Biochemical, biophysical, and mutational analyses of subunit interactions of the human cytomegalovirus nuclear egress complex.
about
Viral and host control of cytomegalovirus maturationGammaherpesvirus Tegument Protein ORF33 Is Associated With Intranuclear Capsids at an Early Stage of the Tegumentation ProcessStructure 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 membranesSurvey of the year 2009: applications of isothermal titration calorimetry.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.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.Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31.Identification of conserved amino acids in pUL34 which are critical for function of the pseudorabies virus nuclear egress complex.Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses.Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cellsGetting to and through the inner nuclear membrane during herpesvirus nuclear egress.Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53.RASCAL is a new human cytomegalovirus-encoded protein that localizes to the nuclear lamina and in cytoplasmic vesicles at late times postinfection.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 complexSpecific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53.A single herpesvirus protein can mediate vesicle formation in the nuclear envelopeProteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.Human 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.Near-native, site-specific and purification-free protein labeling for quantitative protein interaction analysis by MicroScale Thermophoresis.
P2860
Q27007890-4AD47137-2182-4078-B278-853889BB4CB2Q35641439-378DA39A-0F22-425D-8A49-3D343E704199Q35895476-0AD23B7C-5FEC-4D1F-B5B0-ACFF27F3E7B6Q36394653-79882EE4-3C80-463E-8DBF-52DBAB086E51Q36394658-BDAA0616-27F6-452C-89B4-DD79077BFC58Q36759769-F5C22D18-1FA0-4E7E-B7B2-DF14063BF905Q37820930-3F4E609E-02FA-4AF1-AD59-787C4AF73D21Q38051413-5AC5D964-D20A-4DC6-A6D3-197F69354482Q38700888-48E185FB-EEA8-41BC-88A2-0D0C23E08043Q38753357-A793FB54-099E-4113-91C8-95DE21DC1DC9Q38753361-41892306-EAE2-43BC-95E6-895C44E5F1E8Q38928595-573D1F30-7F37-41A8-8A98-E27F1FA7E807Q39013680-0D502126-C125-4B13-A06C-8C58BB7E8F15Q39068838-DB8BF579-003C-42B0-970B-01EF0F5E2CC8Q39071752-0EB728B2-D1D9-407E-A3B6-8D5E054BDB4BQ39086096-A0DBDA27-F813-4853-B281-7D94944783B4Q39275427-4E0DEA3F-10A3-489A-B82D-99C12143360CQ39714762-056F4BC2-79DF-47FA-BC66-5276529B348AQ41268588-4DE6F9A6-7E8C-404F-929E-C074A4942E94Q41691057-3C8426DB-C3F8-4340-9B95-07777874FE68Q41892236-ED3E9B4D-7DB6-4063-A82D-B57433156D71Q42174487-7F783B0A-81FD-471A-B4FE-570019AF9CC6Q42209745-0B8BD20F-3AA6-429E-A7B8-613B3DC60565Q47552402-1B218885-DFD0-4708-BBBD-B182D1231AA6Q47571623-64D5B25D-581F-49AF-A2A0-EC698A296C70Q52347203-FF1BA873-224D-413E-B96E-BABD793727D3
P2860
Biochemical, biophysical, and mutational analyses of subunit interactions of the human cytomegalovirus nuclear egress complex.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 19 January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@en
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@nl
type
label
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@en
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@nl
prefLabel
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@en
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@nl
P2093
P2860
P356
P1433
P1476
Biochemical, biophysical, and ...... ovirus nuclear egress complex.
@en
P2093
Brady T Evans
Donald M Coen
James M Hogle
P2860
P304
P356
10.1128/JVI.02441-08
P407
P577
2009-01-19T00:00:00Z