The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation
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A hippocampal insulin-growth factor 2 pathway regulates the extinction of fear memoriesGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingParalog-selective Hsp90 inhibitors define tumor-specific regulation of HER2Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94Co- and Post-Translational Protein Folding in the ERRole of IGF-I signaling in muscle bone interactionsInduction of premature senescence by hsp90 inhibition in small cell lung cancerExploring the Functional Complementation between Grp94 and Hsp90NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiationEndoplasmic Reticulum-resident Heat Shock Protein 90 (HSP90) Isoform Glucose-regulated Protein 94 (GRP94) Regulates Cell Polarity and Cancer Cell Migration by Affecting Intracellular Transport.Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control.The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?Myofiber stress-response in myositis: parallel investigations on patients and experimental animal models of muscle regeneration and systemic inflammation.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.Targeted deletion of ER chaperone GRP94 in the liver results in injury, repopulation of GRP94-positive hepatocytes, and spontaneous hepatocellular carcinoma development in aged miceIncreased expression of Gp96 by HBx-induced NF-κB activation feedback enhances hepatitis B virus productionProtein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production.A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein.Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response.A Human Variant of Glucose-Regulated Protein 94 That Inefficiently Supports IGF Production.An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells.GRP94 in ER quality control and stress responsesGenerating new neurons to circumvent your fears: the role of IGF signaling.Protein folding in the endoplasmic reticulumCell membrane gp96 facilitates HER2 dimerization and serves as a novel target in breast cancer.Development of radamide analogs as Grp94 inhibitorsImmune chaperone gp96 drives the contributions of macrophages to inflammatory colon tumorigenesis.Development of a Grp94 inhibitor.Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factorsStructural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.Characterization of the Grp94/OS-9 chaperone-lectin complex.Sparing of muscle mass and function by passive loading in an experimental intensive care unit model.GRP94 is an Essential Regulator of Pancreatic β Cell Development, Mass and Function in Male Mice.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
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The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 21 January 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The chaperone activity of GRP9 ...... response to serum deprivation
@en
The chaperone activity of GRP9 ...... response to serum deprivation.
@nl
type
label
The chaperone activity of GRP9 ...... response to serum deprivation
@en
The chaperone activity of GRP9 ...... response to serum deprivation.
@nl
prefLabel
The chaperone activity of GRP9 ...... response to serum deprivation
@en
The chaperone activity of GRP9 ...... response to serum deprivation.
@nl
P2093
P2860
P356
P1476
The chaperone activity of GRP9 ...... response to serum deprivation
@en
P2093
Noreen T Ahmed
Olga Ostrovsky
Yair Argon
P2860
P304
P356
10.1091/MBC.E08-04-0346
P577
2009-01-21T00:00:00Z