Human pathogens and the host cell SUMOylation system. - Wikidata - awgldk - TriplyDB

Human pathogens and the host cell SUMOylation system.

Human pathogens and the host cell SUMOylation system.

http://www.wikidata.org/entity/Q37954599

about

Analysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection Human Oncogenic Herpesvirus and Post-translational Modifications - Phosphorylation and SUMOylation Infected cell protein 0 functional domains and their coordination in herpes simplex virus replication Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways JASSA: a comprehensive tool for prediction of SUMOylation sites and SIMs Host response to respiratory bacterial pathogens as identified by integrated analysis of human gene expression data The inhibitory effects of anacardic acid on hepatitis C virus life cycle NEDDylation is essential for Kaposi's sarcoma-associated herpesvirus latency and lytic reactivation and represents a novel anti-KSHV target Geminivirus protein structure and function.The chromatin modification by SUMO-2/3 but not SUMO-1 prevents the epigenetic activation of key immune-related genes during Kaposi's sarcoma associated herpesvirus reactivation Rotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.Sumoylation of influenza A virus nucleoprotein is essential for intracellular trafficking and virus growth.Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli Ehrlichia chaffeensis exploits host SUMOylation pathways to mediate effector-host interactions and promote intracellular survival.Camouflage and misdirection: the full-on assault of ebola virus disease SUMO and KSHV Replication Identification of sumoylated proteins in the silkworm Bombyx mori.K-bZIP Mediated SUMO-2/3 Specific Modification on the KSHV Genome Negatively Regulates Lytic Gene Expression and Viral Reactivation.Analysis of the SUMO2 Proteome during HSV-1 Infection.The SUMOylation Pathway Restricts Gene Transduction by Adeno-Associated Viruses Posttranslational modification of vesicular stomatitis virus glycoprotein, but not JNK inhibition, is the antiviral mechanism of SP600125 Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains.Quantitative proteomics reveals factors regulating RNA biology as dynamic targets of stress-induced SUMOylation in Arabidopsis SCE1, the SUMO-conjugating enzyme in plants that interacts with NIb, the RNA-dependent RNA polymerase of Turnip mosaic virus, is required for viral infection SUMO Modification Stabilizes Dengue Virus Nonstructural Protein 5 To Support Virus Replication.Detection of the Wolbachia protein WPIP0282 in mosquito spermathecae: implications for cytoplasmic incompatibility.SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication.Regulation of Ebola virus VP40 matrix protein by SUMO.NEDDylation of PB2 Reduces Its Stability and Blocks the Replication of Influenza A Virus Type I interferons regulate susceptibility to inflammation-induced preterm birth.Emerging roles for ubiquitin in adenovirus cell entry.Adenovirus degradation of cellular proteins.HTLV-1 Rex: the courier of viral messages making use of the host vehicle.Ubiquitin-like protein modifiers and their potential for antiviral and anti-HCV therapy.Sumoylation at the host-pathogen interface.Viral evasion mechanisms of early antiviral responses involving regulation of ubiquitin pathways.The role of ubiquitin and ubiquitin-like modification systems in papillomavirus biology.Analysis of EV71 infection progression using triple-SILAC-based proteomics approach.Sumo and the cellular stress response.The Human Cytomegalovirus IE1 Protein Antagonizes PML Nuclear Body-Mediated Intrinsic Immunity via the Inhibition of PML De Novo SUMOylation

P2860

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P2860

Human pathogens and the host cell SUMOylation system.

http://www.wikidata.org/entity/Q37954599

description

2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Human pathogens and the host cell SUMOylation system.

@en

Human pathogens and the host cell SUMOylation system.

@nl

type

label

Human pathogens and the host cell SUMOylation system.

@en

Human pathogens and the host cell SUMOylation system.

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prefLabel

Human pathogens and the host cell SUMOylation system.

@en

Human pathogens and the host cell SUMOylation system.

@nl

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Journal of Virology

P1476

Human pathogens and the host cell SUMOylation system.

@en

P2093

Peter Wimmer

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

Sabrina Schreiner

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

Thomas Dobner

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

P2860

Bovine papillomavirus E1 protein is sumoylated by the host cell Ubc9 protein

A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection

Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0

Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies

Identification of host proteins required for HIV infection through a functional genomic screen

An extended consensus motif enhances the specificity of substrate modification by SUMO

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

The mechanisms of PML-nuclear body formation

A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

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642-654

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scholarly article

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10.1128/JVI.06227-11

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2

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86

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2011-11-09T00:00:00Z

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3255802

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