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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.
Cancer-associated fibroblasts induced GRP78 expression in A549 and SPCA-1 (show ATP2C1 Proteins) cells to facilitate Non-Small Cell Lung Cancer cell migration and invasion
results suggest that the cooperative effects of radiotherapy and cetuximab could be further improved by inhibiting GRP78 in non-responsive oropharyngeal carcinoma patients
Study reports that the endoplasmic reticulum luminal co-chaperone ERdj4/DNAJB9 (show DNAJB9 Proteins) is a selective IRE1 (show ERN1 Proteins) repressor that promotes a complex between the luminal Hsp70 (show HSP70 Proteins) BiP (show GDF10 Proteins) and the luminal stress-sensing domain of IRE1alpha (show ERN1 Proteins).
GRP78 role in the resistance to cisplatin in the nasopharyngeal carcinoma cells.
High expression of GRP78 is associated with nonalcoholic steatohepatitis.
Data show that cancer-associated fibroblasts (CAFs (show TBX1 Proteins))-derived hepatocyte growth factor (HGF (show HGF Proteins)) or recombinant HGF (show HGF Proteins) activated c-Met/phosphoinositide 3-kinase (PI3K (show PIK3CA Proteins))/Akt (show AKT1 Proteins) and glucose-regulated protein 78 (GRP78) signalling pathways in ovarian cancer cells.
HSPA5/BIP has roles in endoplasmic reticulum stress, autophagy and apoptosis; inhibitors of HSPA5 could be useful in cancer treatment
Immunohistochemical analysis showed that STAT3 (show STAT3 Proteins), GRP78 and BAX (show BAX Proteins) protein levels in the combination group were significantly higher than those in STAT3 (show STAT3 Proteins) group and CDDP group (P<0.05). Exogenous STAT3 (show STAT3 Proteins) and CDDP may synergistically inhibit the xenograft tumour growth through up-regulation of BAX (show BAX Proteins) protein via GRP78.
GRP78 inhibition enhances ATF4 (show ATF4 Proteins)-induced cell death by the deubiquitination and stabilization of CHOP (show DDIT3 Proteins) in human osteosarcoma cells.
the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD (show MVD Proteins) against PDI (show PADI1 Proteins)-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 (show ADAM17 Proteins) inhibition.
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.
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.
data show that Med inhibits ER stress-induced apoptosis and promotes osteoblast cell survival by targeting GRP78.
These results suggested the important roles of endoplasmic reticulum-related chaperons, Bip and SIL1 (show SIL1 Proteins), in Alzheimer's disease-like tau hyperphosphorylation.
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