

Share to Hydrogen Bonding

Share to Interferon-beta

Share to Molecular Dynamics Simulation

Share to Viral Proteins

Source

Identifiers

PMID: 28418440
DOI: 10.1039/c7mb00136c

Genes

KPNA5

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

An all-atom molecular dynamics study of the anti-interferon signaling of Ebola virus: interaction mechanisms of EBOV VP24 binding to Karyopherin alpha5.PMID 28418440Read ↗

Correlating the ability of VP24 protein from Ebola and Marburg viruses to bind human karyopherin to their immune suppression mechanism and pathogenicity using computational methodsSemantic proximity Read ↗

Exploring interaction mechanisms of the inhibitor binding to the VP35 IID region of Ebola virus by all atom molecular dynamics simulation method.Semantic proximity Read ↗

Ebolavirus Species-Specific Interferon Antagonism Mediated by VP24Semantic proximity Read ↗

Exploration micromechanism of VP35 IID interaction and recognition dsRNA: A molecular dynamics simulation.Semantic proximity Read ↗

Effect of novel leukemia mutations (K75E & E222K) on interferon regulatory factor 1 and its interaction with DNA: insights from molecular dynamics simulations and docking studies.Semantic proximity Read ↗

A multiscale in silico approach to impede the interaction between Dengue NS1 and Human RPL18, aiming to suppress the Dengue viral translation and proliferationSemantic proximity Read ↗

Molecular Dynamic Simulation Insights into the Normal State and Restoration of p53 FunctionSemantic proximity Read ↗

Exploring the molecular basis of dsRNA recognition by NS1 protein of influenza A virus using molecular dynamics simulation and free energy calculation.Semantic proximity Read ↗

Molecular dynamics exploration of the binding mechanism and properties of single-walled carbon nanotube to WT and mutant VP35 FBP region of Ebola virus.Semantic proximity Read ↗

Structural and molecular investigation of the impact of S30L and D88N substitutions in G9R protein on coupling with E4R from Monkeypox virus (MPXV).Semantic proximity Read ↗

Theoretical investigations on the effects of mutations in important residues of NS1B on its RNA-binding using molecular dynamics simulations.Semantic proximity Read ↗

Insight into the binding modes of Lassa nucleoprotein complexed with ssRNA by molecular dynamic simulations and free energy calculations.Semantic proximity Read ↗

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