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Article

Targeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signaling.

PloS one - 26 May 2010

Mao Changhui, Wang Miao, Luo Biquan, Wey Shiuan, Dong Dezheng, Wesselschmidt Robin, Rawlings Stephen, Lee Amy S

Abstract excerpt

Glucose-regulated protein 94 (GRP94) is one of the most abundant endoplasmic reticulum (ER) resident proteins and is the ER counterpart of the cytoplasmic heat shock protein 90 (HSP90). GRP94, a component of the GRP78 chaperone system in protein processing, has pro-survival properties with implicated function in cancer progression and autoimmune disease. Previous studies on the loss of GRP94 function showed that...

Topics

Alleles
Alternative Splicing
Animals
DNA-Binding Proteins
Embryo Loss
Embryonic Development
Embryonic Stem Cells
Endoplasmic Reticulum
Endoplasmic Reticulum Chaperone BiP
Gene Expression Profiling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Gene Targeting

Heat-Shock Proteins

Heterozygote

Homozygote

Intercellular Signaling Peptides and Proteins

Membrane Glycoproteins

Mice

Mice, Knockout

Source

Open in PubMed Open full text

Identifiers

PMID: 20520781
DOI: 10.1371/journal.pone.0010852
PMCID: PMC2877114

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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Targeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signaling.PMID 20520781Read ↗

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