Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.
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Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virusSolution and Crystallographic Structures of the Central Region of the Phosphoprotein from Human MetapneumovirusCoiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative exampleStructure of Nipah virus unassembled nucleoprotein in complex with its viral chaperoneStructural disorder within paramyxoviral nucleoproteinsInherent structural disorder and dimerisation of murine norovirus NS1-2 protein.Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteinsCharacterization of the interactions between the nucleoprotein and the phosphoprotein of HenipavirusEvolution and structural organization of the C proteins of paramyxovirinae.Plasticity 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.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins.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.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.Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein.Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V.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
Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural disorder within Hen ...... ns to experimental assessment.
@ast
Structural disorder within Hen ...... ns to experimental assessment.
@en
type
label
Structural disorder within Hen ...... ns to experimental assessment.
@ast
Structural disorder within Hen ...... ns to experimental assessment.
@en
prefLabel
Structural disorder within Hen ...... ns to experimental assessment.
@ast
Structural disorder within Hen ...... ns to experimental assessment.
@en
P2093
P2860
P1433
P1476
Structural disorder within Hen ...... ns to experimental assessment.
@en
P2093
Hervé Darbon
Johnny Habchi
Laurent Mamelli
Sonia Longhi
P2860
P304
P356
10.1371/JOURNAL.PONE.0011684
P407
P577
2010-07-21T00:00:00Z