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

High-Resolution X-Ray Structure and Functional Analysis of the Murine Norovirus 1 Capsid Protein Protruding Domain

25 Mar 2010

Abstract excerpt

Murine noroviruses (MNV) are closely related to the human noroviruses (HuNoV), which cause the majority of nonbacterial gastroenteritis. Unlike HuNoV, MNV grow in culture and in a small-animal model that represents a tractable model to study norovirus biology. To begin a detailed investigation of molecular events that occur during norovirus binding to cells, the crystallographic structure of the murine norovirus...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to Viral gastroenteritis research and epidemiology
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20335262
DOI: 10.1128/jvi.00316-10

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High-Resolution X-Ray Structure and Functional Analysis of the Murine Norovirus 1 Capsid Protein Protruding DomainPMID 20335262Read ↗

Atomic Structure of the Murine Norovirus Protruding Domain and Soluble CD300lf Receptor ComplexSemantic proximity Read ↗

Protruding Domain of Capsid Protein Is Necessary and Sufficient To Determine Murine Norovirus Replication and Pathogenesis <i>In Vivo</i>Semantic proximity Read ↗

Dynamic rotation of the protruding domain enhances the infectivity of norovirusSemantic proximity Read ↗

High-Resolution Cryo-EM Reveals Dynamics in the Murine Norovirus CapsidSemantic proximity Read ↗

Noroviruses—The State of the Art, Nearly Fifty Years after Their Initial DiscoverySemantic proximity Read ↗

Structure of Antibody-Neutralized Murine Norovirus and Unexpected Differences from Viruslike ParticlesSemantic proximity Read ↗

A single-amino-acid substitution in the P2 domain of VP1 of murine norovirus is sufficient for escape from antibody neutralization.Semantic proximity Read ↗

Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM.Semantic proximity Read ↗

Conformational plasticity of the human norovirus GII.3 capsid reveals alternative P domain interaction networksSemantic proximity Read ↗

Environmentally-triggered contraction of the norovirus virion determines diarrheagenic potentialSemantic proximity Read ↗

Amino acid substitutions in norovirus VP1 dictate cell tropism via an attachment process dependent on membrane mobilitySemantic proximity Read ↗

Discovery of a proteinaceous cellular receptor for a norovirusSemantic proximity Read ↗

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