about
Protein folding and quality control in the ERModulation of the unfolded protein response by the human hepatitis B virusOrchestration of secretory protein folding by ER chaperonesCorresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulationsParalog-selective Hsp90 inhibitors define tumor-specific regulation of HER2Co- and Post-Translational Protein Folding in the ERMapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90Radicol, a Novel Trinorguaiane-Type Sesquiterpene, Induces Temozolomide-Resistant Glioma Cell Apoptosis via ER Stress and Akt/mTOR Pathway Blockade.Fanconi anemia proteins and their interacting partners: a molecular puzzleDifferential requirement of GRP94 and GRP78 in mammary gland development.Mitochondrial Hsp90s suppress calcium-mediated stress signals propagating from mitochondria to the ER in cancer cellsThe endoplasmic reticulum chaperone protein GRP94 is required for maintaining hematopoietic stem cell interactions with the adult bone marrow niche.Identification and characterization of novel ER-based hsp90 gene in the red flour beetle, Tribolium castaneum.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.Liver-specific knockout of GRP94 in mice disrupts cell adhesion, activates liver progenitor cells, and accelerates liver tumorigenesis.Targeted deletion of ER chaperone GRP94 in the liver results in injury, repopulation of GRP94-positive hepatocytes, and spontaneous hepatocellular carcinoma development in aged miceParenteral nutrition-associated liver injury and increased GRP94 expression prevented by ω-3 fish oil-based lipid emulsion supplementation.Exploiting the mitochondrial unfolded protein response for cancer therapy in mice and human cellsIncreased expression of Gp96 by HBx-induced NF-κB activation feedback enhances hepatitis B virus productionOverexpression of GmHsp90s, a heat shock protein 90 (Hsp90) gene family cloning from soybean, decrease damage of abiotic stresses in Arabidopsis thaliana.Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopmentDeletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production.Glucose-regulated protein 94 triage of mutant myocilin through endoplasmic reticulum-associated degradation subverts a more efficient autophagic clearance mechanism.Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis.Depletion of the ER chaperone ENPL-1 sensitizes C. elegans to the anticancer drug cisplatin.α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasisHsp90 regulation of mitochondrial protein folding: from organelle integrity to cellular homeostasisThe mammalian endoplasmic reticulum-associated degradation systemGlucosidase II β-subunit, a novel substrate for caspase-3-like activity in rice, plays as a molecular switch between autophagy and programmed cell deathStructural insights into complexes of glucose-regulated Protein94 (Grp94) with human immunoglobulin G. relevance for Grp94-IgG complexes that form in vivo in pathological conditions.Modelling the effect of GRP78 on anti-oestrogen sensitivity and resistance in breast cancer.A novel benzofuran derivative, ACDB, induces apoptosis of human chondrosarcoma cells through mitochondrial dysfunction and endoplasmic reticulum stress.The effects of myocilin expression on functionally relevant trabecular meshwork genes: a mini-review.TRAP-1, the mitochondrial Hsp90.The functional role of stress proteins in ER stress mediated cell death.Molecular dynamics simulations of hsp90 with an eye to inhibitor design.Heat shock proteins in multiple myelomaEndoplasmic reticulum proteins quality control and the unfolded protein response: the regulative mechanism of organisms against stress injuries.The evolving paradigm of cell-nonautonomous UPR-based regulation of immunity by cancer cells.Comparative RNA-sequencing analysis of ER-based HSP90 functions and signal pathways in Tribolium castaneum.
P2860
Q26823157-F0E79886-6D0C-471B-AE6A-A00592159C1EQ26999215-96C236B0-596D-4C12-87DB-064307493157Q27013551-88E08F79-0E7E-4CCD-8861-BA8E4382C024Q27331720-FF9B29ED-19A9-4F04-80D5-045898EE95B8Q27679845-8D17E047-836C-49B7-A436-3CE9A6D606DAQ28078736-A7667AA5-DE8F-4D0A-A2AA-9EBA56152E40Q28468412-014DEBC2-EAF0-433F-8F7D-AB94D497053AQ32181359-F175AA30-2B62-4319-A691-19B152867998Q33353826-832CDF3A-9504-44C7-96EC-DCF90739134CQ33788940-BA2727BA-B3C8-4A49-8401-A16D18F62C00Q33804537-2BF6AE73-6F61-4FAE-8B39-46FCB5BCADA4Q33925176-07D7DC3F-1BD7-4506-AADB-C3588D1CE97AQ34099871-FD60F9D2-6060-4835-ADD5-9E88FDE5BA24Q34146759-03C30644-5115-4FC2-85EE-4E893CE30DA0Q34426580-C4F4C243-1F19-4A5E-826F-A724E7B7AB94Q34529312-914D7302-9B0C-4C73-88B4-7B6058654B05Q34631697-174E5E5C-75D8-44EF-9CBB-4D53DE105F8DQ34755334-326F515B-2A4D-4C05-9DF3-547B5DD54410Q34775798-6A4546FD-8DE2-4D1C-BFB9-469BC8B8F562Q34921307-DC867293-33B4-46EA-A7E1-F724B9090050Q35077605-8D738A8E-C5E4-4E6D-8D26-E56F8711AB10Q36183694-CE41C3F4-F2F0-465D-80BB-9BA744D106A0Q36418920-6420FF2B-4254-47F0-8699-0708AC0726DEQ36497621-2E252A90-6BBD-4470-9F23-FA4D6AEEAA04Q36896039-DC06C555-0D77-49A3-8787-DEB95E39DDD6Q36947798-E04C32D2-A77C-4417-BAE6-B5A6781CA64AQ37056146-C94FF977-9CD0-4CF5-8442-E346E411D043Q37122324-D2B75484-1A00-4DE6-AA67-835D71E7BF24Q37188852-F3D308E9-4592-4566-91EA-21775041CA47Q37525176-992F2A94-EABE-4C56-83B3-025A6DA695F7Q37561430-38ADD38A-3E78-4453-8EBA-9A80CF7C8D25Q37696338-09F0FA9E-889F-4186-8202-C862506A4CBBQ37710660-FA4649B0-E231-42C3-81CF-17E0A754E945Q37924023-F85FB267-C21A-4F6D-BBE6-CC254CA2496AQ37973684-9E3C5C08-F3EB-41E5-B580-FCB94EB126FBQ38166531-DDB79EBC-E8C5-4C8D-B881-1114BC48627DQ38199919-4E133A50-B981-4FC0-BBD6-5DD341F669D2Q38296280-16BFCAC3-1110-4B58-801B-CD1CD694EE2AQ38429699-51F74462-0B80-46EF-AB20-6932C3A50C7FQ38431608-47FF1668-85AA-4526-AA56-CC83F47420EC
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 16 March 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
GRP94 in ER quality control and stress responses
@en
GRP94 in ER quality control and stress responses.
@nl
type
label
GRP94 in ER quality control and stress responses
@en
GRP94 in ER quality control and stress responses.
@nl
prefLabel
GRP94 in ER quality control and stress responses
@en
GRP94 in ER quality control and stress responses.
@nl
P2093
P2860
P1476
GRP94 in ER quality control and stress responses
@en
P2093
Davide Eletto
Devin Dersh
Yair Argon
P2860
P304
P356
10.1016/J.SEMCDB.2010.03.004
P577
2010-03-16T00:00:00Z