Role of the UL25 protein in herpes simplex virus DNA encapsidation - Wikidata - thesis-toulmin - TriplyDB

Role of the UL25 protein in herpes simplex virus DNA encapsidation

Role of the UL25 protein in herpes simplex virus DNA encapsidation

http://www.wikidata.org/entity/Q30439328

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Fluorescent Protein Approaches in Alpha Herpesvirus Research A "coiled-coil" motif is important for oligomerization and DNA binding properties of human cytomegalovirus protein UL77 Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.Uncoupling uncoating of herpes simplex virus genomes from their nuclear import and gene expression.Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton.Murine cytomegalovirus capsid assembly is dependent on US22 family gene M140 in infected macrophages Association of herpes simplex virus pUL31 with capsid vertices and components of the capsid vertex-specific complex.Organization of capsid-associated tegument components in Kaposi's sarcoma-associated herpesvirus Visualizing Herpesvirus Procapsids in Living Cells Major capsid reinforcement by a minor protein in herpesviruses and phage.Isolation and characterization of the herpes simplex virus 1 terminase complex.Residues of the UL25 protein of herpes simplex virus that are required for its stable interaction with capsids The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention.A modified screening system for loss-of-function and dominant negative alleles of essential MCMV genes.Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25 Fusion of a fluorescent protein to the pUL25 minor capsid protein of pseudorabies virus allows live-cell capsid imaging with negligible impact on infection.Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions.Vertex-Specific Proteins pUL17 and pUL25 Mechanically Reinforce Herpes Simplex Virus Capsids.The C Terminus of the Herpes Simplex Virus UL25 Protein Is Required for Release of Viral Genomes from Capsids Bound to Nuclear Pores.The human cytomegalovirus UL51 protein is essential for viral genome cleavage-packaging and interacts with the terminase subunits pUL56 and pUL89.Involvement of the N-Terminal Deubiquitinating Protease Domain of Human Cytomegalovirus UL48 Tegument Protein in Autoubiquitination, Virion Stability, and Virus Entry.Phosphorylation of Bovine Herpesvirus 1 VP8 Plays a Role in Viral DNA Encapsidation and Is Essential for Its Cytoplasmic Localization and Optimal Virion Incorporation.Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins.Dominant-negative proteins in herpesviruses - from assigning gene function to intracellular immunization.Herpes Simplex Virus 1 Small Capsomere-Interacting Protein VP26 Regulates Nucleocapsid Maturation.A mutation in UL15 of herpes simplex virus 1 that reduces packaging of cleaved genomes.Analysis of the early steps of herpes simplex virus 1 capsid tegumentation.Herpesvirus Capsid Assembly and DNA Packaging.Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation Mutational analysis of the herpes simplex virus type 1 UL25 DNA packaging protein reveals regions that are important after the viral DNA has been packaged.Effects of major capsid proteins, capsid assembly, and DNA cleavage/packaging on the pUL17/pUL25 complex of herpes simplex virus 1.Characterization of pseudorabies virus (PrV) cleavage-encapsidation proteins and functional complementation of PrV pUL32 by the homologous protein of herpes simplex virus type 1.The Essential Human Cytomegalovirus Proteins pUL77 and pUL93 Are Structural Components Necessary for Viral Genome Encapsidation.A Domain of Herpes Simplex Virus pUL33 Required To Release Monomeric Viral Genomes from Cleaved Concatemeric DNA.Intracellular Distribution of Capsid-Associated pUL77 of Human Cytomegalovirus and Interactions with Packaging Proteins and pUL93.A pUL25 dimer interfaces the pseudorabies virus capsid and tegument.

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P2860

Role of the UL25 protein in herpes simplex virus DNA encapsidation

http://www.wikidata.org/entity/Q30439328

description

2008 nî lūn-bûn

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2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Journal of Virology

P1476

Role of the UL25 protein in herpes simplex virus DNA encapsidation

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Fred L Homa

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Minerva E Sanchez

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Shelley K Cockrell

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P2860

A generic protein purification method for protein complex characterization and proteome exploration

Inhibition of human cytomegalovirus DNA maturation by a benzimidazole ribonucleoside is mediated through the UL89 gene product

Resistance of human cytomegalovirus to benzimidazole ribonucleosides maps to two open reading frames: UL89 and UL56

Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus

Herpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the vertices

Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids.

The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA.

Herpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to its maturation.

The herpes simplex virus type 1 cleavage/packaging protein, UL32, is involved in efficient localization of capsids to replication compartments

ATP depletion blocks herpes simplex virus DNA packaging and capsid maturation

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10.1128/JVI.01889-08

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1

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