A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
about
The Great (Nuclear) Escape: New Insights into the Role of the Nuclear Egress Complex of HerpesvirusesFluorescent Protein Approaches in Alpha Herpesvirus ResearchThe Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain.Chromatin organization regulates viral egress dynamics.Structural 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.The Prolyl Isomerase Pin1 Promotes the Herpesvirus-Induced Phosphorylation-Dependent Disassembly of the Nuclear Lamina Required for Nucleocytoplasmic EgressStructural 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 RemodelingA 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.The absence of p53 during Human Cytomegalovirus infection leads to decreased UL53 expression, disrupting UL50 localization to the inner nuclear membrane, and thereby inhibiting capsid nuclear egress.This bud's for you: mechanisms of cellular nucleocytoplasmic trafficking via nuclear envelope budding.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.Mechanisms and functions of nuclear envelope remodelling.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.Vesicular Nucleo-Cytoplasmic Transport-Herpesviruses as Pioneers in Cell Biology.cBid, Bax and Bcl-xL exhibit opposite membrane remodeling activities.Venture from the Interior-Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane.
P2860
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P2860
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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name
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@en
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@nl
type
label
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@en
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@nl
prefLabel
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@en
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@nl
P2093
P2860
P50
P356
P1476
A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
@en
P2093
Barbara G Klupp
Michael Lorenz
Thomas C Mettenleiter
P2860
P304
P356
10.1074/JBC.M114.627521
P407
P577
2015-01-20T00:00:00Z