Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site.
about
Rhabdovirus Matrix Protein Structures Reveal a Novel Mode of Self-AssociationCrystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding propertiesStructure of the Nucleoprotein Binding Domain of Mokola Virus PhosphoproteinThe 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings.Cloning and expression of fragment of the rabies virus nucleoprotein gene in Escherichia coli and evaluation of antigenicity of the expression product.Purification and characterization of Nipah virus nucleocapsid protein produced in insect cells.A bioinformatics approach to the structure, function, and evolution of the nucleoprotein of the order mononegavirales.Oligomerization of Mumps Virus Phosphoprotein.Interaction of vesicular stomatitis virus P and N proteins: identification of two overlapping domains at the N terminus of P that are involved in N0-P complex formation and encapsidation of viral genome RNA.Genetic and evolutionary characterization of RABVs from China using the phosphoprotein gene.Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains.Structural and functional properties of the vesicular stomatitis virus nucleoprotein-RNA complex as revealed by proteolytic digestion.Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity.Asymmetric Trimeric Ring Structure of the Nucleocapsid Protein of Tospovirus.Identification of very small open reading frames in the genomes of Holmes Jungle virus, Ord River virus, and Wongabel virus of the genus Hapavirus, family Rhabdoviridae.Structural difference recognized by a monoclonal antibody #404-11 between the rabies virus nucleocapsid (NC) produced in virus infected cells and the NC-like structures produced in the nucleoprotein (N) cDNA-transfected cells.Oligomerization of Hantavirus N protein: C-terminal alpha-helices interact to form a shared hydrophobic space.The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein.
P2860
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P2860
Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
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2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structure of recombinant rabie ...... e phosphoprotein binding site.
@ast
Structure of recombinant rabie ...... e phosphoprotein binding site.
@en
type
label
Structure of recombinant rabie ...... e phosphoprotein binding site.
@ast
Structure of recombinant rabie ...... e phosphoprotein binding site.
@en
prefLabel
Structure of recombinant rabie ...... e phosphoprotein binding site.
@ast
Structure of recombinant rabie ...... e phosphoprotein binding site.
@en
P2093
P2860
P1433
P1476
Structure of recombinant rabie ...... he phosphoprotein binding site
@en
P2093
P2860
P304
P356
10.1128/JVI.75.1.490-498.2001
P50
P577
2001-01-01T00:00:00Z