Skip to search formSkip to main contentSkip to account menu

HSP90B1 gene

Known as: GRP94, GP96, HEAT-SHOCK PROTEIN, 90-KD, BETA, 1 
This gene plays a role in both ATP metabolism and protein folding.
National Institutes of Health

Related topics

Related topics

6 relations
ATP HydrolysisEnzyme Activity AlterationHSP90B1 protein, humancellular response to unfolded protein

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2015
Highly Cited
2015
ING5 suppresses proliferation, apoptosis, migration and invasion, and induces autophagy and differentiation of gastric cancer cells: a good marker for carcinogenesis and subsequent progression
Here, we found that ING5 overexpression increased autophagy, differentiation, and decreased proliferation, apoptosis, migration… 
Highly Cited
2010
Highly Cited
2010
High efficiency CD91- and LOX-1-mediated re-presentation of gp96-chaperoned peptides by MHC II molecules.
Exogenous antigens enter antigen-presenting cells through non-specific mechanisms and are presented by the MHC II molecules. We… 
2010
2010
Ovalbumin-Derived Precursor Peptides Are Transferred Sequentially from gp96 and Calreticulin to MHC Class I in the Endoplasmic Reticulum
Cellular peptides generated by proteasomal degradation of proteins in the cytosol and destined for presentation by MHC class I… 
Highly Cited
2005
Highly Cited
2005
Generation of Murine CTL by a Hepatitis B Virus-Specific Peptide and Evaluation of the Adjuvant Effect of Heat Shock Protein Glycoprotein 96 and Its Terminal Fragments1
Previously, we reported that a 7-mer HLA-A11-restricted peptide (YVNTNMG) of hepatitis B virus (HBV) core Ag (HBcAg88–94) was… 
Highly Cited
2005
Highly Cited
2005
Testing the Role of gp96 as Peptide Chaperone in Antigen Processing*
gp96 is a 96-kDa glycoprotein of the endoplasmic reticulum that is believed to be involved in antigen processing as an… 
Review
2002
Review
2002
An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response.
Heat shock protein (HSP) gp96, or grp94 is an endoplasmic reticular (ER) paralog of the cytosolic HSP90. Being abundant and non… 
Highly Cited
2001
Highly Cited
2001
Heat shock protein-peptide complexes elicit cytotoxic T-lymphocyte and antibody responses specific for bovine herpesvirus 1.
Highly Cited
2001
Highly Cited
2001
gp96-Peptide Vaccination of Mice against Intracellular Bacteria
ABSTRACT This work demonstrates that gp96 preparations isolated from cells infected with intracellular bacteria induce cytotoxic… 
Review
1996
Review
1996
Heat shock protein‐peptide complexes for use in vaccines
The heat shock proteins gp96, HSP70, and HSP90 are complexed to a diverse array of cellular proteins and peptides as a… 
Highly Cited
1987
Highly Cited
1987
5'-structural analysis of genes encoding polymorphic antigens of chemically induced tumors.
We have proposed that the distinct tumor rejection antigens of chemically induced sarcomas in inbred mice belong to a family of… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)