Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein - Test2 - elhamkhani - TriplyDB

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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The polymerase of negative-stranded RNA viruses Structure of the Tetramerization Domain of Measles Virus Phosphoprotein Structural and Functional Characterization of the Mumps Virus Phosphoprotein Structure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus Phosphoprotein Crystal Structure of the Nipah Virus Phosphoprotein Tetramerization Domain Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example Against the odds? De novo structure determination of a pilin with two cysteine residues by sulfur SAD.Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus Focal adhesion kinase is involved in rabies virus infection through its interaction with viral phosphoprotein P Growth signalobody selects functional intrabodies in the mammalian cytoplasm.Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds A novel nuclear trafficking module regulates the nucleocytoplasmic localization of the rabies virus interferon antagonist, P protein Oligomerization of Mumps Virus Phosphoprotein.Quantitative Analysis of the Microtubule Interaction of Rabies Virus P3 Protein: Roles in Immune Evasion and Pathogenesis.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins.RNA synthetic mechanisms employed by diverse families of RNA viruses.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.An In Vitro RNA Synthesis Assay for Rabies Virus Defines Ribonucleoprotein Interactions Critical for Polymerase Activity Negri bodies are viral factories with properties of liquid organelles.Prokaryotic Expression, Purification, and Polyclonal Antibody Production of a Truncated Recombinant Rabies Virus L Protein.Asymmetric packaging of polymerases within vesicular stomatitis virus.

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P2860

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

http://www.wikidata.org/entity/Q27659060

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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type

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Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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prefLabel

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

@en

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

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Journal of Virology

P1476

Structure of the dimerization domain of the rabies virus phosphoprotein

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Ivan Ivanov

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Marc Jamin

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Rob W H Ruigrok

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P2860

The FoldX web server: an online force field

Tetrameric coiled coil domain of Sendai virus phosphoprotein

Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein

Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution

Solution structure of the C-terminal nucleoprotein-RNA binding domain of the vesicular stomatitis virus phosphoprotein

Automated protein model building combined with iterative structure refinement

Refinement of macromolecular structures by the maximum-likelihood method

An approach to multi-copy search in molecular replacement

Auto-rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment

Location of the binding domains for the RNA polymerase L and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus.

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10.1128/JVI.02557-09

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7

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84

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Thibaut Crépin

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2010-01-20T00:00:00Z

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20089657

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