glucose-regulated protein GRP94

Known as: GRP94 
 
National Institutes of Health

Papers overview

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Review
2012
Review
2012
GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.
Glucose-regulated protein 94 is the HSP90-like protein in the lumen of the endoplasmic reticulum and therefore it chaperones… (More)
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Highly Cited
2008
Highly Cited
2008
OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD
Terminally misfolded or unassembled proteins in the early secretory pathway are degraded by a ubiquitin- and proteasome-dependent… (More)
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Highly Cited
2008
Highly Cited
2008
Overexpression of GRP78 and GRP94 are markers for aggressive behavior and poor prognosis in gastric carcinomas.
Glucose-related proteins (GRPs) are ubiquitously expressed in endoplasmic reticulum and able to assist in protein folding and… (More)
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2000
2000
Reduced amount of the glucose-regulated protein GRP94 in skeletal myoblasts results in loss of fusion competence.
We previously showed that skeletal myocytes of the adult rabbit do not accumulate the endoplasmic reticulum glucose-regulated… (More)
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Highly Cited
1996
Highly Cited
1996
p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2.
Treatment of SKBr3 cells with benzoquinone ansamycins, such as geldanamycin (GA), depletes p185erbB2, the receptor tyrosine… (More)
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Review
1994
Review
1994
The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications.
The knowledge of GRPs as molecular chaperones is rapidly evolving. It is anticipated that the GRPs will make special… (More)
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Highly Cited
1994
Highly Cited
1994
Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
DURING their transit through the endoplasmic reticulum, newly synthesized light and heavy chains of immunoglobulins associate… (More)
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Highly Cited
1992
Highly Cited
1992
The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains.
The molecular chaperone BiP/GRP78 associates with various polypeptides in the endoplasmic reticulum, including immunoglobulin… (More)
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1989
1989
Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.
We isolated the promoter of the human gene encoding the 94,000-dalton glucose-regulated protein (GRP94). The 5'-flanking region… (More)
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Highly Cited
1988
Highly Cited
1988
The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
Two glucose-regulated proteins, GRP78 and GRP94, are major constituents of the endoplasmic reticulum (ER) of mammalian cells… (More)
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