Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus
about
Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virusFuzzy complexes: Specific binding without complete foldingProtein domain definition should allow for conditional disorderCrystal Structure of the Nipah Virus Phosphoprotein Tetramerization DomainExploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.Structural disorder within paramyxoviral nucleoproteinsConditionally disordered proteins: bringing the environment back into the fold.Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe.Fuzziness endows viral motif-mimicry.The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1.Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy.Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy.Interfacial Properties of NTAIL, an Intrinsically Disordered Protein.Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V.The Unstructured Paramyxovirus Nucleocapsid Protein Tail Domain Modulates Viral Pathogenesis through Regulation of Transcriptase Activity.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.
P2860
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P2860
Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus
description
2011 nî lūn-bûn
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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Characterization of the intera ...... phosphoprotein of Henipavirus
@ast
Characterization of the intera ...... phosphoprotein of Henipavirus
@en
Characterization of the intera ...... phosphoprotein of Henipavirus
@nl
type
label
Characterization of the intera ...... phosphoprotein of Henipavirus
@ast
Characterization of the intera ...... phosphoprotein of Henipavirus
@en
Characterization of the intera ...... phosphoprotein of Henipavirus
@nl
prefLabel
Characterization of the intera ...... phosphoprotein of Henipavirus
@ast
Characterization of the intera ...... phosphoprotein of Henipavirus
@en
Characterization of the intera ...... phosphoprotein of Henipavirus
@nl
P2093
P2860
P356
P1476
Characterization of the intera ...... phosphoprotein of Henipavirus
@en
P2093
Hervé Darbon
Johnny Habchi
Laurent Mamelli
Martin Blackledge
Michael Oglesbee
Sonia Longhi
Stéphanie Blangy
Yaoling Shu
P2860
P304
13583-13602
P356
10.1074/JBC.M111.219857
P407
P577
2011-02-11T00:00:00Z