Structure-Function Analysis of the ϕX174 DNA-Piloting Protein Using Length-Altering Mutations. - Wikidata - awgldk - TriplyDB

Structure-Function Analysis of the ϕX174 DNA-Piloting Protein Using Length-Altering Mutations.

Structure-Function Analysis of the ϕX174 DNA-Piloting Protein Using Length-Altering Mutations.

http://www.wikidata.org/entity/Q37182709

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Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.Breaking Symmetry in Viral Icosahedral Capsids as Seen through the Lenses of X-ray Crystallography and Cryo-Electron Microscopy.

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Structure-Function Analysis of the ϕX174 DNA-Piloting Protein Using Length-Altering Mutations.

http://www.wikidata.org/entity/Q37182709

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 29 June 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Structure-Function Analysis of ...... ing Length-Altering Mutations.

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Structure-Function Analysis of ...... ing Length-Altering Mutations.

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type

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Structure-Function Analysis of ...... ing Length-Altering Mutations.

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Structure-Function Analysis of ...... ing Length-Altering Mutations.

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prefLabel

Structure-Function Analysis of ...... ing Length-Altering Mutations.

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Structure-Function Analysis of ...... ing Length-Altering Mutations.

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Journal of Virology

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Structure-Function Analysis of ...... ing Length-Altering Mutations.

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Aaron P Roznowski

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Bentley A Fane

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P2860

Structural plasticity of helical nanotubes based on coiled-coil assemblies

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

Three-dimensional structure of a viral genome-delivery portal vertex

Icosahedral bacteriophage ΦX174 forms a tail for DNA transport during infection

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

Atomic structure of the degraded procapsid particle of the bacteriophage G4: induced structural changes in the presence of calcium ions and functional implications

Structure of a viral procapsid with molecular scaffolding

In VITRO ASSEMBLY of the øX174 procapsid from external scaffolding protein oligomers and early pentameric assembly intermediates

The lysis protein E of phi X174 is a specific inhibitor of the MraY-catalyzed step in peptidoglycan synthesis.

High-resolution structure of a virally encoded DNA-translocating conduit and the mechanism of DNA penetration.

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7956-7966

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scholarly article

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10.1128/JVI.00914-16

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17

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90

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2016-06-29T00:00:00Z

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27356899

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protein structure

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4988169

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