Activation of the unfolded protein response by Listeria monocytogenes (Q39398972)

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scientific article published on 8 March 2012

Language	Label	Description	Also known as
English	Activation of the unfolded protein response by Listeria monocytogenes	scientific article published on 8 March 2012

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

Activation of the unfolded protein response by Listeria monocytogenes (English)

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

Listeria monocytogenes

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Trinad Chakraborty

4

object named as

Trinad Chakraborty

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

author name string

Helena Pillich

1

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

Maria Loose

2

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

Klaus-Peter Zimmer

3

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

publication date

8 March 2012

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

Cellular Microbiology

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Europe PubMed Central

PubMed publication ID

11 September 2017

14

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Europe PubMed Central

PubMed publication ID

11 September 2017

6

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

949-964

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

Integration of endoplasmic reticulum signaling in health and disease

1 reference

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Hypoxia and the hypoxic response pathway protect against pore-forming toxins in C. elegans

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

1 reference

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Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo.

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IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA

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The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi

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Endoplasmic reticulum stress response is involved in Mycobacterium tuberculosis protein ESAT-6-mediated apoptosis.

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Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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Extracellular group A Streptococcus induces keratinocyte apoptosis by dysregulating calcium signalling

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Cholera toxin up-regulates endoplasmic reticulum proteins that correlate with sensitivity to the toxin

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Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line

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Listeria monocytogenes desensitizes immune cells to subsequent Ca2+ signaling via listeriolysin O-induced depletion of intracellular Ca2+ stores

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Novel bacterial artificial chromosome vector pUvBBAC for use in studies of the functional genomics of Listeria spp.

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

1 reference

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Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress

1 reference

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Viruses, endoplasmic reticulum stress, and interferon responses

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Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12.

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Endoplasmic reticulum stress and the inflammatory basis of metabolic disease

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Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes

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Endoplasmic reticulum stress regulator XBP-1 contributes to effector CD8+ T cell differentiation during acute infection.

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XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease

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Listeriolysin O suppresses phospholipase C-mediated activation of the microbicidal NADPH oxidase to promote Listeria monocytogenes infection

1 reference

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

1 reference

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Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells

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The increase in mucin exocytosis and the upregulation of MUC genes encoding for membrane-bound mucins induced by the thiol-activated exotoxin listeriolysin O is a host cell defence response that inhibits the cell-entry of Listeria monocytogenes

1 reference

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Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress

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Airway epithelial inflammation-induced endoplasmic reticulum Ca2+ store expansion is mediated by X-box binding protein-1.

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TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages.

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A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus

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Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells

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A new mathematical model for relative quantification in real-time RT-PCR

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RNAi screen of endoplasmic reticulum-associated host factors reveals a role for IRE1alpha in supporting Brucella replication

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Listeriolysin of Listeria monocytogenes forms Ca2+-permeable pores leading to intracellular Ca2+ oscillations

1 reference

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Listeria monocytogenes impairs SUMOylation for efficient infection

1 reference

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Signal integration in the endoplasmic reticulum unfolded protein response

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Structural characteristics of the plasmid-encoded toxin from enteroaggregative Escherichia coli

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Listeriolysin O: a phagosome-specific lysin

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Endoplasmic reticulum stress responses

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Induction of ER stress in macrophages of tuberculosis granulomas

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XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation

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

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XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum.

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Listeria pathogenesis and molecular virulence determinants

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Pathogenicity islands and virulence evolution in Listeria.

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Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways

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ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs

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Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress

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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

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

1 reference

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Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response

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Identifiers

10.1111/J.1462-5822.2012.01769.X

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

11 September 2017

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