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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.
Upon IgM expression, its levels temporarily eclipse those of the endoplasmic reticulum chaperone BiP (zeige GDF10 Proteine), leading to acute, full-geared unfolded protein response activation. Once BiP (zeige GDF10 Proteine) is in excess (zeige RCC1 Proteine) again, the unfolded protein response transitions to chronic, submaximal activation, indicating that the unfolded protein response senses endoplasmic reticulum stress in a ratiometric fashion.
GRP78 binds to and acts in concert with a glycosylphosphatidylinositol-anchored protein, CD109 (zeige CD109 Proteine), in blocking TGF-beta (zeige TGFB1 Proteine) signaling by promoting the routing of the TGF-beta (zeige TGFB1 Proteine) receptor to the caveolae, thereby disrupting its binding to and activation of Smad2 (zeige SMAD2 Proteine).
this study demonstrates the reaction of placental GRP78 with sera from women with multiple sclerosis
This meta-analysis shows that BiP (zeige GDF10 Proteine) or anti-BiP (zeige GDF10 Proteine) antibodies have a moderate accuracy for the diagnosis of rheumatoid arthritis with a moderate sensitivity and high specificity. It can be an efficient supplement to the existing diagnostic method. [Meta-Analysis]
the expression of three cytokines for the pathogenesis of osteoarthritis (OA). which include IL-1beta (zeige IL1B Proteine), MMP14 (zeige MMP14 Proteine) and GRP78 was decreased by the various concentrations of icariin. These preliminary results imply that icariin might be an effective compound for the treatment of OA disease.
In a retrospective cervical cancer cohort, high GRP78 expression was correlated with poor survival. miR (zeige MLXIP Proteine)-181a suppressed cervical cancer development via downregulating GRP78.
We revealed that DAL-1 (zeige EPB41L3 Proteine) was downregulated while HSPA5 was upregulated in NSCLC and found the protein of DAL-1 (zeige EPB41L3 Proteine) and HSPA5 co-localized in the cytoplasm and nucleus. We demonstrated that DAL-1 (zeige EPB41L3 Proteine) can suppress the expression of HSPA5 on mRNA and protein levels, and decrease EMT (zeige ITK Proteine), migration, invasion and proliferation abilities by down-regulating HSPA5
We found that inhibiting the function of surface GRP78 suppressed cancer cell survival and growth proving that the surface-expressed GRP78 is a vital receptor involved in the proliferation of high-grade glioma.
BiP/GRP78 is significantly associated with tumor aggressiveness and progression. The increased expression of BiP/GRP78 was identified as an independent factor for predicting poor OS in patients with early stage of disease.
GRP78 overexpression decreased advanced glycation end product levels and rescued the cells from Ribosome-induced cytotoxicity.
This paper reports the localization of both GRP78 and HSP60 (zeige HSPD1 Proteine) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (zeige HSPD1 Proteine) 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.
prolonged endoplasmic reticulum stress promotes apoptosis via a p53 (zeige TP53 Proteine)-dependent inhibition of BiP expression
analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma
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 (zeige PTCH1 Proteine)-mRNA levels during induction of ER stress in vivo.
Data suggest that activation of GRP78/Ire1 (zeige ERN1 Proteine)/Xbp1 (zeige XBP1 Proteine) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Upregulating HSF1 (zeige HSF1 Proteine) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (zeige DDIT3 Proteine) and increasing HSP70 (zeige HSP70 Proteine) a5 (BiP/GRP78). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 (zeige HSF1 Proteine) 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 (zeige HSP70 Proteine) 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 (zeige DDIT3 Proteine)-mediated macrophage apoptosis was found to protect against bleomycin-induced fibrosis.
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