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

Divalent cation-induced conformational changes of influenza virus hemagglutinin.

Scientific reports - 22 Sept 2020

Seok Jong Hyeon, Kim Hyojin, Lee Dan Bi, An Jeong Suk, Kim Eun Jeong, Lee Ji-Hye, Chung Mi Sook, Kim Kyung Hyun

Abstract excerpt

Divalent cations Cu2+ and Zn2+ can prevent the viral growth in mammalian cells during influenza infection, and viral titers decrease significantly on a copper surface. The underlying mechanisms include DNA damage by radicals, modulation of viral protease, M1 or neuraminidase, and morphological changes in viral particles. However, the molecular mechanisms underlying divalent cation-mediated antiviral activities...

Read the complete abstract on PubMed

Topics

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

Share to Cations, Divalent
Share to Hemagglutinin Glycoproteins, Influenza Virus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Models, Molecular

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 32963316
DOI: 10.1038/s41598-020-72368-x
PMCID: PMC7508890

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Divalent cation-induced conformational changes of influenza virus hemagglutinin.PMID 32963316Read ↗

Strong and heterogeneous adsorption of infectious bursal disease VP2 subviral particle with immobilized metal ions dependent on two surface histidine residues.Semantic proximity Read ↗

Metal-Protein Nanoparticles Facilitate Anti-VSV and H1N1 Viruses Through the Coordinative Actions on Innate Immune Responses and METTL14.Semantic proximity Read ↗

A single amino acid in VP2 is critical for the attachment of infectious bursal disease subviral particles to immobilized metal ions and DF-1 cells.Semantic proximity Read ↗

Retroviral nucleocapsid protein-metal ion interactions: folding and sequence variants.Semantic proximity Read ↗

Role of Zn <sup>2+</sup> Ions in Host-Virus InteractionsSemantic proximity Read ↗

The relevance of salt bridges for the stability of the influenza virus hemagglutinin.Semantic proximity Read ↗

Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease.Semantic proximity Read ↗

Mn<sup>2+</sup> Mediated Antiviral Activity Through Both the cGAS-STING -IFN and ROS-Apoptosis Pathways in Porcine Alveolar Macrophage CellsSemantic proximity Read ↗

Manganese Enhances DNA- or RNA-Mediated Innate Immune Response by Inducing Phosphorylation of TANK-Binding Kinase 1Semantic proximity Read ↗

The NS5A protein of hepatitis C virus is a zinc metalloprotein.Semantic proximity Read ↗

Zinc <sup>2+</sup> ion inhibits SARS-CoV-2 main protease and viral replication <i>in vitro</i>Semantic proximity Read ↗

Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.Semantic proximity Read ↗

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