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.
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Fuzzy complexes: Specific binding without complete foldingInteraction between the C-terminal domains of N and P proteins of measles virus investigated by NMRHost-Pathogen Interactions in Measles Virus Replication and Anti-Viral ImmunityStructural disorder within paramyxoviral nucleoproteinsComparison of the immune responses induced by chimeric alphavirus-vectored and formalin-inactivated alum-precipitated measles vaccines in miceFunctional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings.Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.Conformational analysis of the partially disordered measles virus N(TAIL)-XD complex by SDSL EPR spectroscopy.ff14IDPs force field improving the conformation sampling of intrinsically disordered proteins.Expression of measles virus nucleoprotein induces apoptosis and modulates diverse functional proteins in cultured mammalian cellsRecognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain.Probing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteinesOne-step generation of error-prone PCR libraries using Gateway® technology.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 HenipavirusIntrinsic disorder mediates hepatitis C virus core-host cell protein interactions.hsp72, a host determinant of measles virus neurovirulenceDividing to unveil protein microheterogeneities: traveling wave ion mobility studyPlasticity 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.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins.Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrilsA self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.Predicting intrinsic disorder in proteins: an overview.Protein intrinsic disorder and oligomericity in cell signaling.Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins.Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering.How random are intrinsically disordered proteins? A small angle scattering perspective.Interactions via intrinsically disordered regions: what kind of motifs?Bridging the past and the future of virology: surface plasmon resonance as a powerful tool to investigate virus/host interactions.Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Newly identified minor phosphorylation site threonine-279 of measles virus nucleoprotein is a prerequisite for nucleocapsid formation.FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies.
P2860
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P2860
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.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
The intrinsically disordered C ...... emains predominantly unfolded.
@ast
The intrinsically disordered C ...... emains predominantly unfolded.
@en
type
label
The intrinsically disordered C ...... emains predominantly unfolded.
@ast
The intrinsically disordered C ...... emains predominantly unfolded.
@en
altLabel
The intrinsically disordered C ...... remains predominantly unfolded
@en
prefLabel
The intrinsically disordered C ...... emains predominantly unfolded.
@ast
The intrinsically disordered C ...... emains predominantly unfolded.
@en
P2093
P2860
P50
P356
P1433
P1476
The intrinsically disordered C ...... emains predominantly unfolded.
@en
P2093
Hervé Darbon
Matthew Buccellato
Michael Oglesbee
Sonia Longhi
Stéphanie Finet
Véronique Receveur-Bréchot
Xinsheng Zhang
P2860
P304
P356
10.1110/PS.051411805
P407
P577
2005-08-01T00:00:00Z