(Q40258062)

18 September 2017

title

Cell biology. Stressed cells cope with protein overload (English)

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18 September 2017

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1

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18 September 2017

language of work or name

English

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publication date

1 July 2006

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18 September 2017

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18 September 2017

volume

313

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18 September 2017

issue

5783

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18 September 2017

page(s)

52-53

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Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response.

18 September 2017

cites work

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https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

Transcriptional and translational control in the Mammalian unfolded protein response

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

On the mechanism of sensing unfolded protein in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1130469

21 January 2018

Identifiers

DOI

10.1126/SCIENCE.1130469

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18 September 2017

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