Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein.
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The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain.Role of herpes simplex virus 1 immediate early protein ICP22 in viral nuclear egress.Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B.Cytomegalovirus downregulates IRE1 to repress the unfolded protein response.Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins.US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cellsStructure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication.Structural basis of membrane budding by the nuclear egress complex of herpesviruses.Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complexInteractions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress complex: ORF69 is a potent factor for remodeling cellular membranesPhosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids.Nuclear actin and lamins in viral infections.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.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.Reconstitution of herpes simplex virus type 1 nuclear capsid egress in vitro.Characterization of the nuclear import and export signals of pseudorabies virus UL31.Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31.Intragenic and extragenic suppression of a mutation in herpes simplex virus 1 UL34 that affects both nuclear envelope targeting and membrane 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.Mapping of sequences in Pseudorabies virus pUL34 that are required for formation and function of the nuclear egress complex.Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53.Structural determinants for nuclear envelope localization and function of pseudorabies virus pUL34.Herpes simplex virus 1 pUL34 plays a critical role in cell-to-cell spread of virus in addition to its role in virus replicationHuman Cytomegalovirus pUL93 Links Nucleocapsid Maturation and Nuclear Egress.Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids.Herpesvirus Nuclear Egress.Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection.Functional domains of murine cytomegalovirus nuclear egress protein M53/p38.Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53.Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation.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
Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein.
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Identification of an essential ...... to interact with UL31 protein.
@ast
Identification of an essential ...... to interact with UL31 protein.
@en
type
label
Identification of an essential ...... to interact with UL31 protein.
@ast
Identification of an essential ...... to interact with UL31 protein.
@en
prefLabel
Identification of an essential ...... to interact with UL31 protein.
@ast
Identification of an essential ...... to interact with UL31 protein.
@en
P2860
P1433
P1476
Identification of an essential ...... to interact with UL31 protein.
@en
P2093
Joel D Baines
P2860
P304
P356
10.1128/JVI.79.6.3797-3806.2005
P577
2005-03-01T00:00:00Z