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glucose-regulated protein 170

Known as: GRP170, glucose regulated stress protein, 170 kDa 
National Institutes of Health

Related topics

Related topics

3 relations

Broader (2)

GlycoproteinsHeat-Shock Proteins 70
HYOU1 gene

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2015
Review
2015
BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions.
BiP (immunoglobulin heavy-chain binding protein) is the endoplasmic reticulum (ER) orthologue of the Hsp70 family of molecular… Expand
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Highly Cited
2012
Highly Cited
2012
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells
Co-translational transport of polypeptides into the endoplasmic reticulum (ER) involves the Sec61 channel and additional… Expand
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Highly Cited
2006
Highly Cited
2006
The nucleotide exchange factor activity of Grp170 may explain the non‐lethal phenotype of loss of Sil1 function in man and mouse
Recent genetic work characterized homozygous mutations in the SIL1 gene as cause for the neurodegeneration that is associated… Expand
Highly Cited
2006
Highly Cited
2006
Chaperoning function of stress protein grp170, a member of the hsp70 superfamily, is responsible for its immunoadjuvant activity.
When used as vaccines, tumor-derived stress proteins can elicit antitumor immune responses. For members of the hsp70 superfamily… Expand
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Highly Cited
2005
Highly Cited
2005
Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum.
In alpha1-antitrypsin (alpha1-AT) deficiency, a mutant form of alpha1-AT polymerizes in the endoplasmic reticulum (ER) of liver… Expand
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Highly Cited
2002
Highly Cited
2002
A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.
We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein complex that is comprised of the… Expand
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Highly Cited
2001
Highly Cited
2001
Characterization of Heat Shock Protein 110 and Glucose-Regulated Protein 170 as Cancer Vaccines and the Effect of Fever-Range Hyperthermia on Vaccine Activity1
Several studies have confirmed that certain stress proteins can function as potent vaccines against a specific cancer when… Expand
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Review
2000
Review
2000
The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s
Both the Grp170 and Hsp110 families represent relatively conserved and distinct sets of stress proteins, within a more diverse… Expand
Highly Cited
1997
Highly Cited
1997
Multiple Molecular Chaperones Complex with Misfolded Large Oligomeric Glycoproteins in the Endoplasmic Reticulum*
Thyroglobulin (Tg), the major protein secreted by thyroid epithelial cells and precursor of thyroid hormones, is a large dimeric… Expand
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Highly Cited
1996
Highly Cited
1996
A microsomal ATP‐binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum.
Protein transport into the mammalian endoplasmic reticulum depends on nucleoside triphosphates. Photoaffinity labelling of… Expand
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