Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus. - Wikidata - awgldk - TriplyDB

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

http://www.wikidata.org/entity/Q42209745

about

MS_HistoneDB, a manually curated resource for proteomic analysis of human and mouse histones.Regulation of postsynaptic function by the dementia-related ESCRT-III subunit CHMP2B The Emerging Roles of Viroporins in ER Stress Response and Autophagy Induction during Virus Infection 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 Egress Human Cytomegalovirus Nuclear Egress Proteins Ectopically Expressed in the Heterologous Environment of Plant Cells are Strictly Targeted to the Nuclear Envelope.The Prolyl Isomerase Pin1 Promotes the Herpesvirus-Induced Phosphorylation-Dependent Disassembly of the Nuclear Lamina Required for Nucleocytoplasmic Egress The life cycle and pathogenesis of human cytomegalovirus infection: lessons from proteomics Bdf1 Bromodomains Are Essential for Meiosis and the Expression of Meiotic-Specific Genes.Nuclear Exodus: Herpesviruses Lead the Way.Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A/C through the γ134.5 Protein That Facilitates Nuclear Egress Manipulation of host pathways by human cytomegalovirus: insights from genome-wide studies.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.Getting to and through the inner nuclear membrane during herpesvirus nuclear egress.Proteomic Interaction Patterns between Human Cyclins, the Cyclin-Dependent Kinase Ortholog pUL97 and Additional Cytomegalovirus Proteins.The Essential Human Cytomegalovirus Proteins pUL77 and pUL93 Are Structural Components Necessary for Viral Genome Encapsidation.Herpesvirus Nuclear Egress.Preparation of the Human Cytomegalovirus Nuclear Egress Complex and Associated Proteins.Crystal Structure of the Human Cytomegalovirus pUL50-pUL53 Core Nuclear Egress Complex Provides Insight into a Unique Assembly Scaffold for Virus-Host Protein Interactions.The Interaction between Cyclin B1 and Cytomegalovirus Protein Kinase pUL97 is Determined by an Active Kinase Domain Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation.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.An algal photoenzyme converts fatty acids to hydrocarbons.Systematic quantitative analysis of H2A and H2B variants by targeted proteomics.The PHD finger protein Spp1 has distinct functions in the Set1 and the meiotic DSB formation complexes.WDR5 Facilitates Human Cytomegalovirus Replication by Promoting Capsid Nuclear Egress.The Long Hunt for pssR-Looking for a Phospholipid Synthesis Transcriptional Regulator, Finding the Ribosome.Transmembrane protein pUL50 of human cytomegalovirus inhibits ISGylation by downregulating UBE1L.

P2860

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P2860

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

http://www.wikidata.org/entity/Q42209745

description

2014 nî lūn-bûn

@nan

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

2014年论文

@zh

2014年论文

@zh-cn

name

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@en

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@nl

type

label

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@en

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@nl

prefLabel

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@en

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@nl

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MCP.M113.035782

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Molecular & Cellular Proteomics

P1476

Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus.

@en

P2093

Alexandra Kraut

http://www.w3.org/2001/XMLSchema#string

Cathrin Schmeiser

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Claudia Claus

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Corina Hutterer

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Eric Sonntag

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Manfred Marschall

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Sabrina Wagner

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Sandra Pinkert

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Stuart T Hamilton

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Tihana Lenac

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P2860

Viral and host control of cytomegalovirus maturation

Structural characterization of the LEM motif common to three human inner nuclear membrane proteins

Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA

Solution NMR structure of the barrier-to-autointegration factor-Emerin complex

BAF is required for emerin assembly into the reforming nuclear envelope

p32/gC1qR is indispensable for fetal development and mitochondrial translation: importance of its RNA-binding ability

BIOCHEMISTRY: Not Comparable, But Complementary

Three-dimensional structure of the human cytomegalovirus cytoplasmic virion assembly complex includes a reoriented secretory apparatus.

Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirus

Spatial relationships between markers for secretory and endosomal machinery in human cytomegalovirus-infected cells versus those in uninfected cells

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2132-2146

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8

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13

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Heinrich Sticht

William D. Rawlinson

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2014-06-26T00:00:00Z

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24969177

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