(Q38845249)

6 September 2017

Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response (English)

1 reference

6 September 2017

2

Peter Walter

1 reference

6 September 2017

Brooke M Gardner

1

1 reference

PMC publication ID

3202989

6 September 2017

language of work or name

English

0 references

publication date

18 August 2011

1 reference

6 September 2017

1 reference

6 September 2017

333

1 reference

6 September 2017

6051

1 reference

6 September 2017

1891-1894

1 reference

Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Messenger RNA targeting to endoplasmic reticulum stress signalling sites.

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Signal integration in the endoplasmic reticulum unfolded protein response

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

On the mechanism of sensing unfolded protein in the endoplasmic reticulum

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

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

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

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

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

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

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

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

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1.

9 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Specificity of DnaK for arginine/lysine and effect of DnaJ on the amino acid specificity of DnaK.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3202989

Peptide binding and release by proteins implicated as catalysts of protein assembly

22 August 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21852455

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21852455

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1126/SCIENCE.1209126

1 reference

6 September 2017

0 references

1 reference

PMC publication ID

3202989

6 September 2017

PubMed publication ID

21852455

1 reference

PMC publication ID

3202989