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

Plasticity in Structural and Functional Interactions between the Phosphoprotein and Nucleoprotein of Measles Virus

9 Feb 2012

Abstract excerpt

The measles virus (MeV) phosphoprotein (P) tethers the polymerase to the nucleocapsid template for transcription and genome replication. Binding of P to nucleocapsid is mediated by the X domain of P (XD) and a conserved sequence (Box-2) within the C-terminal domain of the nucleoprotein (N(TAIL)). XD binding induces N(TAIL) α-helical folding, which in turn has been proposed to stabilize the polymerase-nucleocapsid...

Read the complete abstract on PubMed

Topics

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

Share to Viral Infections and Immunology Research
Share to Virology and Viral Diseases
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22318731
DOI: 10.1074/jbc.m111.333088

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Plasticity in Structural and Functional Interactions between the Phosphoprotein and Nucleoprotein of Measles VirusPMID 22318731Read ↗

Sequence of Events in Measles Virus Replication: Role of Phosphoprotein-Nucleocapsid InteractionsSemantic proximity Read ↗

The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.Semantic proximity Read ↗

Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding StrengthSemantic proximity Read ↗

Regulation of measles virus gene expression by P protein coiled-coil propertiesSemantic proximity Read ↗

Intrinsic disorder in measles virus nucleocapsidsSemantic proximity Read ↗

Structures of the measles virus polymerase complex with non-nucleoside inhibitors and mechanism of inhibitionSemantic proximity Read ↗

Structure of the measles virus ternary polymerase complexSemantic proximity Read ↗

The C Protein Is Recruited to Measles Virus Ribonucleocapsids by the PhosphoproteinSemantic proximity Read ↗

Structural and Functional Characterization of the Mumps Virus PhosphoproteinSemantic proximity Read ↗

The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradientSemantic proximity Read ↗

Cyclical adaptation of measles virus quasispecies to epithelial and lymphocytic cells: To V, or not to VSemantic proximity Read ↗

Functional benefit of structural disorder for the replication of measles, Nipah and Hendra virusesSemantic proximity Read ↗

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