Structure of the Tetramerization Domain of Measles Virus Phosphoprotein - Test2 - elhamkhani - TriplyDB

Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus Computational Docking Study of p7 Ion Channel from HCV Genotype 3 and Genotype 4 and Its Interaction with Natural Compounds Organization, Function, and Therapeutic Targeting of the Morbillivirus RNA-Dependent RNA Polymerase Complex Crystal Structure of the Nipah Virus Phosphoprotein Tetramerization Domain Solution and Crystallographic Structures of the Central Region of the Phosphoprotein from Human Metapneumovirus Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example Structural disorder within paramyxoviral nucleoproteins Routine phasing of coiled-coil protein crystal structures with AMPLE Short self-interacting N-terminal region of rubella virus capsid protein is essential for cooperative actions of capsid and nonstructural p150 proteins.Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Oligomerization of Mumps Virus Phosphoprotein.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.Crystal Structure of the Measles Virus Nucleoprotein Core in Complex with an N-Terminal Region of Phosphoprotein.The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.Crystal Structure of the Marburg Virus VP35 Oligomerization Domain.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.A biomimetic approach to hormone resistant prostate cancer cell isolation using inactivated Sendai virus (HVJ-E).Self-Assembly of Measles Virus Nucleocapsid-like Particles: Kinetics and RNA Sequence Dependence.Inactivated Sendai Virus (HVJ-E) Immobilized Electrospun Nanofiber for Cancer Therapy.Sequence of events in measles virus replication: role of phosphoprotein-nucleocapsid interactions Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function

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P2860

Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

http://www.wikidata.org/entity/Q27677318

description

2013 nî lūn-bûn

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2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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type

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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Journal of Virology

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Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

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P2093

Damien Maurin

http://www.w3.org/2001/XMLSchema#string

Guillaume Communie

http://www.w3.org/2001/XMLSchema#string

Martin Blackledge

http://www.w3.org/2001/XMLSchema#string

Rob W H Ruigrok

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Thibaut Crépin

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P2860

Tetrameric coiled coil domain of Sendai virus phosphoprotein

Buried polar residues in coiled-coil interfaces

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

Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

Molecular replacement with MOLREP

REFMAC5 for the refinement of macromolecular crystal structures

Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7

Features and development of Coot

Identification of four conserved motifs among the RNA-dependent polymerase encoding elements

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7166-9

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scholarly article

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3582028

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10.1128/JVI.00487-13

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12

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87

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Malene Ringkjøbing Jensen

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2013-06-01T00:00:00Z

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23576502

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3676081

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