Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteins.
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Structure of the Nucleocapsid-Binding Domain from the Mumps Virus Polymerase; an Example of Protein Folding Induced by CrystallizationStructural Basis for the Interaction of Unstructured Neuron Specific Substrates Neuromodulin and Neurogranin with CalmodulinStructural and Functional Characterization of the Mumps Virus PhosphoproteinProtein domain definition should allow for conditional disorderStructural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsidStructural disorder within paramyxoviral nucleoproteinsConditionally disordered proteins: bringing the environment back into the fold.Mapping of the VP40-binding regions of the nucleoprotein of Ebola virus.Characterization of a mumps virus nucleocapsidlike particleProbing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteinesThe C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction.Functional mapping of the nucleoprotein of Ebola virus.Characterization of the interactions between the nucleoprotein and the phosphoprotein of HenipavirusIntrinsic disorder in measles virus nucleocapsids.hsp72, a host determinant of measles virus neurovirulenceRoles of Phosphorylation of the Nucleocapsid Protein of Mumps Virus in Regulating Viral RNA Transcription and Replication.Identification of mumps virus protein and lipid composition by mass spectrometry.Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Characterization of a viral phosphoprotein binding site on the surface of the respiratory syncytial nucleoprotein.Oligomerization of Mumps Virus Phosphoprotein.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.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.Linkers in the structural biology of protein-protein interactionsThe 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.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics.Heat Shock Protein 90 Ensures Efficient Mumps Virus Replication by Assisting with Viral Polymerase Complex Formation.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Structure-guided design of small-molecule therapeutics against RSV disease.C-Terminal DxD-Containing Sequences within Paramyxovirus Nucleocapsid Proteins Determine Matrix Protein Compatibility and Can Direct Foreign Proteins into Budding Particles.The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein.The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment.Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoproteinThe feet of the measles virus polymerase bind the viral nucleocapsid protein at a single site.Identification and functional analysis of phosphorylation in Newcastle disease virus phosphoprotein.Noctilisin, a Venom Glycopeptide of Sirex noctilio (Hymenoptera: Siricidae), Causes Needle Wilt and Defense Gene Responses in Pines.Peroxiredoxin 1 is required for efficient transcription and replication of measles virusNucleoprotein-RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy.Insights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR.
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P2860
Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteins.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Characterization of nucleocaps ...... d mumps virus phosphoproteins.
@en
type
label
Characterization of nucleocaps ...... d mumps virus phosphoproteins.
@en
prefLabel
Characterization of nucleocaps ...... d mumps virus phosphoproteins.
@en
P2093
P2860
P1433
P1476
Characterization of nucleocaps ...... d mumps virus phosphoproteins.
@en
P2093
Leslie S Gay
Richard L Kingston
Walter A Baase
P2860
P304
P356
10.1128/JVI.78.16.8630-8640.2004
P407
P577
2004-08-01T00:00:00Z