Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
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Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virusOrganization, Function, and Therapeutic Targeting of the Morbillivirus RNA-Dependent RNA Polymerase ComplexHost-Pathogen Interactions in Measles Virus Replication and Anti-Viral ImmunityStructural disorder within paramyxoviral nucleoproteinsThe 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings.Biological heterogeneity of the peptide-binding motif of the 70-kDa heat shock protein by surface plasmon resonance analysis.Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.Expression of measles virus nucleoprotein induces apoptosis and modulates diverse functional proteins in cultured mammalian cellsThe C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction.A single codon in the nucleocapsid protein C terminus contributes to in vitro and in vivo fitness of Edmonston measles virus.Characterization of the interactions between the nucleoprotein and the phosphoprotein of HenipavirusInteractome analysis of the human respiratory syncytial virus RNA polymerase complex identifies protein chaperones as important cofactors that promote L-protein stability and RNA synthesisIntrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Insights into the regulatory mechanism controlling the inhibition of vaccine-induced seroconversion by maternal antibodies.hsp72, a host determinant of measles virus neurovirulenceThe dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcriptionPlasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.hsp70 and a novel axis of type I interferon-dependent antiviral immunity in the measles virus-infected brain.Major histocompatibility complex haplotype determines hsp70-dependent protection against measles virus neurovirulenceThe measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.Heat shock protein 70 enhances mucosal immunity against human norovirus when coexpressed from a vesicular stomatitis virus vector.Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Hsp70 protein positively regulates rabies virus infection.Determination of a phosphorylation site in Nipah virus nucleoprotein and its involvement in virus transcriptionMeasles virus neurovirulence and host immunity.The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment.Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.Peroxiredoxin 1 is required for efficient transcription and replication of measles virusNucleoprotein-RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy.An amino acid of human parainfluenza virus type 3 nucleoprotein is critical for template function and cytoplasmic inclusion body formation.Upon Infection the Cellular WD Repeat-containing Protein 5 (WDR5) Localizes to Cytoplasmic Inclusion Bodies and Enhances Measles Virus Replication.Measles virus: Background and oncolytic virotherapy.The Unstructured Paramyxovirus Nucleocapsid Protein Tail Domain Modulates Viral Pathogenesis through Regulation of Transcriptase Activity.How disorder influences order and vice versa--mutual effects in fusion proteins containing an intrinsically disordered and a globular protein.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.
P2860
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P2860
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
description
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2005
@ast
im Juni 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 2005/06/20)
@nl
наукова стаття, опублікована в червні 2005
@uk
مقالة علمية (نشرت في 20-6-2005)
@ar
name
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@ast
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@en
type
label
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@ast
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@en
prefLabel
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@ast
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@en
P2093
P921
P3181
P1433
P1476
Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
@en
P2093
Benjamin Morin
Matthew Buccellato
Michael Oglesbee
Sonia Longhi
Thomas Carsillo
Xinsheng Zhang
P304
P3181
P356
10.1016/J.VIROL.2005.03.035
P407
P577
2005-06-20T00:00:00Z