78 kD glucose-regulated protein; GRP 78; heat shock 70 kD protein 5; immunoglobulin heavy chain-binding protein; BiP; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78 (HSPA5, GRP78)

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Function

Structure

belongs to the heat shock protein 70 family

Compartment

Expression

Pathology

Comparative biology

More general terms

References

  1. Ou WJ et al Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364:771 1993 PMID: https://www.ncbi.nlm.nih.gov/pubmed/8102790
  2. Arlan Richardson, AGE meeting Oct 3-6, 1990 New York, NY
  3. 3.0 3.1 Rampon C, Jiang CH, Dong H, Tang YP, Lockhart DJ, Schultz PG, Tsien JZ, Hu Y. Effects of environmental enrichment on gene expression in the brain. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12880-4. PMID: https://www.ncbi.nlm.nih.gov/pubmed/11070096
  4. Abrams Z New drug shows promise for fighting both COVID-19 and cancer. Keck School of Medicine USC. Keck School News. Nov 14, 2022 https://keck.usc.edu/new-drug-shows-promise-for-fighting-both-covid-19-and-cancer/
    Shin WJ, Ha DP, Machida K, Lee AS The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein. Nature Communications. 2022. 13:6551. Nov 14 PMID: https://www.ncbi.nlm.nih.gov/pubmed/36376289 PMCID: PMC9663498 Free PMC article. https://www.nature.com/articles/s41467-022-34065-3

Database