Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A chimeric mutant analysis in yeast cells suggests BiP independent regulation of the mammalian endoplasmic reticulum-stress sensor IRE1α.

Bioscience, biotechnology, and biochemistry - 1 Sept 2018

Mai Thanh Chi, Munakata Takeo, Tran Duc Minh, Takagi Hiroshi, Kimata Yukio

Abstract excerpt

An endoplasmic reticulum (ER)-located transmembrane protein, Ire1, triggers cytoprotective events upon ER stress. Chimeric yeast Ire1 carrying the luminal domain of the mammalian major Ire1 paralogue IRE1α is upregulated in ER-stressed yeast cells, but is poorly associated with the ER-located chaperone BiP even under non-stressed conditions. This observation contradicts the theory that BiP is the master regulator...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Basic-Leucine Zipper Transcription Factors
Share to Endoplasmic Reticulum Stress

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoribonucleases

Share to HSP70 Heat-Shock Proteins

Share to Microscopy, Fluorescence

Share to Mutant Chimeric Proteins

Share to RNA Splicing

Share to Unfolded Protein Response

Source

Identifiers

PMID: 29806786
DOI: 10.1080/09168451.2018.1478716

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A chimeric mutant analysis in yeast cells suggests BiP independent regulation of the mammalian endoplasmic reticulum-stress sensor IRE1α.PMID 29806786Read ↗

Experimental approaches for elucidation of stress-sensing mechanisms of the IRE1 family proteins.Semantic proximity Read ↗

Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1.Semantic proximity Read ↗

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

IRE1 and efferent signaling from the endoplasmic reticulumSemantic proximity Read ↗

IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast.Semantic proximity Read ↗

The protein kinase Ire1 impacts pathogenicity of Candida albicans by regulating homeostatic adaptation to endoplasmic reticulum stressSemantic proximity Read ↗

How IRE1 Reacts to ER StressSemantic proximity Read ↗

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

ER stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stressSemantic proximity Read ↗

The UPR Branch IRE1-bZIP60 in Plants Plays an Essential Role in Viral Infection and Is Complementary to the Only UPR Pathway in YeastSemantic proximity Read ↗

LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum.Semantic proximity Read ↗

Defects in IRE1 enhance cell death and fail to degrade mRNAs encoding secretory pathway proteins in the Arabidopsis unfolded protein response.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.