Glycoproteins required for entry are not necessary for egress of pseudorabies virus. - Wikidata - awgldk - TriplyDB

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

http://www.wikidata.org/entity/Q39767140

about

Virion-incorporated glycoprotein B mediates transneuronal spread of pseudorabies virus.Polarized cell migration during cell-to-cell transmission of herpes simplex virus in human skin keratinocytes.Directional transneuronal spread of α-herpesvirus infection.The Primary Enveloped Virion of Herpes Simplex Virus 1: Its Role in Nuclear Egress.The suppression of apoptosis by α-herpesvirus.Herpes simplex virus glycoproteins gB and gD function in a redundant fashion to promote secondary envelopment Proteomic characterization of pseudorabies virus extracellular virions Deletion of the ORF9p acidic cluster impairs the nuclear egress of varicella-zoster virus capsids.Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase.The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cells Nuclear Exodus: Herpesviruses Lead the Way.Herpesvirus transport to the nervous system and back again.Viral serine/threonine protein kinases Herpesviruses remodel host membranes for virus egress.The way out: what we know and do not know about herpesvirus nuclear egress.Integrity of the linker of nucleoskeleton and cytoskeleton is required for efficient herpesvirus nuclear egress.Functional Relevance of the N-Terminal Domain of Pseudorabies Virus Envelope Glycoprotein H and Its Interaction with Glycoprotein L.Multiple Roles of the Cytoplasmic Domain of Herpes Simplex Virus 1 Envelope Glycoprotein D in Infected Cells.Mutations in Pseudorabies Virus Glycoproteins gB, gD, and gH Functionally Compensate for the Absence of gL.Functional Characterization of Glycoprotein H Chimeras Composed of Conserved Domains of the Pseudorabies Virus and Herpes Simplex Virus 1 Homologs.Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.The highly conserved proline at position 438 in pseudorabies virus gH is important for regulation of membrane fusion.A physical link between the pseudorabies virus capsid and the nuclear egress complex.Nuclear envelope breakdown induced by herpes simplex virus type 1 involves the activity of viral fusion proteins.Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses.Glycoproteins gB and gH are required for syncytium formation but not for herpesvirus-induced nuclear envelope breakdown.Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Structural determinants for nuclear envelope localization and function of pseudorabies virus pUL34.Nuclear envelope breakdown can substitute for primary envelopment-mediated nuclear egress of herpesviruses.Primary B-cell infection with a deltaBALF4 Epstein-Barr virus comes to a halt in the endosomal compartment yet still elicits a potent CD4-positive cytotoxic T-cell response.Herpesvirus Nuclear Egress.Herpes simplex virus Membrane Fusion.Vesicular Nucleo-Cytoplasmic Transport-Herpesviruses as Pioneers in Cell Biology.Alternative nuclear transport for cellular protein quality control Early, active, and specific localization of herpes simplex virus type 1 gM to nuclear membranes Functional role of N-linked glycosylation in pseudorabies virus glycoprotein gH.Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.

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P2860

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

http://www.wikidata.org/entity/Q39767140

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

@wuu

2008年学术文章

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2008年学术文章

@zh-hans

2008年学术文章

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh

2008年學術文章

@zh-hant

name

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@en

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@nl

type

label

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@en

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@nl

prefLabel

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@en

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@nl

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Journal of Virology

P1476

Glycoproteins required for entry are not necessary for egress of pseudorabies virus.

@en

P2093

Barbara Klupp

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Harald Granzow

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Jan Altenschmidt

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Walter Fuchs

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P2860

The protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown

Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment --> deenvelopment --> reenvelopment pathway

Egress of alphaherpesviruses: comparative ultrastructural study

Viral and developmental cell fusion mechanisms: conservation and divergence

Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

Karyopherin-mediated import of integral inner nuclear membrane proteins.

Herpesvirus assembly: a tale of two membranes

Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter

Electron tomography of nascent herpes simplex virus virions

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6299-6309

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10.1128/JVI.00386-08

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13

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82

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Thomas Mettenleiter

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2008-04-16T00:00:00Z

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18417564

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