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Human GRP78 Protein expressed in Escherichia coli (E. coli) - ABIN1686700
Yang, Turner, Gaut: The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. in The Journal of biological chemistry 1998
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Human GRP78 Protein expressed in Escherichia coli (E. coli) - ABIN1686682
Rechthand, Smith, Latker, Rapoport: Altered blood-nerve barrier permeability to small molecules in experimental diabetes mellitus. in Journal of neuropathology and experimental neurology 1987
Show all 9 Pubmed References
Human GRP78 Protein expressed in Wheat germ - ABIN1307202
Taylor, Gercel-Taylor, Parker: Patient-derived tumor-reactive antibodies as diagnostic markers for ovarian cancer. in Gynecologic oncology 2009
In amphibians, the association of BiP with unfolded protein and its possible role in aggresome function may be vital in the maintenance of cellular proteostasis.
Hspa5 is essential for pronephros formation by mediating retinoic acid signaling.
GRP78 silencing promoted lung epithelial cell apoptosis during hyperoxia, via regulation of the CHOP (show DDIT3 Proteins) pathway.
GRP78 role in dengue virus infection.
Overexpression of GRP78 is a novel predictor of favorable outcomes in patients with advanced thymic carcinoma. who receive combination chemotherapy.
GRP78 is an autoantigen that could stimulate autoimmune responses and serve as a potential marker for recurrent and metastatic progression in HCC (show FAM126A Proteins).
These results identify GRP78 antibodies as a potential component of Neuromyelitis optica pathogenesis.
HSPA5 (GRP78) and GEP were identified to interact. Clinical analysis showed that expression of GRP78 was up-regulated in hepatocellular carcinoma tumor and correlated with GEP expression.
an endoplasmic reticulum complex of resident chaperones that includes HSP47 (show SERPINH1 Proteins), FKBP65 (show FKBP10 Proteins), and BiP (show GDF10 Proteins) regulating the activity of LH2 (show PLOD2 Proteins).
The present study indicates that GRP78 is increased in BALF in cigarette smokers; that HAEC secrete GRP78; and that GRP78 secretion by HAEC is augmented by cigarette smoke particulates. Enhanced secretion of GRP78 by lung cells makes it a potential biomarker of cigarette smoke-induced lung injury.
P4HB (show P4HB Proteins) promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition.
analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma
This paper reports the localization of both GRP78 and HSP60 (show HSPD1 Proteins) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (show HSPD1 Proteins) in the sperm midpiece.
BiP is a master regulator of endoplasmic reticulum function, and its cleavage by subtilase cytotoxin represents a previously unknown trigger for cell death
Over-expression of GRP78 enhances replication of Porcine Circovirus 2.
candidate genes that modulate Hspa5 expression in the retina, were examined.
These results indicate that GRP78, but not nutritional status, is a potent up-regulator of hepatic PTC (show PTCH1 Proteins)-mRNA levels during induction of ER stress in vivo.
Data suggest that activation of GRP78/Ire1 (show ERN1 Proteins)/Xbp1 (show XBP1 Proteins) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Upregulating HSF1 (show HSF1 Proteins) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (show DDIT3 Proteins) and increasing HSP70 (show HSP70 Proteins) a5 (BiP/GRP78). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 (show HSF1 Proteins) being one likely key player in both systems.
These results demonstrate a key role for GRP78 in alveolar epithelial cell survival.
These results indicate that GRP78, an endoplasmic reticulum chaperon of the HSP70 (show HSP70 Proteins) family, is a novel host factor involved at multiple steps of the Japanese encephalitis virus life cycle and could be a potential therapeutic target.
Genetic or pharmacologic inhibition of the HSPA5-GPX4 pathway enhanced gemcitabine sensitivity by disinhibiting ferroptosis in vitro and in both subcutaneous and orthotopic animal models of PDAC.
The data presented indicate that the unfolded protein response is activated in fibrotic lung tissue and strongly localized to macrophages. GRP78- and CHOP (show DDIT3 Proteins)-mediated macrophage apoptosis was found to protect against bleomycin-induced fibrosis.
Endoplasmic reticulum stress gene GRP78 is involved in signaling pathway during hepatitis B virus-mediated hepatocarcinogenesis.
Phosphatidylinositol deficient zebrafish have elevated hspa5 expression in the liver and hepatic lipid accumulation due to endoplasmic reticulum stress response.
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.
78 kDa glucose-regulated protein
, heat shock 70 kDa protein 5
, Protein 1603
, 78 kDa glucose-regulated protein homolog
, luminal-binding protein
, glucose-regulated protein 78
, glucose-regulated protein 78kDa
, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
, GRP 78
, heavy-chain binding protein BiP
, immunoglobulin heavy chain-binding protein
, endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
, glucose-regulated protein, 78kDa
, XAP-1 antigen
, glucose regulated protein, 78 kDa
, heat shock 70kD protein 5 (glucose-regulated protein, 78kD)
, heat shock 70kD protein 5
, heat shock 70kDa protein 5 (glucose-regulated protein)
, steroidogenesis-activator polypeptide