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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
Show all 10 Pubmed References
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.
Endoplasmic reticulum resident chaperone GRP78, mitochondrial protein (show COX6B2 Proteins) Prohibitin (show PHB Proteins) and heterogeneous nuclear ribonucleoprotein (show PCBP2 Proteins) hnRNPC (show HNRNPC Proteins) (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection.
We revealed that a small amount of GRP78 effectively inhibited fibrillation of Abeta (show APP Proteins) fragments. Intriguingly, the fibrillation inhibition by GRP78 was confirmed in the absence of ATP, suggesting GRP78 exhibited ATP-independent interaction with Abeta (show APP Proteins) fragments.
Testosterone exposure could deregulate glucose availability by reducing GRP78 protein levels in endometrial stromal cells
Low GRP78 expression is associated with cancer.
These results highlight a functional role for CRIPTO (show TDGF1 Proteins) and GRP78 in prostate cancer metastasis and suggest that targeting CRIPTO (show TDGF1 Proteins)/GRP78 signaling may have significant therapeutic potential.
High GRP78 expression is associated with resistance to sorafeinib in liver cancer.
Results show that GRP78 was up-regulated in human prostate cancer and inversely correlated with PCA3 expression.
Inhibition of 17beta-HSD (show HSD17B3 Proteins) 7 modulates breast cancer protein profile and enhances apoptosis by down-regulating GRP78.
GALNT6 (show GALNT6 Proteins)-induced O-glycosylation is critical for the stability, subcellular localization, and anti-apoptotic function of GRP78 protein in cancer cells. We also suggest that GRP78 might enhance the activity of GALNT6 (show GALNT6 Proteins) in carcinogenesis through driving Golgi-to-ER relocation of GALNT6 (show GALNT6 Proteins).
BiP (show GDF10 Proteins) binds to the unfolded state of MJ0366 and prevents its refolding, and that this effect is dependent on both the type and concentration of nucleotides.
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.
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.
We show that chronic VPA treatment did not modify the ATXN3 (show ATXN3 Proteins) inclusion load and astrogliosis in affected brain regions However, VPA chronic treatment was able to increase GRP78 protein levels at 30 weeks of age, one of its known neuroprotective effects
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