Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25 - Wikidata - wikimedia - TriplyDB

Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25

Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25

http://www.wikidata.org/entity/Q35180608

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Tegument Assembly and Secondary Envelopment of Alphaherpesviruses Viral and host control of cytomegalovirus maturation The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain.Association of herpes simplex virus pUL31 with capsid vertices and components of the capsid vertex-specific complex.The Primary Enveloped Virion of Herpes Simplex Virus 1: Its Role in Nuclear Egress.Trafficking to uncharted territory of the nuclear envelope Gammaherpesvirus Tegument Protein ORF33 Is Associated With Intranuclear Capsids at an Early Stage of the Tegumentation Process Herpes Simplex Virus 1 Recruits CD98 Heavy Chain and β1 Integrin to the Nuclear Membrane for Viral De-Envelopment Structural basis of membrane budding by the nuclear egress complex of herpesviruses.Interactions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress complex: ORF69 is a potent factor for remodeling cellular membranes The herpes simplex virus 2 UL21 protein is essential for virus propagation Nuclear Exodus: Herpesviruses Lead the Way.The way out: what we know and do not know about herpesvirus nuclear egress.The human cytomegalovirus nuclear egress complex unites multiple functions: Recruitment of effectors, nuclear envelope rearrangement, and docking to nuclear capsids.Characterization of the nuclear import and export signals of pseudorabies virus UL31.Herpes simplex virus 1 UL47 interacts with viral nuclear egress factors UL31, UL34, and Us3 and regulates viral nuclear egress.The Product of the Herpes Simplex Virus 2 UL16 Gene Is Critical for the Egress of Capsids from the Nuclei of Infected Cells.Quantitative Evaluation of Protein Heterogeneity within Herpes Simplex Virus 1 Particles.Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31.A physical link between the pseudorabies virus capsid and the nuclear egress complex.A mutation in the DNA polymerase accessory factor of herpes simplex virus 1 restores viral DNA replication in the presence of raltegravir.Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses.Analysis of the early steps of herpes simplex virus 1 capsid tegumentation.Mapping of sequences in Pseudorabies virus pUL34 that are required for formation and function of the nuclear egress complex.An Epstein-Barr virus mutant produces immunogenic defective particles devoid of viral DNA.Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53.Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdown Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation Structural determinants for nuclear envelope localization and function of pseudorabies virus pUL34.Human Cytomegalovirus pUL93 Links Nucleocapsid Maturation and Nuclear Egress.The Essential Human Cytomegalovirus Proteins pUL77 and pUL93 Are Structural Components Necessary for Viral Genome Encapsidation.Lysine 242 within helix 10 of the pseudorabies virus nuclear egress complex pUL31 component is critical for primary envelopment of nucleocapsids.A Domain of Herpes Simplex Virus pUL33 Required To Release Monomeric Viral Genomes from Cleaved Concatemeric DNA.Herpesvirus Nuclear Egress.The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.Incorporation of the Kaposi's sarcoma-associated herpesvirus capsid vertex-specific component (CVSC) into self-assembled capsids.Herpes Simplex Virus 1 UL34 Protein Regulates the Global Architecture of the Endoplasmic Reticulum in Infected Cells.Vesicular Nucleo-Cytoplasmic Transport-Herpesviruses as Pioneers in Cell Biology.Herpes Simplex Virus Capsid Localization to ESCRT-VPS4 Complexes in the Presence and Absence of the Large Tegument Protein UL36p.Human Cytomegalovirus pUL93 Is Required for Viral Genome Cleavage and Packaging.

P2860

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P2860

Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25

http://www.wikidata.org/entity/Q35180608

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

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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Selection of HSV capsids for e ...... onents pUL31, pUL17, and pUL25

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

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Selection of HSV capsids for e ...... onents pUL31, pUL17, and pUL25

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Joel D Baines

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Kui Yang

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P2860

Evolutionarily conserved herpesviral protein interaction networks

Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34

Herpes simplex virus 1 protein kinase is encoded by open reading frame US3 which is not essential for virus growth in cell culture

Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton.

Role of the UL25 protein in herpes simplex virus DNA encapsidation

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.

Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes.

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