Translational control is required for the unfolded protein response and in vivo glucose homeostasis (Q28204066)

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9 November 2019

title

Translational control is required for the unfolded protein response and in vivo glucose homeostasis (English)

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9 November 2019

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7

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9 November 2019

author name string

D Scheuner

1

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9 November 2019

B Song

2

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9 November 2019

E McEwen

3

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9 November 2019

C Liu

4

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9 November 2019

R Laybutt

5

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9 November 2019

P Gillespie

6

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9 November 2019

S Bonner-Weir

8

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9 November 2019

R J Kaufman

9

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9 November 2019

language of work or name

English

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publication date

1 June 2001

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9 November 2019

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9 November 2019

volume

7

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9 November 2019

issue

6

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9 November 2019

page(s)

1165-1176

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Integration of endoplasmic reticulum signaling in health and disease

9 November 2019

cites work

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

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Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response

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Perk is essential for translational regulation and cell survival during the unfolded protein response

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

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

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Translational control of proinsulin synthesis by glucose

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Chronic hyperglycemia triggers loss of pancreatic beta cell differentiation in an animal model of diabetes

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Double-stranded RNA-activated protein kinase mediates virus-induced apoptosis: a new role for an old actor

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Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

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Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes

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7 January 2021

The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

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Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion

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Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum.

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Tripartite management of unfolded proteins in the endoplasmic reticulum

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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta

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CCAAT/enhancer-binding protein mRNA is translated into multiple proteins with different transcription activation potentials

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Initiation of protein synthesis in eukaryotic cells

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Determination of phosphoenolpyruvate carboxykinase activity with deoxyguanosine 5′-diphosphate as nucleotide substrate

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Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation

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The unfolded protein response represses nitrogen-starvation induced developmental differentiation in yeast

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7 January 2021

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

789576

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430820%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

789576

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

789576