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

The μ1 72-96 loop controls conformational transitions during reovirus cell entry.

Journal of virology - 1 Dec 2013

Sarkar Payel, Danthi Pranav

Abstract excerpt

The reovirus outer capsid protein μ1 forms a lattice surrounding the viral core. In the native state, μ1 determines the environmental stability of the viral capsid. Additionally, during cell entry, μ1 undergoes structural rearrangements that facilitate delivery of the viral cores across the membrane. To determine how the capsid-stabilizing functions of μ1 impinge on the capacity of μ1 to undergo conformational...

Read the complete abstract on PubMed

Topics

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

Share to Capsid
Share to Capsid Proteins
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallization

Share to Protein Conformation

Share to Reoviridae

Share to Reoviridae Infections

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 24089575
DOI: 10.1128/JVI.01899-13
PMCID: PMC3838289

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The μ1 72-96 loop controls conformational transitions during reovirus cell entry.PMID 24089575Read ↗

Reovirus Core Proteins λ1 and σ2 Promote Stability of Disassembly Intermediates and Influence Early Replication Events.Semantic proximity Read ↗

Reovirus σ1 Conformational Flexibility Modulates the Efficiency of Host Cell Attachment.Semantic proximity Read ↗

Optimum length and flexibility of reovirus attachment protein σ1 are required for efficient viral infection.Semantic proximity Read ↗

Thermostabilizing mutations in reovirus outer-capsid protein mu1 selected by heat inactivation of infectious subvirion particles.Semantic proximity Read ↗

Reovirus μ1 Protein Affects Infectivity by Altering Virus-Receptor InteractionsSemantic proximity Read ↗

Thermolabilizing pseudoreversions in reovirus outer-capsid protein micro 1 rescue the entry defect conferred by a thermostabilizing mutation.Semantic proximity Read ↗

Reovirus core protein mu2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules.Semantic proximity Read ↗

Reovirus replication protein μ2 influences cell tropism by promoting particle assembly within viral inclusions.Semantic proximity Read ↗

The reovirus mutant tsA279 has temperature-sensitive lesions in the M2 and L2 genes: the M2 gene is associated with decreased viral protein production and blockade in transmembrane transport.Semantic proximity Read ↗

The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change.Semantic proximity Read ↗

Reovirus mu2 protein determines strain-specific differences in the rate of viral inclusion formation in L929 cells.Semantic proximity Read ↗

Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus.Semantic proximity Read ↗

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