ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response (Q28611502)

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English	ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response	scientific journal article

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PubMed publication ID

3 February 2017

ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response (English)

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PubMed publication ID

3 February 2017

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author name string

H. Yoshida

1

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PubMed publication ID

3 February 2017

T. Okada

2

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PubMed publication ID

3 February 2017

K. Haze

3

1 reference

PubMed publication ID

3 February 2017

H. Yanagi

4

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PubMed publication ID

3 February 2017

T. Yura

5

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PubMed publication ID

3 February 2017

M. Negishi

6

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3 February 2017

K. Mori

7

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3 February 2017

language of work or name

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publication date

1 September 2000

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PubMed publication ID

3 February 2017

Molecular and Cellular Biology

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PubMed publication ID

3 February 2017

20

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PubMed publication ID

3 February 2017

18

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PubMed publication ID

3 February 2017

6755–6767

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PubMed publication ID

3 February 2017

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

1 reference

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An essential role in liver development for transcription factor XBP-1

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

1 reference

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CHOP-Dependent stress-inducible expression of a novel form of carbonic anhydrase VI

1 reference

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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

1 reference

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1 reference

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1 reference

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1 reference

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CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum

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1 reference

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1 reference

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Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway

1 reference

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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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tRNA ligase is required for regulated mRNA splicing in the unfolded protein response

1 reference

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A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

1 reference

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The basic domain/leucine zipper protein hXBP-1 preferentially binds to and transactivates CRE-like sequences containing an ACGT core

1 reference

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Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element

1 reference

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

1 reference

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

1 reference

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A new member of the leucine zipper class of proteins that binds to the HLA DR alpha promoter

1 reference

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Multiple cDNA clones encoding nuclear proteins that bind to the tax-dependent enhancer of HTLV-1: all contain a leucine zipper structure and basic amino acid domain

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Isolation, characterization and chromosomal localization of the human GADD153 gene

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

1 reference

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

1 reference

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Protein folding in the cell

1 reference

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

1 reference

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Tripartite management of unfolded proteins in the endoplasmic reticulum

1 reference

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mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response

1 reference

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Mechanism of non-spliceosomal mRNA splicing in the unfolded protein response pathway

1 reference

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The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex

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Translational attenuation mediated by an mRNA intron

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Endoplasmic Reticulum Stress-induced mRNA Splicing Permits Synthesis of Transcription Factor Hac1p/Ern4p That Activates the Unfolded Protein Response

1 reference

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1 reference

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1 reference

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1 reference

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Unconventional splicing of HAC1/ERN4 mRNA required for the unfolded protein response. Sequence-specific and non-sequential cleavage of the splice sites

1 reference

https://pubmed.ncbi.nlm.nih.gov/10958673

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inferred from PubMed ID database lookup

Normal Fibroblasts Induce the C/EBPβ and ATF-4 bZIP Transcription Factors in Response to Anoxia

1 reference

https://pubmed.ncbi.nlm.nih.gov/10958673

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inferred from PubMed ID database lookup

The endoplasmic reticulum as a protein-folding compartment

1 reference

https://pubmed.ncbi.nlm.nih.gov/10958673

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inferred from PubMed ID database lookup

A high-efficiency HeLa cell nuclear transcription extract

1 reference

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based on heuristic

inferred from PubMed ID database lookup

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10.1128/MCB.20.18.6755-6767.2000

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24 November 2022

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Consolidated OpenCitations Corpus – April 2017

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