Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions. - Wikidata - awgldk - TriplyDB

Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.

Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.

http://www.wikidata.org/entity/Q35518621

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Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Cryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end Organization, Function, and Therapeutic Targeting of the Morbillivirus RNA-Dependent RNA Polymerase Complex Structure and assembly of a paramyxovirus matrix protein Perspective on Global Measles Epidemiology and Control and the Role of Novel Vaccination Strategies Intracellular transport of the measles virus ribonucleoprotein complex is mediated by Rab11A-positive recycling endosomes and drives virus release from the apical membrane of polarized epithelial cells.Architecture of respiratory syncytial virus revealed by electron cryotomography.Structural analysis of respiratory syncytial virus reveals the position of M2-1 between the matrix protein and the ribonucleoprotein complex Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein Multiple origins of viral capsid proteins from cellular ancestors Detailed morphological characterisation of Hendra virus infection of different cell types using super-resolution and conventional imaging.Electron tomography imaging of surface glycoproteins on human parainfluenza virus 3: association of receptor binding and fusion proteins before receptor engagement Averaging of viral envelope glycoprotein spikes from electron cryotomography reconstructions using Jsubtomo Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Receptor-Targeted Nipah Virus Glycoproteins Improve Cell-Type Selective Gene Delivery and Reveal a Preference for Membrane-Proximal Cell Attachment.Base of the measles virus fusion trimer head receives the signal that triggers membrane fusion.Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.Crystal Structure of the Measles Virus Nucleoprotein Core in Complex with an N-Terminal Region of Phosphoprotein.Measles virus nonstructural C protein modulates viral RNA polymerase activity by interacting with host protein SHCBP1 The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.Membrane dynamics and interactions in measles virus dendritic cell infections.Dimerization Efficiency of Canine Distemper Virus Matrix Protein Regulates Membrane-Budding Activity.The Density Code for the Development of a Vaccine?A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.Structure and organization of paramyxovirus particles.Capturing enveloped viruses on affinity grids for downstream cryo-electron microscopy applications.Structural analysis of the complex between influenza B nucleoprotein and human importin-α.Dissection of epitope-specific mechanisms of neutralization of influenza virus by intact IgG and Fab fragments.Ultrastructural features of PPRV infection in Vero cells.Promotion of virus assembly and organization by the measles virus matrix protein.The Near-to-Native-State Architecture of Measles Virus Assembly Sites and Isolated Measles Virus Particles

P2860

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P2860

Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.

http://www.wikidata.org/entity/Q35518621

description

2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Electron cryotomography of mea ...... ocapsid within intact virions.

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Electron cryotomography of mea ...... ocapsid within intact virions.

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Electron cryotomography of mea ...... ocapsid within intact virions.

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Electron cryotomography of mea ...... ocapsid within intact virions.

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Electron cryotomography of mea ...... ocapsid within intact virions.

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Electron cryotomography of mea ...... ocapsid within intact virions.

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PNAS.1105770108

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Proceedings of the National Academy of Sciences of the United States of America

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Electron cryotomography of mea ...... ocapsid within intact virions.

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P2093

Ari Ora

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

Lassi Liljeroos

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Sarah J Butcher

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P2860

High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells

Chimeric measles viruses with a foreign envelope

A matrix-less measles virus is infectious and elicits extensive cell fusion: consequences for propagation in the brain.

Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR

Influence of lipids on the interfacial disposition of respiratory syncytical virus matrix protein

Automated electron microscope tomography using robust prediction of specimen movements

Structural basis for the attachment of a paramyxoviral polymerase to its template.

Transcription inhibition and other properties of matrix proteins expressed by M genes cloned from measles viruses and diseased human brain tissue.

Paramyxovirus ultrastructure and genome packaging: cryo-electron tomography of sendai virus.

Structural organization of a filamentous influenza A virus.

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18085-18090

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44

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Juha T Huiskonen

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