Membrane deformation and scission by the HSV-1 nuclear egress complex.
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The ESCRT machinery: new roles at new holesThe Great (Nuclear) Escape: New Insights into the Role of the Nuclear Egress Complex of HerpesvirusesThe Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain.The Primary Enveloped Virion of Herpes Simplex Virus 1: Its Role in Nuclear Egress.Chromatin organization regulates viral egress dynamics.Herpes Simplex Virus 1 Recruits CD98 Heavy Chain and β1 Integrin to the Nuclear Membrane for Viral De-EnvelopmentStructural Basis of Vesicle Formation at the Inner Nuclear Membrane.Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication.Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear EgressThe Prolyl Isomerase Pin1 Promotes the Herpesvirus-Induced Phosphorylation-Dependent Disassembly of the Nuclear Lamina Required for Nucleocytoplasmic EgressHerpes Simplex Virus Capsid-Organelle Association in the Absence of the Large Tegument Protein UL36pStructural basis of membrane budding by the nuclear egress complex of herpesviruses.Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complexCrystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane RemodelingCharacterization of a Herpes Simplex Virus 1 (HSV-1) Chimera in Which the Us3 Protein Kinase Gene Is Replaced with the HSV-2 Us3 Gene.A Role for Nuclear F-Actin Induction in Human Cytomegalovirus Nuclear EgressNuclear Exodus: Herpesviruses Lead the Way.The human cytomegalovirus nuclear egress complex unites multiple functions: Recruitment of effectors, nuclear envelope rearrangement, and docking to nuclear capsids.Multiple Roles of the Cytoplasmic Domain of Herpes Simplex Virus 1 Envelope Glycoprotein D in Infected Cells.Human Cytomegalovirus nuclear egress and secondary envelopment are negatively affected in the absence of cellular p53.This bud's for you: mechanisms of cellular nucleocytoplasmic trafficking via nuclear envelope budding.Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31.Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses.Getting to and through the inner nuclear membrane during herpesvirus nuclear egress.Lysine 242 within helix 10 of the pseudorabies virus nuclear egress complex pUL31 component is critical for primary envelopment of nucleocapsids.Herpesvirus Nuclear Egress.The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.Herpes Simplex Virus 1 UL34 Protein Regulates the Global Architecture of the Endoplasmic Reticulum in Infected Cells.Expression, Purification and Crystallization of the Herpesvirus Nuclear Egress Complex (NEC).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.The Torsin Activator LULL1 Is Required for Efficient Growth of Herpes Simplex Virus 1.Crystal Structure of the Human Cytomegalovirus pUL50-pUL53 Core Nuclear Egress Complex Provides Insight into a Unique Assembly Scaffold for Virus-Host Protein Interactions.Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complexA single herpesvirus protein can mediate vesicle formation in the nuclear envelopeHuman Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97.Venture from the Interior-Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane.ESCRT-III mediates budding across the inner nuclear membrane and regulates its integrityRoles of the Phosphorylation of Herpes Simplex Virus 1 UL51 at a Specific Site in Viral Replication and PathogenicityQualitative Differences in Capsidless L-Particles Released as a By-Product of Bovine Herpesvirus 1 and Herpes Simplex Virus 1 Infections
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P2860
Membrane deformation and scission by the HSV-1 nuclear egress complex.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Membrane deformation and scission by the HSV-1 nuclear egress complex.
@ast
Membrane deformation and scission by the HSV-1 nuclear egress complex.
@en
type
label
Membrane deformation and scission by the HSV-1 nuclear egress complex.
@ast
Membrane deformation and scission by the HSV-1 nuclear egress complex.
@en
prefLabel
Membrane deformation and scission by the HSV-1 nuclear egress complex.
@ast
Membrane deformation and scission by the HSV-1 nuclear egress complex.
@en
P2860
P356
P1476
Membrane deformation and scission by the HSV-1 nuclear egress complex
@en
P2093
Daniela Nicastro
Janna M Bigalke
P2860
P2888
P356
10.1038/NCOMMS5131
P407
P577
2014-06-11T00:00:00Z
P5875
P6179
1010840669