(Q43226732)

English

PERK (eIF2alpha kinase) is required to activate the stress-activated MAPKs and induce the expression of immediate-early genes upon disruption of ER calcium homoeostasis

scientific article published in January 2006

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scholarly article

1 reference

Europe PubMed Central

16 November 2017

PERK (eIF2alpha kinase) is required to activate the stress-activated MAPKs and induce the expression of immediate-early genes upon disruption of ER calcium homoeostasis (English)

1 reference

Europe PubMed Central

16 November 2017

immediate early gene

1 reference

based on heuristic

inferred from title

Douglas R. Cavener

5

object named as

Douglas R Cavener

1 reference

Europe PubMed Central

16 November 2017

author name string

Shun-Hsin Liang

1

1 reference

Europe PubMed Central

16 November 2017

Wei Zhang

2

1 reference

Europe PubMed Central

16 November 2017

Barbara C McGrath

3

1 reference

Europe PubMed Central

16 November 2017

Peichuan Zhang

4

1 reference

Europe PubMed Central

16 November 2017

language of work or name

0 references

publication date

1 January 2006

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Europe PubMed Central

16 November 2017

Biochemical Journal

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Europe PubMed Central

16 November 2017

393

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Europe PubMed Central

16 November 2017

Pt 1

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Europe PubMed Central

16 November 2017

201-209

1 reference

Europe PubMed Central

16 November 2017

describes a project that uses

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC1383678/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response

1 reference

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Activating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response

1 reference

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Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses

1 reference

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PERK eIF2alpha kinase regulates neonatal growth by controlling the expression of circulating insulin-like growth factor-I derived from the liver

1 reference

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Activation of GCN2 in UV-irradiated cells inhibits translation

1 reference

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The endoplasmic reticulum as an integrating signalling organelle: from neuronal signalling to neuronal death

1 reference

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

1 reference

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Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: activating transcription factor 6 as a target [...]

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Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3

1 reference

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The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas

1 reference

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Intracellular calcium mobilization induces period genes via MAP kinase pathways in NIH3T3 cells

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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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Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals

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Elevation of intracellular calcium ions is essential for the H2O2-induced activation of SAPK/JNK but not for that of p38 and ERK in Chinese hamster V79 cells.

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Dependence of vital cell function on endoplasmic reticulum calcium levels: implications for the mechanisms underlying neuronal cell injury in different pathological states

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Regulated translation initiation controls stress-induced gene expression in mammalian cells

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Pausing to decide

1 reference

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The calcium-sensing receptor stimulates JNK in MDCK cells.

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Abnormal intracellular ca(2+)homeostasis and disease

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EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome

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

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Participation of mitogen-activated protein kinase in thapsigargin- and TPA-induced histamine production in murine macrophage RAW 264.7 cells

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Action of Myc in vivo - proliferation and apoptosis

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Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1

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From receptors to stress-activated MAP kinases

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The stress-activated protein kinase pathways

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MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction

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1 reference

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BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2+

1 reference

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inferred from PubMed ID database lookup

Identifiers

10.1042/BJ20050374

1 reference

Europe PubMed Central

16 November 2017

1 reference

Europe PubMed Central

16 November 2017

1 reference

Europe PubMed Central

16 November 2017

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