scholarly article | Q13442814 |
P2093 | author name string | Yair Argon | |
Olga Ostrovsky | |||
Noreen T Ahmed | |||
P2860 | cites work | The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis | Q22010566 |
GRP94 reduces cell death in SH-SY5Y cells perturbated calcium homeostasis | Q24296432 | ||
OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD | Q24312778 | ||
Up-regulation of 94-kDa glucose-regulated protein by hypoxia-inducible factor-1 in human endothelial cells in response to hypoxia | Q24336918 | ||
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome | Q24533430 | ||
Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages | Q24609722 | ||
Colocalization of chaperone Cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for Cpn60 in insulin processing | Q28564975 | ||
Role of insulin-like growth factors in embryonic and postnatal growth | Q29620034 | ||
GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion | Q30480141 | ||
SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins | Q33336944 | ||
GRP94, an ER chaperone with protein and peptide binding properties | Q33794238 | ||
Role of insulin-like growth factors and their binding proteins in growth control and carcinogenesis | Q33853206 | ||
Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability | Q34093483 | ||
The insulin-like growth factor system and cancer | Q34200058 | ||
Redundancy of autocrine loops in human rhabdomyosarcoma cells: induction of differentiation by suramin | Q36081413 | ||
The peptide-binding activity of GRP94 is regulated by calcium. | Q40148862 | ||
The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications | Q40647911 | ||
In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER. | Q40806034 | ||
IGF-II ameliorates the dystrophic phenotype and coordinately down-regulates programmed cell death | Q40834560 | ||
Post-translational processing of the insulin-like growth factor-2 precursor. Analysis of O-glycosylation and endoproteolysis | Q41026364 | ||
Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells | Q41092630 | ||
Pattern of the insulin-like growth factor II gene expression during early mouse embryogenesis | Q41173042 | ||
Regulation of the glucose-regulated protein genes by beta-mercaptoethanol requires de novo protein synthesis and correlates with inhibition of protein glycosylation | Q41467340 | ||
Specific, temporally regulated expression of the insulin-like growth factor II gene during muscle cell differentiation | Q41535411 | ||
The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin | Q42826312 | ||
GRP94 (94 kDa glucose-regulated protein) suppresses ischemic neuronal cell death against ischemia/reperfusion injury | Q44553319 | ||
All-trans-retinoic acid inhibits the growth of human rhabdomyosarcoma cell lines | Q44901243 | ||
Suppression of stress protein GRP78 induction in tumor B/C10ME eliminates resistance to cell mediated cytotoxicity | Q46172318 | ||
Transcriptional regulation and biological significance of the insulin like growth factor II gene. | Q52180058 | ||
Overexpression of insulin-like growth factor-II in mouse embryonic stem cells promotes myogenic differentiation. | Q53928256 | ||
Suramin disrupts insulin-like growth factor-II (IGF-II) mediated autocrine growth in human SH-SY5Y neuroblastoma cells | Q58843216 | ||
Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum | Q59060210 | ||
Mouse Lymphoma Cells Destined to Undergo Apoptosis in Response to Thapsigargin Treatment Fail to Generate a Calcium-mediatedgrp78/grp94Stress Response | Q61853658 | ||
Transcriptional regulation of two genes specifically induced by glucose starvation in a hamster mutant fibroblast cell line | Q67246516 | ||
Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin | Q68189236 | ||
Depletion of intracellular calcium stores by calcium ionophore A23187 induces the genes for glucose-regulated proteins in hamster fibroblasts | Q70355655 | ||
Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions | Q74456160 | ||
Radicicol-sensitive peptide binding to the N-terminal portion of GRP94 | Q74633065 | ||
Antibodies directed against the E region of pro-insulin-like growth factor-II used to evaluate non-islet cell tumor-induced hypoglycemia | Q77221663 | ||
Quantitative proteomics analysis of the secretory pathway | Q79438532 | ||
P433 | issue | 6 | |
P921 | main subject | molecular chaperones | Q422496 |
preproinsulin | Q7240673 | ||
P304 | page(s) | 1855-1864 | |
P577 | publication date | 2009-01-21 | |
P1433 | published in | Molecular Biology of the Cell | Q2338259 |
P1476 | title | The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation | |
P478 | volume | 20 |
Q36215027 | A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein |
Q36911625 | A Human Variant of Glucose-Regulated Protein 94 That Inefficiently Supports IGF Production |
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Q37261639 | An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells |
Q38924681 | Cell membrane gp96 facilitates HER2 dimerization and serves as a novel target in breast cancer |
Q42048334 | Characterization of the Grp94/OS-9 chaperone-lectin complex |
Q28075479 | Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94 |
Q28078736 | Co- and Post-Translational Protein Folding in the ER |
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Q39340802 | Development of a Grp94 inhibitor |
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Q47260586 | GRP94 is an Essential Regulator of Pancreatic β Cell Development, Mass and Function in Male Mice |
Q26860153 | GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum |
Q38094638 | Generating new neurons to circumvent your fears: the role of IGF signaling. |
Q39774482 | Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factors |
Q33695850 | Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control |
Q39014670 | Immune chaperone gp96 drives the contributions of macrophages to inflammatory colon tumorigenesis |
Q34775798 | Increased expression of Gp96 by HBx-induced NF-κB activation feedback enhances hepatitis B virus production |
Q39694714 | Increased mitochondrial superoxide dismutase expression and lowered production of reactive oxygen species during rotavirus infection |
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Q28594645 | NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation |
Q27679845 | Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2 |
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Q39323829 | Proteome analysis of tunicamycin-induced ER stress |
Q34146759 | Proteomic plasma membrane profiling reveals an essential role for gp96 in the cell surface expression of LDLR family members, including the LDL receptor and LRP6. |
Q28082188 | Role of IGF-I signaling in muscle bone interactions |
Q44539075 | Sparing of muscle mass and function by passive loading in an experimental intensive care unit model |
Q41705197 | Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site. |
Q35899122 | Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94 |
Q34529312 | Targeted deletion of ER chaperone GRP94 in the liver results in injury, repopulation of GRP94-positive hepatocytes, and spontaneous hepatocellular carcinoma development in aged mice |
Q27326154 | Targeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signaling |
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