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

Effects of N-glycosylation and inositol on the ER stress response in yeast Saccharomyces cerevisiae.

Bioscience, biotechnology, and biochemistry - 1 Jul 2005

Uchimura Seiichi, Sugiyama Minetaka, Nikawa Jun-ichi

Abstract excerpt

IRE1 and HAC1 are essential for the unfolded protein response in the endoplasmic reticulum (ER). IRE1- and HAC1-disruptants require high concentrations of inositol for its normal growth. The ALG6, ALG8, and ALG10 genes encode the glucosyltransferases necessary for the completion of the synthesis of the lipid-linked oligosaccharide used for the asparagine-linked glycosylation of proteins in that order. Here we...

Read the complete abstract on PubMed

Topics

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

Share to Culture Media
Share to Endoplasmic Reticulum
Share to Glucosyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to HSP70 Heat-Shock Proteins

Share to Inositol

Share to Monosaccharide Transport Proteins

Share to Tunicamycin

Source

Identifiers

PMID: 16041130
DOI: 10.1271/bbb.69.1274

Genes

ALG10
ALG6
ALG8

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

Effects of N-glycosylation and inositol on the ER stress response in yeast Saccharomyces cerevisiae.PMID 16041130Read ↗

Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae.Semantic proximity Read ↗

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

The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane.Semantic proximity Read ↗

The response to inositol: regulation of glycerolipid metabolism and stress response signaling in yeast.Semantic proximity Read ↗

Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling.Semantic proximity Read ↗

Saccharomyces cerevisiae Is Dependent on Vesicular Traffic between the Golgi Apparatus and the Vacuole When Inositolphosphorylceramide Synthase Aur1 Is Inactivated.Semantic proximity Read ↗

Role of the unfolded protein response pathway in regulation of INO1 and in the sec14 bypass mechanism in Saccharomyces cerevisiae.Semantic proximity Read ↗

Inositol depletion regulates phospholipid metabolism and activates stress signaling in HEK293T cellsSemantic proximity Read ↗

Disruption of aldo-keto reductase genes leads to elevated markers of oxidative stress and inositol auxotrophy in Saccharomyces cerevisiae.Semantic proximity Read ↗

SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast.Semantic proximity Read ↗

Cell wall integrity MAPK pathway is essential for lipid homeostasis.Semantic proximity Read ↗

Biosynthesis of mannosylinositolphosphoceramide in Saccharomyces cerevisiae is dependent on genes controlling the flow of secretory vesicles from the endoplasmic reticulum to the Golgi.Semantic proximity Read ↗

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