Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly. - Wikidata - wikimedia - TriplyDB

Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly.

Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly.

http://www.wikidata.org/entity/Q36423955

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Escherichia coli Subtilase Cytotoxin Human Cytomegalovirus Strategies to Maintain and Promote mRNA Translation Dengue Virus Infection Induces Upregulation of GRP78, Which Acts To Chaperone Viral Antigen Production Modulation of the Translational Landscape During Herpesvirus Infection Modulation of the Akt pathway reveals a novel link with PERK/eIF2α, which is relevant during hypoxia Spatial relationships between markers for secretory and endosomal machinery in human cytomegalovirus-infected cells versus those in uninfected cells Identification of essential filovirion-associated host factors by serial proteomic analysis and RNAi screen.Identification and characterization of two novel spliced genes located in the orf47-orf46-orf45 gene locus of Kaposi's sarcoma-associated herpesvirus.Structure, biological functions and applications of the AB5 toxins.The human cytomegalovirus assembly compartment: a masterpiece of viral manipulation of cellular processes that facilitates assembly and egress Role of the host cell's unfolded protein response in arenavirus infection.Widespread evidence of viral miRNAs targeting host pathways New cell-signaling pathways for controlling cytomegalovirus replication.Cytomegalovirus downregulates IRE1 to repress the unfolded protein response.Viral effects on metabolism: changes in glucose and glutamine utilization during human cytomegalovirus infection.The human cytomegalovirus protein pUL38 suppresses endoplasmic reticulum stress-mediated cell death independently of its ability to induce mTORC1 activation.Transcriptional activation of endoplasmic reticulum chaperone GRP78 by HCMV IE1-72 protein Quantitative proteomic analyses of human cytomegalovirus-induced restructuring of endoplasmic reticulum-mitochondrial contacts at late times of infection.Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting Murine cytomegalovirus targets transcription factor ATF4 to exploit the unfolded-protein response Administration of Recombinant Heat Shock Protein 70 Delays Peripheral Muscle Denervation in the SOD1(G93A) Mouse Model of Amyotrophic Lateral Sclerosis Dynein mediates the localization and activation of mTOR in normal and human cytomegalovirus-infected cells.Visualization of Host-Polerovirus Interaction Topologies Using Protein Interaction Reporter Technology.Decreased ER-associated degradation of alpha-TCR induced by Grp78 depletion with the SubAB cytotoxin.The TORrid affairs of viruses: effects of mammalian DNA viruses on the PI3K-Akt-mTOR signalling pathway.Two-dimensional blue native/SDS-PAGE analysis reveals heat shock protein chaperone machinery involved in hepatitis B virus production in HepG2.2.15 cells.The unfolded protein response and autophagy: herpesviruses rule!Subtilase cytotoxin cleaves newly synthesized BiP and blocks antibody secretion in B lymphocytes.The endoplasmic reticulum chaperone BiP/GRP78 is important in the structure and function of the human cytomegalovirus assembly compartment.Deletion of the human cytomegalovirus US17 gene increases the ratio of genomes per infectious unit and alters regulation of immune and endoplasmic reticulum stress response genes at early and late times after infection.The unfolded protein response: how protein folding became a restrictive aspect for innate immunity and B lymphocytes.The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis.Human cytomegalovirus infection maintains mTOR activity and its perinuclear localization during amino acid deprivation.GRP78 Is an Important Host Factor for Japanese Encephalitis Virus Entry and Replication in Mammalian Cells.Potent Inhibition of Human Cytomegalovirus by Modulation of Cellular SNARE Syntaxin 5.Fatty acid elongase 7 catalyzes lipidome remodeling essential for human cytomegalovirus replication.Human cytomegalovirus induces multiple means to combat reactive oxygen species.Betanodavirus up-regulates chaperone GRP78 via ER stress: roles of GRP78 in viral replication and host mitochondria-mediated cell death.Human Herpesvirus 8 Interleukin-6 Interacts with Calnexin Cycle Components and Promotes Protein Folding.Human cytomegalovirus induces the endoplasmic reticulum chaperone BiP through increased transcription and activation of translation by using the BiP internal ribosome entry site.

P2860

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P2860

Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly.

http://www.wikidata.org/entity/Q36423955

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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name

Human cytomegalovirus specific ...... required for virion assembly.

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Human cytomegalovirus specific ...... required for virion assembly.

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type

label

Human cytomegalovirus specific ...... required for virion assembly.

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Human cytomegalovirus specific ...... required for virion assembly.

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prefLabel

Human cytomegalovirus specific ...... required for virion assembly.

@ast

Human cytomegalovirus specific ...... required for virion assembly.

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Journal of Virology

P1476

Human cytomegalovirus specific ...... required for virion assembly.

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P2093

James C Alwine

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James C Paton

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Nicholas J Buchkovich

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Tobi G Maguire

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Yongjun Yu

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P2860

Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor- and rictor-containing complexes

Human cytomegalovirus infection activates and regulates the unfolded protein response.

ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals

Translational control in stress and apoptosis

Coping with stress: eIF2 kinases and translational control

A trip to the ER: coping with stress

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31-39

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10.1128/JVI.01881-07

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1

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82

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Adrienne W Paton

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2007-10-17T00:00:00Z

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5902175

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17942541

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P921

molecular chaperones

Cytomegalovirus

endoplasmic reticulum

P932

2224369

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